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Conserved domains on  [gi|42741659|ref|NP_000918|]
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ATP-dependent translocase ABCB1 isoform 2 [Homo sapiens]

Protein Classification

ABC transporter B family protein( domain architecture ID 1000096)

ABC transporter B (ABCB) family protein, similar to human phosphatidylcholine translocator ABCB4 that functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi of hepatocytes

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PTZ00265 super family cl36537
multidrug resistance protein (mdr1); Provisional
53-1267 0e+00

multidrug resistance protein (mdr1); Provisional


The actual alignment was detected with superfamily member PTZ00265:

Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 613.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    53 VGTLAAIIHGAGLPLMMLVFGEmtdifanagnledLMSNitnrsdindtgffMNLEEDMTRYAYYYSGIGAGVLVAAYIq 132
Cdd:PTZ00265   64 VSFVCATISGGTLPFFVSVFGV-------------IMKN-------------MNLGENVNDIIFSLVLIGIFQFILSFI- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   133 vSFWCL--AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:PTZ00265  117 -SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFK 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:PTZ00265  196 NARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   291 KAITANISIGAAFLLIYASYALAFWYGTTLVLS--------GEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAA 362
Cdd:PTZ00265  276 ANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   363 YEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 442
Cdd:PTZ00265  356 NSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   443 LYDPTEGMVSV-DGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG------------------------------ 491
Cdd:PTZ00265  434 LYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrns 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   492 ------------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:PTZ00265  514 crakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA 593
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   545 LVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI------------------------ 598
Cdd:PTZ00265  594 IIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkd 673
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   599 -----------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQTAGNEVELENAAD---ESKSEI--- 648
Cdd:PTZ00265  674 nkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNNDNDkdsDMKSSAykd 753
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   649 -----DALEMSSN--DSRSSLIRKRSTRRSVRGSQAQDR--KLSTKEALDESIPPV-SFWRIMKLNLTEWPYFVVGVFCA 718
Cdd:PTZ00265  754 sergyDPDEMNGNskHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALS 833
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   719 II-NGGLQPAFAIIFSKIIGVFTRIDDPETkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSML 797
Cdd:PTZ00265  834 ILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL 910
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   798 RQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMK 877
Cdd:PTZ00265  911 YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRAR 990
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   878 MLSGQALkDKKELEGSGKI----------------ATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGIT 941
Cdd:PTZ00265  991 LTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSML 1069
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   942 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSY 1021
Cdd:PTZ00265 1070 WGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1022 STEGLM---PNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------- 1088
Cdd:PTZ00265 1150 DNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfk 1229
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1089 --------------------------------------------PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1124
Cdd:PTZ00265 1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PTZ00265 1310 MSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
                        1370      1380      1390      1400      1410      1420      1430
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1205 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1267
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
53-1267 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 613.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    53 VGTLAAIIHGAGLPLMMLVFGEmtdifanagnledLMSNitnrsdindtgffMNLEEDMTRYAYYYSGIGAGVLVAAYIq 132
Cdd:PTZ00265   64 VSFVCATISGGTLPFFVSVFGV-------------IMKN-------------MNLGENVNDIIFSLVLIGIFQFILSFI- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   133 vSFWCL--AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:PTZ00265  117 -SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFK 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:PTZ00265  196 NARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   291 KAITANISIGAAFLLIYASYALAFWYGTTLVLS--------GEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAA 362
Cdd:PTZ00265  276 ANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   363 YEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 442
Cdd:PTZ00265  356 NSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   443 LYDPTEGMVSV-DGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG------------------------------ 491
Cdd:PTZ00265  434 LYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrns 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   492 ------------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:PTZ00265  514 crakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA 593
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   545 LVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI------------------------ 598
Cdd:PTZ00265  594 IIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkd 673
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   599 -----------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQTAGNEVELENAAD---ESKSEI--- 648
Cdd:PTZ00265  674 nkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNNDNDkdsDMKSSAykd 753
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   649 -----DALEMSSN--DSRSSLIRKRSTRRSVRGSQAQDR--KLSTKEALDESIPPV-SFWRIMKLNLTEWPYFVVGVFCA 718
Cdd:PTZ00265  754 sergyDPDEMNGNskHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALS 833
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   719 II-NGGLQPAFAIIFSKIIGVFTRIDDPETkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSML 797
Cdd:PTZ00265  834 ILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL 910
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   798 RQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMK 877
Cdd:PTZ00265  911 YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRAR 990
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   878 MLSGQALkDKKELEGSGKI----------------ATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGIT 941
Cdd:PTZ00265  991 LTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSML 1069
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   942 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSY 1021
Cdd:PTZ00265 1070 WGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1022 STEGLM---PNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------- 1088
Cdd:PTZ00265 1150 DNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfk 1229
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1089 --------------------------------------------PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1124
Cdd:PTZ00265 1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PTZ00265 1310 MSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
                        1370      1380      1390      1400      1410      1420      1430
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1205 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1267
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
48-632 0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 548.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   48 KLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMsnitnrsdindtgffmnleedmtRYAYYYSGIGAGVLV 127
Cdd:COG1132   20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALL-----------------------LLLLLLLGLALLRAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  128 AAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVG 207
Cdd:COG1132   77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  208 FTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRI 287
Cdd:COG1132  157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  288 GIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFK 367
Cdd:COG1132  237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  368 IIDNKPSIDSySKSGHKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT 447
Cdd:COG1132  317 LLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  448 EGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGER 527
Cdd:COG1132  394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  528 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIV 607
Cdd:COG1132  474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
                        570       580
                 ....*....|....*....|....*
gi 42741659  608 EKGNHDELMKEKGIYFKLVTMQTAG 632
Cdd:COG1132  554 EQGTHEELLARGGLYARLYRLQFGE 578
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
51-365 3.17e-163

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 489.09  E-value: 3.17e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   51 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEdlmSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAY 130
Cdd:cd18558    1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTN---ITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  131 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:cd18558   78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:cd18558  158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  291 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 365
Cdd:cd18558  238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
36-626 1.87e-140

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 444.16  E-value: 1.87e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     36 VFSMFRYSNwLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNItnrsdindtgFFMNLeedMTRYA 115
Cdd:TIGR00958  149 LFRLLGLSG-RDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAI----------FFMCL---LSIAS 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    116 YYYSGIGAGVLVAAYiqvsfwclaaGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQ 195
Cdd:TIGR00958  215 SVSAGLRGGSFNYTM----------ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLR 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    196 SMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 275
Cdd:TIGR00958  285 NLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEAS 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    276 RYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLtvffSVLIGAFSVGQASPSIEAF 355
Cdd:TIGR00958  365 RFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYV 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    356 AN----ARGAAYEIFKIIDNKPSIDSysKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGC 431
Cdd:TIGR00958  441 YSgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGS 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    432 GKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 511
Cdd:TIGR00958  519 GKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHD 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    512 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQValDKARKGRTTIVIAHRLST 591
Cdd:TIGR00958  599 FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLST 676
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 42741659    592 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 626
Cdd:TIGR00958  677 VERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
51-343 5.44e-84

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 275.29  E-value: 5.44e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     51 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFanagnledlmsnitnrSDINDTGFFmnleeDMTRYAYYYSGIGAGVLVAAY 130
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVL----------------LPDGDPETQ-----ALNVYSLALLLLGLAQFILSF 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    131 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:pfam00664   60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:pfam00664  140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659    291 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQ--VLTVFFSVLIGAF 343
Cdd:pfam00664  220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1048-1246 1.29e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 91.14  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlrahlgiVSQEPILFDCSI 1127
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSLPLTV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1128 AENIAYGDNSRVVSQEEIVRAAKEANIHAF----IESLPNKystKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:NF040873   75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALervgLADLAGR---QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 42741659  1204 SALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1246
Cdd:NF040873  148 TGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
400-596 1.65e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.67  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   400 SYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirTINVRFLREIIGVVSQEPVl 479
Cdd:NF040873    1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   480 fatTIAENIRYGR-------ENVTMDEiEKAVKEAnaydfIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 552
Cdd:NF040873   73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 42741659   553 LLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTVRNAD 596
Cdd:NF040873  142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
GguA NF040905
sugar ABC transporter ATP-binding protein;
392-608 1.30e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.46  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQ-----DIRTi 461
Cdd:NF040905    2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   462 nvrflREIIGVV--SQE----PVLfatTIAENIRYGRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAqlsg 533
Cdd:NF040905   75 -----SEALGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV---- 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   534 GQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVE 608
Cdd:NF040905  143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
GguA NF040905
sugar ABC transporter ATP-binding protein;
1046-1253 1.10e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.76  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGKVLLDGKEIKRLNvqwLRA--HLGIV--SQ 1118
Cdd:NF040905   10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1119 E----PILfdcSIAENIAYGdNSR----VVSQEEIVRAAKEANIHAFIESLPNkysTKVGDKGTqlsgGQKQRIAIARAL 1190
Cdd:NF040905   86 ElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKAL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1191 VRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKE 1253
Cdd:NF040905  155 SKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
419-611 1.23e-13

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 69.71  E-value: 1.23e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     419 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPTEGMVSVDGQDIRTINVRFLREIIgvvsqepvlfattiaenirygrenvtm 497
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     498 deiekavkeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALD--- 574
Cdd:smart00382   54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 42741659     575 ----KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 611
Cdd:smart00382  108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
427-562 6.03e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.98  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   427 GNSGCGKSTTVQLMQRLYDPTEGMV-----SVDGQDIRTinvrflREIIGVVSQEPVLfattiaenirYG----REN--- 494
Cdd:NF033858  299 GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT------RRRVGYMSQAFSL----------YGeltvRQNlel 362
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   495 ------VTMDEIEKAVKEanaydfimkLPHKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:NF033858  363 harlfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
406-620 1.00e-05

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVqLMQRLYDPTEGMvsvdgQDIR----TINVRFLREIIGVvsQEPVLFA 481
Cdd:NF000106   25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRf*twCANRRALRRTIG*--HRPVR*G 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENiryGRENVTM--DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 559
Cdd:NF000106   97 RRESFS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   560 ALD--TESEAVVQVAlDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 620
Cdd:NF000106  174 GLDprTRNEVWDEVR-SMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
GguA NF040905
sugar ABC transporter ATP-binding protein;
1034-1230 1.61e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1034 NVTFGEVVF-------NYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-LAGKVLLDGKEIKRL 1104
Cdd:NF040905  250 TPKIGEVVFevknwtvYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVS 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1105 NVQWL-----------RAHLGIVSQEPILFDCSIA--ENIAygdNSRVVSQEEIVRAAKEanihaFIESLPNKYSTkVGD 1171
Cdd:NF040905  330 TVSDAidaglayvtedRKGYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKMNIKTPS-VFQ 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1172 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1230
Cdd:NF040905  401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1170-1265 2.92e-04

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 44.73  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1170 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQ 1247
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
                          90
                  ....*....|....*...
gi 42741659  1248 NGRVKEHGTHQQLLAQKG 1265
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
53-1267 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 613.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    53 VGTLAAIIHGAGLPLMMLVFGEmtdifanagnledLMSNitnrsdindtgffMNLEEDMTRYAYYYSGIGAGVLVAAYIq 132
Cdd:PTZ00265   64 VSFVCATISGGTLPFFVSVFGV-------------IMKN-------------MNLGENVNDIIFSLVLIGIFQFILSFI- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   133 vSFWCL--AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:PTZ00265  117 -SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFK 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:PTZ00265  196 NARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   291 KAITANISIGAAFLLIYASYALAFWYGTTLVLS--------GEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAA 362
Cdd:PTZ00265  276 ANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   363 YEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 442
Cdd:PTZ00265  356 NSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   443 LYDPTEGMVSV-DGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG------------------------------ 491
Cdd:PTZ00265  434 LYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrns 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   492 ------------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:PTZ00265  514 crakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA 593
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   545 LVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI------------------------ 598
Cdd:PTZ00265  594 IIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkd 673
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   599 -----------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQTAGNEVELENAAD---ESKSEI--- 648
Cdd:PTZ00265  674 nkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNNDNDkdsDMKSSAykd 753
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   649 -----DALEMSSN--DSRSSLIRKRSTRRSVRGSQAQDR--KLSTKEALDESIPPV-SFWRIMKLNLTEWPYFVVGVFCA 718
Cdd:PTZ00265  754 sergyDPDEMNGNskHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALS 833
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   719 II-NGGLQPAFAIIFSKIIGVFTRIDDPETkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSML 797
Cdd:PTZ00265  834 ILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL 910
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   798 RQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMK 877
Cdd:PTZ00265  911 YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRAR 990
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   878 MLSGQALkDKKELEGSGKI----------------ATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGIT 941
Cdd:PTZ00265  991 LTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSML 1069
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   942 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSY 1021
Cdd:PTZ00265 1070 WGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1022 STEGLM---PNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------- 1088
Cdd:PTZ00265 1150 DNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfk 1229
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1089 --------------------------------------------PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1124
Cdd:PTZ00265 1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PTZ00265 1310 MSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
                        1370      1380      1390      1400      1410      1420      1430
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1205 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1267
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
48-632 0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 548.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   48 KLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMsnitnrsdindtgffmnleedmtRYAYYYSGIGAGVLV 127
Cdd:COG1132   20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALL-----------------------LLLLLLLGLALLRAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  128 AAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVG 207
Cdd:COG1132   77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  208 FTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRI 287
Cdd:COG1132  157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  288 GIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFK 367
Cdd:COG1132  237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  368 IIDNKPSIDSySKSGHKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT 447
Cdd:COG1132  317 LLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  448 EGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGER 527
Cdd:COG1132  394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  528 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIV 607
Cdd:COG1132  474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
                        570       580
                 ....*....|....*....|....*
gi 42741659  608 EKGNHDELMKEKGIYFKLVTMQTAG 632
Cdd:COG1132  554 EQGTHEELLARGGLYARLYRLQFGE 578
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
696-1276 1.99e-167

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 510.48  E-value: 1.99e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  696 SFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETkrqnSNLFSLLFLALGIISFITFFLQGF 775
Cdd:COG1132    8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA----LLLLLLLLLGLALLRALLSYLQRY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  776 TFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGW 855
Cdd:COG1132   84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  856 QLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKA 935
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  936 HIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKT 1015
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1016 PLIDSySTEGLMPNTLEGNVTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVL 1095
Cdd:COG1132  322 PEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1096 LDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQ 1175
Cdd:COG1132  399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1176 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1255
Cdd:COG1132  477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
                        570       580
                 ....*....|....*....|.
gi 42741659 1256 THQQLLAQKGIYFSMVSVQAG 1276
Cdd:COG1132  557 THEELLARGGLYARLYRLQFG 577
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
51-365 3.17e-163

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 489.09  E-value: 3.17e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   51 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEdlmSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAY 130
Cdd:cd18558    1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTN---ITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  131 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:cd18558   78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:cd18558  158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  291 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 365
Cdd:cd18558  238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
393-629 2.38e-153

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 460.08  E-value: 2.38e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  393 EFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 472
Cdd:cd03249    2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  473 VSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 552
Cdd:cd03249   82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  553 LLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:cd03249  162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1035-1274 8.66e-153

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 458.54  E-value: 8.66e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1114
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILFDCSIAENIAYGDNSRvvSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQP 1194
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1274
Cdd:cd03249  159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
121-630 2.81e-145

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 456.99  E-value: 2.81e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  121 IGAGVLVAAYIQVSF-----WCLA-AGRQI-HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMF 193
Cdd:COG2274  198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  194 FQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKE 273
Cdd:COG2274  277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  274 LERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF--SVGQASPS 351
Cdd:COG2274  357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIGL 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  352 IEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPdNIKGNLEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGC 431
Cdd:COG2274  435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGS 512
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  432 GKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 511
Cdd:COG2274  513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  512 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLST 591
Cdd:COG2274  593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 42741659  592 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQT 630
Cdd:COG2274  673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
701-1018 2.23e-143

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 437.27  E-value: 2.23e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  701 MKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQnSNLFSLLFLALGIISFITFFLQGFTFGKA 780
Cdd:cd18578    1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSE-ANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  781 GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLL 860
Cdd:cd18578   80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  861 LLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGI 940
Cdd:cd18578  160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  941 TFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLI 1018
Cdd:cd18578  240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
36-626 1.87e-140

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 444.16  E-value: 1.87e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     36 VFSMFRYSNwLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNItnrsdindtgFFMNLeedMTRYA 115
Cdd:TIGR00958  149 LFRLLGLSG-RDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAI----------FFMCL---LSIAS 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    116 YYYSGIGAGVLVAAYiqvsfwclaaGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQ 195
Cdd:TIGR00958  215 SVSAGLRGGSFNYTM----------ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLR 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    196 SMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 275
Cdd:TIGR00958  285 NLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEAS 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    276 RYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLtvffSVLIGAFSVGQASPSIEAF 355
Cdd:TIGR00958  365 RFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYV 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    356 AN----ARGAAYEIFKIIDNKPSIDSysKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGC 431
Cdd:TIGR00958  441 YSgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGS 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    432 GKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 511
Cdd:TIGR00958  519 GKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHD 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    512 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQValDKARKGRTTIVIAHRLST 591
Cdd:TIGR00958  599 FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLST 676
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 42741659    592 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 626
Cdd:TIGR00958  677 VERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
711-1008 1.14e-135

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 416.68  E-value: 1.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFT----------------RIDDPETKRQNSNLFSLLFLALGIISFITFFLQG 774
Cdd:cd18558    1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTnggmtnitgnssglnsSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  775 FTFGKAGEILTKRLRYMVFRSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYG 854
Cdd:cd18558   81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  855 WQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRK 934
Cdd:cd18558  159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  935 AHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMS-FEDVLLVFSAVVFGAMAVGQVSSFAPdYAKAKISAAHI 1008
Cdd:cd18558  239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
100-629 1.07e-132

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 419.10  E-value: 1.07e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    100 DTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDV 179
Cdd:TIGR02204   46 DHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDT 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    180 SKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLA 259
Cdd:TIGR02204  126 TLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLG 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    260 AIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVL 339
Cdd:TIGR02204  206 AIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAV 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    340 IGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQS 419
Cdd:TIGR02204  286 MVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRP 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    420 GQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDE 499
Cdd:TIGR02204  366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    500 IEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG 579
Cdd:TIGR02204  446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 42741659    580 RTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:TIGR02204  526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
684-1275 1.09e-131

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 420.78  E-value: 1.09e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  684 TKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAIINGGLQ---PAFA-IIFSKIIGvftriddpetkrqNSNLFSLLF 759
Cdd:COG2274  131 TPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLAlatPLFTqVVIDRVLP-------------NQDLSTLWV 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  760 LALGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGAIGSRLA 834
Cdd:COG2274  198 LAIGLLLALLFegllrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLL 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  835 VITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGsgkIATEAIENFRTVVSLT 911
Cdd:COG2274  275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLfqpRLRRLSREESEASAKRQS---LLVETLRGIETIKALG 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  912 QEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFeDVLLVFSAVVFGAMA-VGQ 990
Cdd:COG2274  352 AESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQ 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  991 VSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNtLEGNVTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVG 1070
Cdd:COG2274  431 LIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVG 508
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1071 SSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAK 1150
Cdd:COG2274  509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAAR 586
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1151 EANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1230
Cdd:COG2274  587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 42741659 1231 AHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQA 1275
Cdd:COG2274  667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
51-365 1.54e-130

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 402.62  E-value: 1.54e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   51 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNitnrsdindtgffmnLEEDMTRYAYYYSGIGAGVLVAAY 130
Cdd:cd18577    1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDE---------------FLDDVNKYALYFVYLGIGSFVLSY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  131 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:cd18577   66 IQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIY 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:cd18577  146 SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  291 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 365
Cdd:cd18577  226 KGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
698-1271 2.62e-120

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 390.24  E-value: 2.62e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    698 WRIMKLNLTEWPYFVVG---VFCAIINGGLQPAF-AIIFSKIIGVFtridDPETkrQNSNLFSLLFLALGiiSFITFFLQ 773
Cdd:TIGR00958  150 FRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYtGRVIDTLGGDK----GPPA--LASAIFFMCLLSIA--SSVSAGLR 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    774 GFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIY 853
Cdd:TIGR00958  222 GGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    854 GWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQE----QKFEHMYAQSLQVPYR 929
Cdd:TIGR00958  300 SPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNKR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    930 NSLRKahifgITFSFTQAMM-YFSYAGCFRFGAYLVAHKLMSFEDvLLVFsavVFGAMAVGQ----VSSFAPDYAKAKIS 1004
Cdd:TIGR00958  380 KALAY-----AGYLWTTSVLgMLIQVLVLYYGGQLVLTGKVSSGN-LVSF---LLYQEQLGEavrvLSYVYSGMMQAVGA 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1005 AAHIIMIIEKTPLIDSysTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1084
Cdd:TIGR00958  451 SEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1085 RFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNK 1164
Cdd:TIGR00958  529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDFIMEFPNG 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1165 YSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLSTIQNADLIV 1244
Cdd:TIGR00958  607 YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQIL 684
                          570       580
                   ....*....|....*....|....*..
gi 42741659   1245 VFQNGRVKEHGTHQQLLAQKGIYFSMV 1271
Cdd:TIGR00958  685 VLKKGSVVEMGTHKQLMEDQGCYKHLV 711
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
753-1274 2.67e-117

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 377.89  E-value: 2.67e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    753 NLFSLLFLALGIISFITFFlQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSR 832
Cdd:TIGR02204   59 RYFAFLLVVALVLALGTAA-RFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSS 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    833 LAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQ 912
Cdd:TIGR02204  136 LSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGH 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    913 EQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDV-LLVFSAVvFGAMAVGQV 991
Cdd:TIGR02204  216 EDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVFYAV-MVAGSIGTL 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    992 SSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGS 1071
Cdd:TIGR02204  295 SEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGP 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1072 SGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdnsRV-VSQEEIVRAAK 1150
Cdd:TIGR02204  375 SGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG---RPdATDEEVEAAAR 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1151 EANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1230
Cdd:TIGR02204  452 AAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLII 531
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 42741659   1231 AHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1274
Cdd:TIGR02204  532 AHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
127-629 3.25e-117

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 377.13  E-value: 3.25e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    127 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 206
Cdd:TIGR02203   69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    207 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR 286
Cdd:TIGR02203  149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    287 IGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFSvligafSVGQASPSIEAFANARG------ 360
Cdd:TIGR02203  229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    361 -AAYEIFKIIDNKPSIDsysKSGHKPDNIKGNLEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL 439
Cdd:TIGR02203  302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    440 MQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGR-ENVTMDEIEKAVKEANAYDFIMKLPH 518
Cdd:TIGR02203  378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    519 KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVI 598
Cdd:TIGR02203  458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
                          490       500       510
                   ....*....|....*....|....*....|.
gi 42741659    599 AGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:TIGR02203  538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
133-629 2.30e-113

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 367.42  E-value: 2.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   133 VSFWCLA--AGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDD------------VSKINEG---IGDKIGMFFQ 195
Cdd:PRK11176   84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREGasiIGLFIMMFYY 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   196 SmatfftgfivgftrgWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 275
Cdd:PRK11176  164 S---------------WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   276 RYNKNLEEAKRIGIKKAITANISIGAAFLLiyASYALAFwygtTLVLSGEYSIGQVL-----TVFFSVLIGAFSVGQASP 350
Cdd:PRK11176  229 RFDKVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAF----VLYAASFPSVMDTLtagtiTVVFSSMIALMRPLKSLT 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   351 SIEA-FANARGAAYEIFKIIDNKPSIDSyskSGHKPDNIKGNLEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNS 429
Cdd:PRK11176  303 NVNAqFQRGMAACQTLFAILDLEQEKDE---GKRVIERAKGDIEFRNVTFTYPG-KEVPALRNINFKIPAGKTVALVGRS 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   430 GCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENV-TMDEIEKAVKEAN 508
Cdd:PRK11176  379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   509 AYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 588
Cdd:PRK11176  459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 42741659   589 LSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:PRK11176  539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
263-641 9.05e-113

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 366.45  E-value: 9.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  263 TVIAFGGQKKELERYNKNLEEAKRIGIKKAITAN-ISIGAAfLLIYASYALAFWYGTTLVLSGEYSIGQVltvffsVLIG 341
Cdd:COG5265  230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAlLNFGQA-LIIALGLTAMMLMAAQGVVAGTMTVGDF------VLVN 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  342 AFSvgqaspsIEAFA--NARGAAY-EI----------FKIIDNKPSIdsYSKSGHKPDNIK-GNLEFRNVHFSY-PSRKe 406
Cdd:COG5265  303 AYL-------IQLYIplNFLGFVYrEIrqaladmermFDLLDQPPEV--ADAPDAPPLVVGgGEVRFENVSFGYdPERP- 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  407 vkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAE 486
Cdd:COG5265  373 --ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAY 450
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  487 NIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 566
Cdd:COG5265  451 NIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  567 AVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAA 641
Cdd:COG5265  531 RAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
392-625 7.94e-109

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 341.90  E-value: 7.94e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:cd03251    1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  552 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKL 625
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
696-1277 1.92e-107

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 350.94  E-value: 1.92e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    696 SFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIgvftriDDPETKRQNSNLFSL------LFLALGIISFIT 769
Cdd:TIGR02203    1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLL------DDGFGGRDRSVLWWVplvvigLAVLRGICSFVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    770 FFLQGFTFGKageiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIII 849
Cdd:TIGR02203   75 TYLLSWVSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    850 SFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYR 929
Cdd:TIGR02203  149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    930 NSLRKAHIFGITFSFTQ-----AMMYFSYAGCFRFGA-YLVAHKLMSFedvllvFSAVVFGAMAVGQVSSFAPDYAKAKI 1003
Cdd:TIGR02203  229 LAMKMTSAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAF------ITAMIALIRPLKSLTNVNAPMQRGLA 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1004 SAAHIIMIIEKTPLIDsysTEGLMPNTLEGNVTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1083
Cdd:TIGR02203  303 AAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1084 ERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnSRVVSQEEIVRAAKEANIHAFIESLPN 1163
Cdd:TIGR02203  379 PRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPL 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1164 KYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1243
Cdd:TIGR02203  458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
                          570       580       590
                   ....*....|....*....|....*....|....
gi 42741659   1244 VVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGT 1277
Cdd:TIGR02203  538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1035-1267 1.76e-104

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 329.96  E-value: 1.76e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1114
Cdd:cd03251    1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILFDCSIAENIAYGDnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQP 1194
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1267
Cdd:cd03251  158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
392-629 1.09e-103

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 328.04  E-value: 1.09e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:cd03253    1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03253   79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  552 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:cd03253  159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1032-1275 1.00e-101

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 336.41  E-value: 1.00e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1032 EGNVTFGEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1111
Cdd:COG5265  355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALV 1191
Cdd:COG5265  433 AIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1192 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMV 1271
Cdd:COG5265  511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590

                 ....
gi 42741659 1272 SVQA 1275
Cdd:COG5265  591 ARQQ 594
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
390-620 1.08e-100

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 319.56  E-value: 1.08e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  390 GNLEFRNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 469
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 549
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  550 KILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKG 620
Cdd:cd03254  159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
139-620 1.49e-100

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 331.72  E-value: 1.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  139 AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVI 218
Cdd:COG4988   85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  219 LAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANIS 298
Cdd:COG4988  165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLS 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  299 IGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTV------FFSVL--IGAFsvgqaspsieaF---ANARGAAYEIFK 367
Cdd:COG4988  245 SAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVlllapeFFLPLrdLGSF-----------YharANGIAAAEKIFA 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  368 IIDNKPSIdsySKSGHKPDNIKGN--LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD 445
Cdd:COG4988  314 LLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  446 PTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVG 525
Cdd:COG4988  389 PYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLG 468
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  526 ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGV 605
Cdd:COG4988  469 EGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGR 548
                        490
                 ....*....|....*
gi 42741659  606 IVEKGNHDELMKEKG 620
Cdd:COG4988  549 IVEQGTHEELLAKNG 563
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
293-629 7.38e-100

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 330.77  E-value: 7.38e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   293 ITANISIGAAFLLiyasyalafwyGTTLVLSGEYSIGQVLTV--FFSVLIGAFSvgqaspSIEAFAN----ARGAAYEIF 366
Cdd:PRK13657  248 AASTITMLAILVL-----------GAALVQKGQLRVGEVVAFvgFATLLIGRLD------QVVAFINqvfmAAPKLEEFF 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   367 KIIDNKPSIDSYSKSGhKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP 446
Cdd:PRK13657  311 EVEDAVPDVRDPPGAI-DLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   447 TEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGE 526
Cdd:PRK13657  388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   527 RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVI 606
Cdd:PRK13657  468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
                         330       340
                  ....*....|....*....|...
gi 42741659   607 VEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:PRK13657  548 VESGSFDELVARGGRFAALLRAQ 570
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1035-1274 8.88e-100

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 317.25  E-value: 8.88e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1114
Cdd:cd03253    1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQP 1194
Cdd:cd03253   79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1274
Cdd:cd03253  157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1033-1265 7.24e-96

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 306.46  E-value: 7.24e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1033 GNVTFGEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAH 1112
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1113 LGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVR 1192
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659 1193 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1265
Cdd:cd03254  157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
754-1276 1.51e-94

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 315.81  E-value: 1.51e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   754 LFSLLFLAlGIISFITFFLQGFTFGKageiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 833
Cdd:PRK11176   71 VIGLMILR-GITSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGAL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   834 AVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIA-GVVE-------------MKMLSG---QALKDKKELEGSGKI 896
Cdd:PRK11176  144 ITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSkrfrnisknmqntMGQVTTsaeQMLKGHKEVLIFGGQ 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   897 ATEaIENFRTVVSLTQEQKFEHMYAQSLQVPyrnslrkahIFGITFSFTQAMMYFsyagcfrfgaylvahkLMSFEDVLL 976
Cdd:PRK11176  224 EVE-TKRFDKVSNRMRQQGMKMVSASSISDP---------IIQLIASLALAFVLY----------------AASFPSVMD 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   977 VFSA----VVFGAM--------AVGQVSS-FAPDYAKAKISAAHIIMIIEKtplidsySTEGLMPNTLEGNVTFGEVVFN 1043
Cdd:PRK11176  278 TLTAgtitVVFSSMialmrplkSLTNVNAqFQRGMAACQTLFAILDLEQEK-------DEGKRVIERAKGDIEFRNVTFT 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1044 YPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILF 1123
Cdd:PRK11176  351 YPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLF 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIAYGDNSRVvSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:PRK11176  430 NDTIANNIAYARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1204 SALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1276
Cdd:PRK11176  509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1026-1251 1.88e-90

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 291.30  E-value: 1.88e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1026 LMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN 1105
Cdd:cd03248    3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1106 VQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIA 1185
Cdd:cd03248   83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1186 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1251
Cdd:cd03248  161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
139-625 2.38e-90

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 303.61  E-value: 2.38e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  139 AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF-QSMATFFTGFIVGFTrgwkLTLV 217
Cdd:COG4987   82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----AVAF 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  218 ILAISPVLGLS-------AAVWAKILSSFTDK---ELLAYAKAGAVAE--EVLAAIRTVIAFGGQKKELERYN---KNLE 282
Cdd:COG4987  150 LAFFSPALALVlalglllAGLLLPLLAARLGRragRRLAAARAALRARltDLLQGAAELAAYGALDRALARLDaaeARLA 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  283 EAKRigiKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLiGAFSVgqASPSIEAFAN---AR 359
Cdd:COG4987  230 AAQR---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL-ALFEA--LAPLPAAAQHlgrVR 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  360 GAAYEIFKIIDNKPSIDSYSKSGHKPDNikGNLEFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL 439
Cdd:COG4987  304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  440 MQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHK 519
Cdd:COG4987  381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  520 FDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIA 599
Cdd:COG4987  461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
                        490       500
                 ....*....|....*....|....*.
gi 42741659  600 GFDDGVIVEKGNHDELMKEKGIYFKL 625
Cdd:COG4987  541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
150-630 9.25e-90

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 305.90  E-value: 9.25e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    150 QFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSA 229
Cdd:TIGR01846  217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLS 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    230 AVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYAS 309
Cdd:TIGR01846  296 VFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLT 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    310 YALAFWYGTTLVLSGEYSIGQVltVFFSVLIGAFS--VGQASPSIEAFANARGAAYEIFKIIdNKPSiDSYSKSGHKPDN 387
Cdd:TIGR01846  376 FAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQTGIALERLGDIL-NSPT-EPRSAGLAALPE 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    388 IKGNLEFRNVHFSY-PSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFL 466
Cdd:TIGR01846  452 LRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    467 REIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALV 546
Cdd:TIGR01846  530 RRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    547 RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 626
Cdd:TIGR01846  610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689

                   ....
gi 42741659    627 TMQT 630
Cdd:TIGR01846  690 QQQS 693
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
44-375 5.38e-88

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 288.20  E-value: 5.38e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   44 NWLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEdlmsnitnrsdindtgffmnLEEDMTRYAYYYSGIGA 123
Cdd:cd18578    4 NKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDE--------------------LRSEANFWALMFLVLAI 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  124 GVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFD--VHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFF 201
Cdd:cd18578   64 VAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  202 TGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNL 281
Cdd:cd18578  144 AGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEAL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  282 EEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGA 361
Cdd:cd18578  224 EEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAA 303
                        330
                 ....*....|....
gi 42741659  362 AYEIFKIIDNKPSI 375
Cdd:cd18578  304 AARIFRLLDRKPEI 317
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
699-1265 8.61e-87

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 293.59  E-value: 8.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  699 RIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKII-GVFTRIDDPetkrqnSNLFSLLFLALGII---SFITFFLQG 774
Cdd:COG4988    7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPL------SALLPLLGLLLAVLllrALLAWLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  775 FTFgKAGEILTKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIG-----SRLAVITQnianLGTGIII 849
Cdd:COG4988   81 AAF-RAAARVKRRLRRRLLEKLLALGPAWLRGKS--TGELATLLTEGVEALDGYFArylpqLFLAALVP----LLILVAV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  850 SFIYgWQLTLLLLAIVPII----AIAGV----------VEMKMLSGQ---ALK----------DKKELEgsgKIATEAiE 902
Cdd:COG4988  154 FPLD-WLSGLILLVTAPLIplfmILVGKgaakasrrqwRALARLSGHfldRLRglttlklfgrAKAEAE---RIAEAS-E 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  903 NFRTvvsltqeqkfehmyaQSLQVpyrnsLRKAhiFGITFsftqAMMYFSYagcfrFGAYLVAhklmsfedVLLVFSAV- 981
Cdd:COG4988  229 DFRK---------------RTMKV-----LRVA--FLSSA----VLEFFAS-----LSIALVA--------VYIGFRLLg 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  982 ----VFGAMAV-----------GQVSSFapdY-AKAK-ISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNY 1044
Cdd:COG4988  270 gsltLFAALFVlllapefflplRDLGSF---YhARANgIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1045 PTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1124
Cdd:COG4988  347 PGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1125 CSIAENIAYGDnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:COG4988  425 GTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1205 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1265
Cdd:COG4988  503 HLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
392-629 2.74e-84

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 274.75  E-value: 2.74e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:cd03252    1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03252   80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  552 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
51-343 5.44e-84

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 275.29  E-value: 5.44e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     51 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFanagnledlmsnitnrSDINDTGFFmnleeDMTRYAYYYSGIGAGVLVAAY 130
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVL----------------LPDGDPETQ-----ALNVYSLALLLLGLAQFILSF 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    131 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:pfam00664   60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:pfam00664  140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659    291 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQ--VLTVFFSVLIGAF 343
Cdd:pfam00664  220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
711-1008 3.14e-83

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 274.35  E-value: 3.14e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRI----DDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTK 786
Cdd:cd18577    1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFgsgeSSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  787 RLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVP 866
Cdd:cd18577   81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  867 IIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQ 946
Cdd:cd18577  159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  947 AMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHI 1008
Cdd:cd18577  239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
385-606 5.95e-83

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 270.50  E-value: 5.95e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  385 PDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR 464
Cdd:cd03248    5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  465 FLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:cd03248   85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  545 LVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVI 606
Cdd:cd03248  165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
840-1265 2.70e-81

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 278.77  E-value: 2.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   840 IANLGTGIIISFIYGWQLTLLLLAIVPI-IAIAGVVEMKMLSGQALKDKKELEGSGKiATEAIENFRTVVSLTQ---EQK 915
Cdd:PRK13657  141 LVALVVLLPLALFMNWRLSLVLVVLGIVyTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRieaETQ 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   916 FEHMYAQSL---QVPYRNSLrkAHIFGIT-FSFTQAMMyfsyaGCFRFGAYLVAHKLMSFEDVLlvfSAVVFGAMAVG-- 989
Cdd:PRK13657  220 ALRDIADNLlaaQMPVLSWW--ALASVLNrAASTITML-----AILVLGAALVQKGQLRVGEVV---AFVGFATLLIGrl 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   990 -QVSSFAPDYAKAKISAAHIIMIIEKTPliDSYSTEGLM-PNTLEGNVTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLA 1067
Cdd:PRK13657  290 dQVVAFINQVFMAAPKLEEFFEVEDAVP--DVRDPPGAIdLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1068 LVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVR 1147
Cdd:PRK13657  366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRA 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1148 AAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTC 1227
Cdd:PRK13657  444 AAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTT 523
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 42741659  1228 IVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1265
Cdd:PRK13657  524 FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
784-1272 3.38e-81

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 278.19  E-value: 3.38e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  784 LTKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIgsrLAVITQNIANLGTGIIISFIYGWQLTLLLLA 863
Cdd:COG4987   86 LLADLRVRLYRRLEPLAPAGLARLR--SGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  864 IVPIIAIAGVVeMKMLSGQALK--DKKELEGSGKIATEAIENFRTVVSLT---QEQKFEHMYAQSLQVPYRNSLRKAHIF 938
Cdd:COG4987  161 LALGLLLAGLL-LPLLAARLGRraGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDAAEARLAAAQRRLARLS 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  939 GITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSfeDVLLVfsAVVFGAMA----VGQVSSFAPDYAKAKISAAHIIMIIEK 1014
Cdd:COG4987  240 ALAQALLQLAAGLAVVAVLWLAAPLVAAGALS--GPLLA--LLVLAALAlfeaLAPLPAAAQHLGRVRAAARRLNELLDA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1015 TPLIDSYSTEGLMPNTLEgnVTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKV 1094
Cdd:COG4987  316 PPAVTEPAEPAPAPGGPS--LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1095 LLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGT 1174
Cdd:COG4987  393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1175 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEH 1254
Cdd:COG4987  471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
                        490
                 ....*....|....*...
gi 42741659 1255 GTHQQLLAQKGIYFSMVS 1272
Cdd:COG4987  551 GTHEELLAQNGRYRQLYQ 568
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1035-1274 2.74e-80

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 263.58  E-value: 2.74e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1113
Cdd:cd03252    1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1114 GIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQ 1193
Cdd:cd03252   79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1194 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSV 1273
Cdd:cd03252  157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236

                 .
gi 42741659 1274 Q 1274
Cdd:cd03252  237 Q 237
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
392-604 4.75e-80

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 260.01  E-value: 4.75e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:cd03228    1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03228   80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 42741659  552 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDG 604
Cdd:cd03228  118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
317-626 4.03e-78

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 269.84  E-value: 4.03e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    317 GTTLVLSGEYSIGQVLTV--FFSVLIGAFSvgQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPdNIKGNLEF 394
Cdd:TIGR01192  261 GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELP-NVKGAVEF 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    395 RNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVS 474
Cdd:TIGR01192  338 RHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVF 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    475 QEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 554
Cdd:TIGR01192  416 QDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVL 495
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659    555 DEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 626
Cdd:TIGR01192  496 DEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1035-1250 1.43e-77

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 253.07  E-value: 1.43e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1114
Cdd:cd03228    1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILFDCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQP 1194
Cdd:cd03228   80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGR 1250
Cdd:cd03228  116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
979-1276 3.03e-76

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 267.38  E-value: 3.03e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    979 SAVVFGAMAVGQVSSF--------AP---------DYAKAKISAAHIIMIIEkTPLIDSYSTEGLMPNtLEGNVTFGEVV 1041
Cdd:TIGR01846  385 HLVIGGALSPGQLVAFnmlagrvtQPvlrlaqlwqDFQQTGIALERLGDILN-SPTEPRSAGLAALPE-LRGAITFENIR 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1042 FNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP 1120
Cdd:TIGR01846  463 FRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1121 ILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:TIGR01846  541 VLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   1201 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1276
Cdd:TIGR01846  619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
694-1267 4.70e-76

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 267.19  E-value: 4.70e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    694 PVSFWRIMKLNLTEWP----YFVVGVFCAIINGGLQPAFAIIFskiigvftrIDDPETKRQNSNLFSLL---FLALGIIS 766
Cdd:TIGR03796  138 KPSLLRALWRRLRGSRgallYLLLAGLLLVLPGLVIPAFSQIF---------VDEILVQGRQDWLRPLLlgmGLTALLQG 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    767 FITFfLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANdAAQVKGAIGSRLAVITQNIANLGTG 846
Cdd:TIGR03796  209 VLTW-LQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFY 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    847 IIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYA--QSL 924
Cdd:TIGR03796  285 ALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAgyQAK 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    925 QVPYRNSL-RKAHIFGItfsFTQAMMYFSYAGCFRFGAYLVAHKLMS------FEDVLLVFSAVVFGAMAVGQ-VSSFAP 996
Cdd:TIGR03796  365 LLNAQQELgVLTQILGV---LPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGtLQELEG 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    997 DYAKAKISAAHIIMIIEKTPLIDSYSTEglMPNTLEGNVTFGEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGK 1076
Cdd:TIGR03796  442 DLNRLDDVLRNPVDPLLEEPEGSAATSE--PPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGK 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1077 STVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHA 1156
Cdd:TIGR03796  519 STIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHD 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1157 FIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLST 1236
Cdd:TIGR03796  597 VITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLST 674
                          570       580       590
                   ....*....|....*....|....*....|.
gi 42741659   1237 IQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1267
Cdd:TIGR03796  675 IRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
712-1274 1.38e-73

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 259.50  E-value: 1.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    712 VVGVFCAIInGGLQP-AFAIIFSKIIgvftriddPETKRQnsnLFSLLFLALGIISFITF---FLQGFTFGKAGEILTKR 787
Cdd:TIGR03797  143 AMGLLGTLL-GMLVPiATGILIGTAI--------PDADRS---LLVQIALALLAAAVGAAafqLAQSLAVLRLETRMDAS 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    788 LRYMVFRSMLRQDVSWFDdpKNTTGALTTRlANDAAQVKGAIGSRL--AVITQNIANLGTGIIisFIYGWQLTL--LLLA 863
Cdd:TIGR03797  211 LQAAVWDRLLRLPVSFFR--QYSTGDLASR-AMGISQIRRILSGSTltTLLSGIFALLNLGLM--FYYSWKLALvaVALA 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    864 IVpIIAIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSL----TQEQKF---EHMYAQSLQVpyrnSLRKAH 936
Cdd:TIGR03797  286 LV-AIAVTLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKLrvagAENRAFarwAKLFSRQRKL----ELSAQR 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    937 IFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTP 1016
Cdd:TIGR03797  357 IENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALP 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1017 LIDSYSTEglmPNTLEGNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVL 1095
Cdd:TIGR03797  437 EVDEAKTD---PGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVF 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1096 LDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsrVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQ 1175
Cdd:TIGR03797  512 YDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGT 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1176 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVFQNGRVKEHG 1255
Cdd:TIGR03797  589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQG 666
                          570
                   ....*....|....*....
gi 42741659   1256 THQQLLAQKGIYFSMVSVQ 1274
Cdd:TIGR03797  667 TYDELMAREGLFAQLARRQ 685
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
711-986 1.58e-72

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 242.93  E-value: 1.58e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETkrQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 790
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    791 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 870
Cdd:pfam00664   79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    871 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 950
Cdd:pfam00664  157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 42741659    951 FSYAGCFRFGAYLVAHKLMSFED--VLLVFSAVVFGAM 986
Cdd:pfam00664  237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
395-1270 4.69e-71

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 262.19  E-value: 4.69e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    395 RNVHFSYpSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrflreiIGVVS 474
Cdd:TIGR00957  640 HNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVP 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    475 QEPVLFATTIAENIRYGREnvTMDEIEKAVKEANAY--DFIMkLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 552
Cdd:TIGR00957  706 QQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    553 LLDEATSALDTEseaVVQVALDKA------RKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFK-L 625
Cdd:TIGR00957  783 LFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfL 859
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    626 VTMQTAGNEVELEN--AADESKSEIDALEMSSNDSRSSLIRKRSTRR---SVRGSQAQDRKLSTKEALDESIPPVSFWRI 700
Cdd:TIGR00957  860 RTYAPDEQQGHLEDswTALVSGEGKEAKLIENGMLVTDVVGKQLQRQlsaSSSDSGDQSRHHGSSAELQKAEAKEETWKL 939
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    701 MKLNLTE---------WPYF-VVGVFCAIINGGL---QPAFAIIFSKIIGVFTriDDP--ETKRQNSNLFSLLFLALGII 765
Cdd:TIGR00957  940 MEADKAQtgqvelsvyWDYMkAIGLFITFLSIFLfvcNHVSALASNYWLSLWT--DDPmvNGTQNNTSLRLSVYGALGIL 1017
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    766 SFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIAN-LG 844
Cdd:TIGR00957 1018 QGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIG 1095
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    845 TGIIISFIygwqlTLLLLAIVPIIAIAGVVEMKMLSGQAlKDKKELEGSGKIA-----TEAIENFRTVVSLTQEQKFEHM 919
Cdd:TIGR00957 1096 ALIVILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQ 1169
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    920 yaQSLQVpyrNSLRKAhifgitfsftqammYFSYAGCFRF---GAYLVAHKLMSFEDVLLVFSAVVFGAMAVG------- 989
Cdd:TIGR00957 1170 --SDLKV---DENQKA--------------YYPSIVANRWlavRLECVGNCIVLFAALFAVISRHSLSAGLVGlsvsysl 1230
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    990 QVSSFAPDYAKAKISAAHIIMIIEKtplIDSYS-TEGLMPNTLEGNVT------FGEVVF-NYPTR--PDIP-VLQGLSL 1058
Cdd:TIGR00957 1231 QVTFYLNWLVRMSSEMETNIVAVER---LKEYSeTEKEAPWQIQETAPpsgwppRGRVEFrNYCLRyrEDLDlVLRHINV 1307
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1059 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSR 1138
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFS 1384
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1139 VVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL 1218
Cdd:TIGR00957 1385 QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|..
gi 42741659   1219 DKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1270
Cdd:TIGR00957 1465 RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
390-610 2.95e-70

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 234.41  E-value: 2.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  390 GNLEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 469
Cdd:cd03245    1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 549
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  550 KILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 610
Cdd:cd03245  160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
104-628 6.52e-68

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 251.87  E-value: 6.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   104 FMNLEEDMTRYAYYYSGIGAGVLVAAYIQvSFWCLAAGRQIHK-IRKQFFHAIMRQEIGWFD--VHDVGELNTRLTDDVS 180
Cdd:PTZ00265  858 FANLEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH 936
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   181 KINEGIGDKIGMFFQSMATFFTGFIVGF----------TRGWKLTLVILAISPVLGLSAAVWAK-------ILSSFTDKE 243
Cdd:PTZ00265  937 LLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpivaavlTGTYFIFMRVFAIRARLTANKDVEKKeinqpgtVFAYNSDDE 1016
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   244 LlaYAKAGAVAEEVLAAIRTVIAFGgqkkeLERYNKNLEEA----KRIGIKKAITAN-----ISIGAAFLLiyasYALAF 314
Cdd:PTZ00265 1017 I--FKDPSFLIQEAFYNMNTVIIYG-----LEDYFCNLIEKaidySNKGQKRKTLVNsmlwgFSQSAQLFI----NSFAY 1085
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   315 WYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDN---IKGN 391
Cdd:PTZ00265 1086 WFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGK 1165
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-------------------------- 445
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgd 1245
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   446 ----------------------------PTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTM 497
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   498 DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVAL---- 573
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1405
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659   574 DKARKgrTTIVIAHRLSTVRNADVIAGFDD----GVIVE-KGNHDELMK-EKGIYFKLVTM 628
Cdd:PTZ00265 1406 DKADK--TIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
161-629 9.71e-67

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 239.47  E-value: 9.71e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    161 GWFDVHDVGELNTRlTDDVSKINEGIGDK-IGMFFQSMATFFTgFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILssf 239
Cdd:TIGR03797  225 SFFRQYSTGDLASR-AMGISQIRRILSGStLTTLLSGIFALLN-LGLMFYYSWKLALVAVALALVAIAVTLVLGLLQ--- 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    240 TDKELLAYAKAGAVAEEVLAAIRTVIAF---GGQKKELERYNKNLEEAKRIGIKKAITANI--SIGAAFLLIyASYALaF 314
Cdd:TIGR03797  300 VRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLltVFNAVLPVL-TSAAL-F 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    315 WYGTTLVLSGEYSIGQVLTvfFSVLIGAF--SVGQASPSIEAfANARGAAYEIFK-IIDNKPSIDSYSKsghKPDNIKGN 391
Cdd:TIGR03797  378 AAAISLLGGAGLSLGSFLA--FNTAFGSFsgAVTQLSNTLIS-ILAVIPLWERAKpILEALPEVDEAKT---DPGKLSGA 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    392 LEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:TIGR03797  452 IEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    472 VVSQEPVLFATTIAENIrYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:TIGR03797  531 VVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRI 609
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659    552 LLLDEATSALDTESEAVVQVALDKARKGRttIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 629
Cdd:TIGR03797  610 LLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
121-645 2.56e-66

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 235.38  E-value: 2.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   121 IGAGVLVAA--YIQVSFWCL----AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 194
Cdd:PRK10789   39 IGTMVLIAVvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   195 QSMATFFTGFIVGFTR-GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKE 273
Cdd:PRK10789  119 DSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQ 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   274 LERY--------NKNLEEAkRIGIKKAITANISIGAAFLLiyasyalAFWYGTTLVLSGEYSIGQvLTVFFSVLigafsv 345
Cdd:PRK10789  199 SALFaadaedtgKKNMRVA-RIDARFDPTIYIAIGMANLL-------AIGGGSWMVVNGSLTLGQ-LTSFVMYL------ 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   346 GQASPSIEAFA---N--ARG-AAY-EIFKIIDNKPSIdsysKSGHKP-DNIKGNLEFRNVHFSYPsRKEVKILKGLNLKV 417
Cdd:PRK10789  264 GLMIWPMLALAwmfNivERGsAAYsRIRAMLAEAPVV----KDGSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFTL 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   418 QSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTM 497
Cdd:PRK10789  339 KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQ 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   498 DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAR 577
Cdd:PRK10789  419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659   578 KGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQtagnevELENAADESK 645
Cdd:PRK10789  499 EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ------QLEAALDDAP 560
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1033-1251 6.78e-66

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 222.08  E-value: 6.78e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1033 GNVTFGEVVFNYPTRPdIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAH 1112
Cdd:cd03245    1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1113 LGIVSQEPILFDCSIAENIAYGDnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVR 1192
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1193 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1251
Cdd:cd03245  158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
354-598 1.74e-65

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 231.79  E-value: 1.74e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    354 AFANARGAAYEIFKIIDNKPSIDSYSKSghKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGK 433
Cdd:TIGR02857  286 ARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    434 STTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFI 513
Cdd:TIGR02857  362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    514 MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVR 593
Cdd:TIGR02857  442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521

                   ....*
gi 42741659    594 NADVI 598
Cdd:TIGR02857  522 LADRI 526
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
390-611 1.01e-64

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 218.90  E-value: 1.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  390 GNLEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 469
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFATTIAENI----RYgrenvTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARAL 545
Cdd:cd03244   80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  546 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 611
Cdd:cd03244  155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
1032-1263 4.17e-64

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 228.86  E-value: 4.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1032 EGNVTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1111
Cdd:COG4618  328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQEPILFDCSIAENIA-YGDnsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARAL 1190
Cdd:COG4618  407 HIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1191 VRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG4618  483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
757-1274 2.81e-63

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 226.52  E-value: 2.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   757 LLFLALgIISFITFFLQGFTFGkAGEILTKRLRYMVFRSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGAIGSR-LAV 835
Cdd:PRK10789   42 MVLIAV-VVYLLRYVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVDRVVFAAGEGvLTL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   836 ITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIA-----GVVEMKMLSGQA----LKDKkelegsgkiATEAIENFRT 906
Cdd:PRK10789  118 VDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMikrygDQLHERFKLAQAafssLNDR---------TQESLTSIRM 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   907 VVSLTQEQKFEHMYAQSLQVPYRNSLRKAHI---FGITFSFTQAMMYFSYAGCfrfGAYLVAHklmsfedvllvfsavvf 983
Cdd:PRK10789  189 IKAFGLEDRQSALFAADAEDTGKKNMRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVN----------------- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   984 GAMAVGQVSSFA--------PDYAKA-------KISAAH--IIMIIEKTPLIDSySTEGLM--PNTLEGNVTfgevVFNY 1044
Cdd:PRK10789  249 GSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAAYsrIRAMLAEAPVVKD-GSEPVPegRGELDVNIR----QFTY 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1045 PTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1124
Cdd:PRK10789  324 PQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PRK10789  403 DTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1205 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1274
Cdd:PRK10789  481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
PLN03232 PLN03232
ABC transporter C family member; Provisional
392-1271 1.50e-62

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 234.87  E-value: 1.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEgMVSVDgqdirtinvrfLREIIG 471
Cdd:PLN03232  615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVLFATTIAENIRYGRENvtmdEIEKAVKeanAYDfIMKLPHKFD-------TLVGERGAQLSGGQKQRIAIARA 544
Cdd:PLN03232  683 YVPQVSWIFNATVRENILFGSDF----ESERYWR---AID-VTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARA 754
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   545 LVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYF 623
Cdd:PLN03232  755 VYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   624 KLvtMQTAG--NEVELENAADESKSEIDA-LEMSSNDSRSSLIRKRSTRRSVrgsqaqdrkLSTKEALDESIppVSFWRI 700
Cdd:PLN03232  835 KL--MENAGkmDATQEVNTNDENILKLGPtVTIDVSERNLGSTKQGKRGRSV---------LVKQEERETGI--ISWNVL 901
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   701 MKLNLTEWPYFVVGVF--CAIinggLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFItfFLQGFTFG 778
Cdd:PLN03232  902 MRYNKAVGGLWVVMILlvCYL----TTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVT--FTNSFWLI 975
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   779 KAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDaaqvkgaIGSrlavITQNIANLGTGIIISFiygWQL- 857
Cdd:PLN03232  976 SSSLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKD-------IGD----IDRNVANLMNMFMNQL---WQLl 1039
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   858 -TLLLLAIVPIIAIAGVVEMKMLSGQAL-------KDKKELEGSGKIAT-----EAIENFRTVVSLTQEQKFEHMYAQSL 924
Cdd:PLN03232 1040 sTFALIGTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGKSM 1119
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   925 QVPYRNSLRKAHIFG---ITFSFTQAMMYFSYA--GCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMA--VGQVSSFAPD 997
Cdd:PLN03232 1120 DNNIRFTLANTSSNRwltIRLETLGGVMIWLTAtfAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSgvLRQASKAENS 1199
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   998 YAKAKISAAHIIMIIEKTPLIDSYSTEGLMPntLEGNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGK 1076
Cdd:PLN03232 1200 LNSVERVGNYIDLPSEATAIIENNRPVSGWP--SRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGK 1275
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1077 STVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHA 1156
Cdd:PLN03232 1276 SSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKD 1352
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1157 FIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1236
Cdd:PLN03232 1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
                         890       900       910
                  ....*....|....*....|....*....|....*.
gi 42741659  1237 IQNADLIVVFQNGRVKEHGTHQQLLAQKG-IYFSMV 1271
Cdd:PLN03232 1433 IIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1033-1256 3.85e-61

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 208.50  E-value: 3.85e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1033 GNVTFGEVVFNYptRPDI-PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1111
Cdd:cd03244    1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALV 1191
Cdd:cd03244   79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1192 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:cd03244  156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
216-618 6.87e-61

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 219.23  E-value: 6.87e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  216 LVILAISPVLGLSAAVWAKILSSFT------DKELL-----AYAKAGAVAEEVLAAIRTVIAFG----GQKKELERYNKN 280
Cdd:COG4618  148 AVLFLFHPLLGLLALVGALVLVALAllnerlTRKPLkeaneAAIRANAFAEAALRNAEVIEAMGmlpaLRRRWQRANARA 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  281 LEEAKRIGIKKAITANISIGAAFLLIYASYALAFWygttLVLSGEYSIGqvltVFF--SVLIG-AFS-VGQASPSIEAFA 356
Cdd:COG4618  228 LALQARASDRAGGFSALSKFLRLLLQSAVLGLGAY----LVIQGEITPG----AMIaaSILMGrALApIEQAIGGWKQFV 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  357 NARGAAYEIFKIIDNKPSIDSYSKSGhKPdniKGNLEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTT 436
Cdd:COG4618  300 SARQAYRRLNELLAAVPAEPERMPLP-RP---KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  437 VQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI-RYGreNVTMDEIEKAVKEANAYDFIMK 515
Cdd:COG4618  375 ARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILR 452
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  516 LPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN 594
Cdd:COG4618  453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAA 532
                        410       420
                 ....*....|....*....|....
gi 42741659  595 ADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:COG4618  533 VDKLLVLRDGRVQAFGPRDEVLAR 556
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
759-1274 1.03e-60

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 219.59  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   759 FLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQ 838
Cdd:PRK10790   71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATVLR 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   839 NIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKF-E 917
Cdd:PRK10790  149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   918 HMYAQSlqvpyrnslrKAHifgitfsftqammYFSYAGCFRFGAYLVAHKLMSFE-----DVLLVFSAVVFGAMAVGQVS 992
Cdd:PRK10790  229 RMGEAS----------RSH-------------YMARMQTLRLDGFLLRPLLSLFSalilcGLLMLFGFSASGTIEVGVLY 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   993 SFapdyakakISaaHIIMIIEktPLIDSYSTEGLMPNTL-------------------------EGNVTFGEVVFNYptR 1047
Cdd:PRK10790  286 AF--------IS--YLGRLNE--PLIELTTQQSMLQQAVvagervfelmdgprqqygnddrplqSGRIDIDNVSFAY--R 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSI 1127
Cdd:PRK10790  352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1128 AENIAYGdnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK10790  432 LANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1208 TESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1274
Cdd:PRK10790  509 SGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
127-627 8.45e-60

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 219.61  E-value: 8.45e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    127 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSMATFFT-GFI 205
Cdd:TIGR01193  211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    206 VGFtRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGqkkELERYNK------ 279
Cdd:TIGR01193  290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefg 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    280 -NLEEAKRIGIKKAITANISIGAAFLLIyasyALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF-----SVGQASPSIE 353
Cdd:TIGR01193  366 dYLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKLQ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    354 AFANARGAAYEIFKIidnkPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGK 433
Cdd:TIGR01193  440 AARVANNRLNEVYLV----DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGK 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    434 STTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG-RENVTMDEIEKAVKEANAYDF 512
Cdd:TIGR01193  514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDD 593
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    513 IMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKArKGRTTIVIAHRLSTV 592
Cdd:TIGR01193  594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVA 672
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 42741659    593 RNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVT 627
Cdd:TIGR01193  673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
990-1245 2.39e-59

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 213.69  E-value: 2.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    990 QVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEgnVTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLALV 1069
Cdd:TIGR02857  279 QLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALV 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1070 GSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRVVSQEEIVRAA 1149
Cdd:TIGR02857  355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREAL 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1150 KEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV 1229
Cdd:TIGR02857  433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
                          250
                   ....*....|....*.
gi 42741659   1230 IAHRLSTIQNADLIVV 1245
Cdd:TIGR02857  513 VTHRLALAALADRIVV 528
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
126-646 1.53e-58

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 213.04  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   126 LVAA---YIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFT 202
Cdd:PRK10790   76 LLAAglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGA 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   203 GFIVGFTRGWKLTLVILAISPVLGLSAAVWAKiLSSFTDKELLAY-AKAGAVAEEVLAAIrTVIAfggQKKELERYNKNL 281
Cdd:PRK10790  156 MLVAMFSLDWRMALVAIMIFPAVLVVMVIYQR-YSTPIVRRVRAYlADINDGFNEVINGM-SVIQ---QFRQQARFGERM 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   282 EEAKRIGIKKAITA----------NISIGAAFLLIyasyALAFWYGttlvLSGEYSIG-QVLTVFFSVLiGAFSvgqaSP 350
Cdd:PRK10790  231 GEASRSHYMARMQTlrldgfllrpLLSLFSALILC----GLLMLFG----FSASGTIEvGVLYAFISYL-GRLN----EP 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   351 SIE------AFANARGAAYEIFKIIDNkpsidsySKSGHKPDNI---KGNLEFRNVHFSYpsRKEVKILKGLNLKVQSGQ 421
Cdd:PRK10790  298 LIElttqqsMLQQAVVAGERVFELMDG-------PRQQYGNDDRplqSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   422 TVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGReNVTMDEIE 501
Cdd:PRK10790  369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVW 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   502 KAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRT 581
Cdd:PRK10790  448 QALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT 527
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   582 TIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKS 646
Cdd:PRK10790  528 LVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
218-589 1.74e-58

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 211.45  E-value: 1.74e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    218 ILAISPVLGLSAAVWAKILSSFTDKELLAYAKaGAVAEEVLAAIR---TVIAFGGQKKELERYNKNLEEAKRIGIKKAIT 294
Cdd:TIGR02868  158 ILAAGLLLAGFVAPLVSLRAARAAEQALARLR-GELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAA 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    295 ANISIGAAFLLIYASYALAFWYGTTLVLSGEYSiGQVLTVFFSVLIGAF-SVGQASPSIEAFANARGAAYEIFKIIDNKP 373
Cdd:TIGR02868  237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVLDAAG 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    374 SIDSYSKSGHKPDNIKG-NLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS 452
Cdd:TIGR02868  316 PVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    453 VDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLS 532
Cdd:TIGR02868  394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659    533 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRL 589
Cdd:TIGR02868  474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
981-1270 1.90e-58

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 212.38  E-value: 1.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   981 VVFGAMA--------------VGQVSSfapdyakakiSAAHIIMIIEKTPLIDSYSTEGLMPNtlEGNVTFGEVVFNYPT 1046
Cdd:PRK11160  283 FVFAALAafealmpvagafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPD 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1047 RPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCS 1126
Cdd:PRK11160  351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1127 IAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESlPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:PRK11160  430 LRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  1207 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1270
Cdd:PRK11160  507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
PLN03130 PLN03130
ABC transporter C family member; Provisional
395-1271 3.16e-58

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 221.54  E-value: 3.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   395 RNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdgqdirtinvrfLREIIGVVS 474
Cdd:PLN03130  618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   475 QEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 554
Cdd:PLN03130  686 QVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   555 DEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLvtMQTAGn 633
Cdd:PLN03130  765 DDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--MENAG- 841
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   634 evELENAADESKSEIDalemsSNDSRSSLIRKRSTRRSVRGSQAQDRK-----LSTKEALDESIppVSFWRIMKLNLTEW 708
Cdd:PLN03130  842 --KMEEYVEENGEEED-----DQTSSKPVANGNANNLKKDSSSKKKSKegksvLIKQEERETGV--VSWKVLERYKNALG 912
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   709 PYFVVGV--FCAIinggLQPAFAIIFSKIIGVFTriDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTK 786
Cdd:PLN03130  913 GAWVVMIlfLCYV----LTEVFRVSSSTWLSEWT--DQGTPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAK 986
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   787 RLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAaqvkGAIGSRLAVITQNIAN-----LGTGIIISFIYgwqlTLLL 861
Cdd:PLN03130  987 RLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKDL----GDIDRNVAVFVNMFLGqifqlLSTFVLIGIVS----TISL 1056
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   862 LAIVPI-IAIAGVVEMKMLSGQALKDKKELEGSGKIAT--EAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSL---RKA 935
Cdd:PLN03130 1057 WAIMPLlVLFYGAYLYYQSTAREVKRLDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLvnmSSN 1136
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   936 HIFGITFSFTQAMMYFsYAGCFRFGAYLVAHKLMSFED---VLLVFSAVVFGAM-AVGQVSSFAPDYAKAKISAAHIIMI 1011
Cdd:PLN03130 1137 RWLAIRLETLGGLMIW-LTASFAVMQNGRAENQAAFAStmgLLLSYALNITSLLtAVLRLASLAENSLNAVERVGTYIDL 1215
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1012 IEKTPL-IDSYSTEGLMPNTleGNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP 1089
Cdd:PLN03130 1216 PSEAPLvIENNRPPPGWPSS--GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1090 LAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKV 1169
Cdd:PLN03130 1292 ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEV 1368
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1170 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTIQNADLIVVFQ 1247
Cdd:PLN03130 1369 SEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLD 1446
                         890       900
                  ....*....|....*....|....*
gi 42741659  1248 NGRVKEHGTHQQLLAQKGIYFS-MV 1271
Cdd:PLN03130 1447 AGRVVEFDTPENLLSNEGSAFSkMV 1471
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
361-625 1.28e-55

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 203.90  E-value: 1.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   361 AAYEIFKIIDNKPSIDSYSKSGHKPDniKGNLEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM 440
Cdd:PRK11160  310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   441 QRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTmDEIEKAVKEANAYDFIMKLPHKF 520
Cdd:PRK11160  387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   521 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG 600
Cdd:PRK11160  466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
                         250       260
                  ....*....|....*....|....*
gi 42741659   601 FDDGVIVEKGNHDELMKEKGIYFKL 625
Cdd:PRK11160  546 MDNGQIIEQGTHQELLAQQGRYYQL 570
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
715-1273 3.69e-55

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 205.74  E-value: 3.69e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    715 VFCAIINGGLQPAFAIIFSKIIGVFTriddPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFR 794
Cdd:TIGR01193  162 VIAAIIVTLISIAGSYYLQKIIDTYI----PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIK 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    795 SMLRQDVSWFDDPKntTGALTTRLAnDAAQVKGAIGSrlaVITQNIANLGTGIIISFIYGWQ---LTLLLLAIVPIIAIA 871
Cdd:TIGR01193  238 HLFELPMSFFSTRR--TGEIVSRFT-DASSIIDALAS---TILSLFLDMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVI 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    872 GVVEMKMLSGQalkDKKELEGSGKIATEAIENF---RTVVSLTQE----QKFEHMYAQSLQVPYRNS----LRKAHIFGI 940
Cdd:TIGR01193  312 IILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETIKSLTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVT 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    941 TFSFTQAMMYFsyagcfrfGAYLVAHKLMSFEDvLLVFSAVV-FGAMAVGQVSSFAPDYAKAKISAAHIimiiEKTPLID 1019
Cdd:TIGR01193  389 KLILNVVILWT--------GAYLVMRGKLTLGQ-LITFNALLsYFLTPLENIINLQPKLQAARVANNRL----NEVYLVD 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1020 SYSTEGLMP---NTLEGNVTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLL 1096
Cdd:TIGR01193  456 SEFINKKKRtelNNLNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1097 DGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQL 1176
Cdd:TIGR01193  534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSI 612
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1177 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:TIGR01193  613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
                          570
                   ....*....|....*..
gi 42741659   1257 HQQLLAQKGIYFSMVSV 1273
Cdd:TIGR01193  692 HDELLDRNGFYASLIHN 708
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
317-618 1.13e-53

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 197.57  E-value: 1.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    317 GTTLVLSGEYSIGqvltvffSVLIGAFSVGQASPSIE-------AFANARGAAYEIFKIIDNKPSIDSYSKSghkPdNIK 389
Cdd:TIGR01842  246 GAYLAIDGEITPG-------MMIAGSILVGRALAPIDgaiggwkQFSGARQAYKRLNELLANYPSRDPAMPL---P-EPE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    390 GNLEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 469
Cdd:TIGR01842  315 GHLSVENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    470 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 549
Cdd:TIGR01842  394 IGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    550 KILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:TIGR01842  474 KLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
354-622 1.36e-52

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 195.45  E-value: 1.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   354 AFANARGAAYEIFKIIDnkpSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGK 433
Cdd:PRK11174  313 AKAQAVGAAESLVTFLE---TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   434 STtvqLMQRL--YDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 511
Cdd:PRK11174  390 TS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSE 466
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   512 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLST 591
Cdd:PRK11174  467 FLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
                         250       260       270
                  ....*....|....*....|....*....|.
gi 42741659   592 VRNADVIAGFDDGVIVEKGNHDELMKEKGIY 622
Cdd:PRK11174  547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
1032-1263 1.39e-52

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 194.49  E-value: 1.39e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1032 EGNVTFGEVVFnYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1111
Cdd:TIGR01842  314 EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1112 HLGIVSQEPILFDCSIAENIA-YGDNsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARAL 1190
Cdd:TIGR01842  393 HIGYLPQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARAL 469
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   1191 VRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:TIGR01842  470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
392-619 2.89e-52

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 183.30  E-value: 2.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:COG1122    1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPV--LFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 543
Cdd:COG1122   79 LVFQNPDdqLFAPTVEEDVAFGPENlgLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  544 ALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
999-1270 5.39e-52

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 193.52  E-value: 5.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   999 AKAK-ISAAHIIMIIEKTPLIDSYSTEGLM----PNTLEGNvtfGEVVFNyptrPDIPVLQG-LSLEVKKGQTLALVGSS 1072
Cdd:PRK11174  313 AKAQaVGAAESLVTFLETPLAHPQQGEKELasndPVTIEAE---DLEILS----PDGKTLAGpLNFTLPAGQRIALVGPS 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1073 GCGKSTVVQLLERFYdPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEA 1152
Cdd:PRK11174  386 GAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD--ASDEQLQQALENA 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1153 NIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1232
Cdd:PRK11174  463 WVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTH 542
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 42741659  1233 RLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1270
Cdd:PRK11174  543 QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
392-616 1.43e-51

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 190.50  E-value: 1.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 469
Cdd:COG1123  261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 ---IGVVSQEPV--LFAT-TIAENIRYGREN---VTMDEIEKAVKEANA-----YDFIMKLPHkfdtlvgergaQLSGGQ 535
Cdd:COG1123  341 rrrVQMVFQDPYssLNPRmTVGDIIAEPLRLhglLSRAERRERVAELLErvglpPDLADRYPH-----------ELSGGQ 409
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  536 KQRIAIARALVRNPKILLLDEATSALDTESEAVVqvaLD-----KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEK 609
Cdd:COG1123  410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486

                 ....*..
gi 42741659  610 GNHDELM 616
Cdd:COG1123  487 GPTEEVF 493
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
393-604 1.79e-50

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 177.66  E-value: 1.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  393 EFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 472
Cdd:cd03225    1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  473 VSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 548
Cdd:cd03225   80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  549 PKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 604
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
392-615 6.73e-50

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 176.60  E-value: 6.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDIRTINVRF- 465
Cdd:cd03260    1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVl 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  466 -LREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFIMKLPHkfdtlvgerGAQLSGGQKQ 537
Cdd:cd03260   78 eLRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  538 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 615
Cdd:cd03260  149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
392-606 2.57e-49

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 172.79  E-value: 2.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:cd03246    1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03246   80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  552 LLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVI 606
Cdd:cd03246  118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1040-1251 7.32e-48

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 168.55  E-value: 7.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYP-TRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ 1118
Cdd:cd03246    6 VSFRYPgAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1119 EPILFDCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILL 1198
Cdd:cd03246   84 DDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1199 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1251
Cdd:cd03246  120 LDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1040-1264 1.47e-47

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 169.82  E-value: 1.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1119
Cdd:COG1122    6 LSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1120 PI--LFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQ 1193
Cdd:COG1122   84 PDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAGVLAME 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659 1194 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:COG1122  153 PEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1049-1260 2.83e-47

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 168.90  E-value: 2.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPI 1121
Cdd:cd03260   12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLELRRRVGMVFQKPN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1122 LFDCSIAENIAYGDNSRVVSQ----EEIVRAA-KEANIHAfieslpnkystKVGDK--GTQLSGGQKQRIAIARALVRQP 1194
Cdd:cd03260   92 PFPGSIYDNVAYGLRLHGIKLkeelDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQRLCLARALANEP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:cd03260  161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
109-365 3.92e-47

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 170.82  E-value: 3.92e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  109 EDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 188
Cdd:cd18557   33 DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTD 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  189 KIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFG 268
Cdd:cd18557  113 NLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  269 GQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLT-VFFSVLIgAFSVGQ 347
Cdd:cd18557  193 AEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGG 271
                        250
                 ....*....|....*...
gi 42741659  348 ASPSIEAFANARGAAYEI 365
Cdd:cd18557  272 LSSLLADIMKALGASERV 289
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
410-559 8.81e-47

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 164.36  E-value: 8.81e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF-ATTIAENI 488
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659    489 RYGREnvtMDEIEKAVKEANAYDFI--MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 559
Cdd:pfam00005   81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
392-587 8.86e-47

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 166.92  E-value: 8.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:COG4619    1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENI----RYGRENVTMDEIEKAVKEANaydfimkLPHKF-DTLVGErgaqLSGGQKQRIAIARALV 546
Cdd:COG4619   78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 42741659  547 RNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 587
Cdd:COG4619  147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
392-615 9.31e-47

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 167.76  E-value: 9.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI- 469
Cdd:cd03258    2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 --IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTlvgeRGAQLSGGQKQRIAIARA 544
Cdd:cd03258   82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLELLE---LVGLEDKADA----YPAQLSGGQKQRVGIARA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  545 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:cd03258  155 LANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1040-1263 3.00e-46

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 174.71  E-value: 3.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIV 1116
Cdd:COG1123  268 KRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMV 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1117 SQEPIL-FDC--SIAENIAYG-DNSRVVSQEEIVRAAKEAnIHA------FIESLPNkystkvgdkgtQLSGGQKQRIAI 1186
Cdd:COG1123  348 FQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LERvglppdLADRYPH-----------ELSGGQRQRVAI 415
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1187 ARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG1123  416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
392-610 3.73e-46

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 165.76  E-value: 3.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI- 469
Cdd:cd03257    2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 --IGVVSQEPVL-------FATTIAENIRYGRENVTMDEIEKAVKEA-----NAYDFIMKLPHkfdtlvgergaQLSGGQ 535
Cdd:cd03257   82 keIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  536 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:cd03257  151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
392-611 6.67e-46

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 168.72  E-value: 6.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI- 469
Cdd:COG1135    2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 --IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPhkfdtlvgergAQLSGG 534
Cdd:COG1135   82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  535 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVaLDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:COG1135  145 QKQRVGIARALANNPKVLLCDEATSALDPETtRSILDL-LKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223

                 .
gi 42741659  611 N 611
Cdd:COG1135  224 P 224
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1040-1250 3.45e-45

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 162.25  E-value: 3.45e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1119
Cdd:cd03225    5 LSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1120 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQ 1193
Cdd:cd03225   84 PddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1194 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
392-621 5.20e-45

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 163.76  E-value: 5.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    392 LEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-NVRFLREII 470
Cdd:TIGR04520    1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    471 GVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIA 542
Cdd:TIGR04520   80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    543 RALVRNPKILLLDEATSALDTES-EAVVQVALD-KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG------NHDE 614
Cdd:TIGR04520  149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228

                   ....*..
gi 42741659    615 LMKEKGI 621
Cdd:TIGR04520  229 LLKEIGL 235
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
392-608 1.00e-44

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 161.75  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 466
Cdd:COG1136    5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  467 REIIGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYdfiMKLPHKFDTLVgergAQLSGGQKQRIAIAR 543
Cdd:COG1136   85 RRHIGFVFQFFNLLPElTALENVALPLLlaGVSRKERRERARELLER---VGLGDRLDHRP----SQLSGGQQQRVAIAR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  544 ALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVIVE 608
Cdd:COG1136  158 ALVNRPKLILADEPTGNLDSKtGEEVLELLRELNRELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
1051-1251 1.23e-44

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 160.75  E-value: 1.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN 1130
Cdd:COG4619   14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IA--YGDNSRVVSQEEIVRAAKEANihafiesLPNKYSTKvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1208
Cdd:COG4619   94 LPfpFQLRERKFDRERALELLERLG-------LPPDILDK---PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 42741659 1209 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:COG4619  164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
974-1234 1.30e-44

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 170.23  E-value: 1.30e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    974 VLLVFSAvvFGAMAVgqVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEG-NVTFGEVVFNYPTRPdiPV 1052
Cdd:TIGR02868  277 VLLPLAA--FEAFAA--LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PV 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN-- 1130
Cdd:TIGR02868  351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlr 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1131 IAYGDnsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:TIGR02868  431 LARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
                          250       260
                   ....*....|....*....|....
gi 42741659   1211 EKVVQEALDKAREGRTCIVIAHRL 1234
Cdd:TIGR02868  507 ADELLEDLLAALSGRTVVLITHHL 530
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
392-617 1.55e-44

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 161.69  E-value: 1.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 469
Cdd:COG1127    6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 -IGVVSQEPVLF-ATTIAENIRYG-RENVTM--DEIEKAVkeanaydfIMKLphkfdTLVGERGA------QLSGGQKQR 538
Cdd:COG1127   83 rIGMLFQGGALFdSLTVFENVAFPlREHTDLseAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  539 IAIARALVRNPKILLLDEATSALD--TeSEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 614
Cdd:COG1127  150 VALARALALDPEILLYDEPTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228

                 ...
gi 42741659  615 LMK 617
Cdd:COG1127  229 LLA 231
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
392-606 1.58e-44

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 160.73  E-value: 1.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKE-VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 466
Cdd:cd03255    1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  467 REIIGVVSQEPVLFAT-TIAENIRYGrenVTMDEIEKAVKEANAYDFI--MKLPHKFDTLVgergAQLSGGQKQRIAIAR 543
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  544 ALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVI 606
Cdd:cd03255  154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
392-615 2.51e-44

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 160.93  E-value: 2.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFLREI 469
Cdd:COG1126    2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVR 547
Cdd:COG1126   79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELLERVGLADKAD----AYPAQLSGGQQQRVAIARALAM 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  548 NPKILLLDEATSALDTE--SEaVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:COG1126  154 EPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
392-617 3.20e-44

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 160.36  E-value: 3.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 469
Cdd:cd03261    1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 -IGVVSQEPVLF-ATTIAENIRYG-RENVTMDE--IEKAVKeanaydfiMKLphkfdTLVGERG------AQLSGGQKQR 538
Cdd:cd03261   78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  539 IAIARALVRNPKILLLDEATSALD-TESEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:cd03261  145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224

                 ..
gi 42741659  616 MK 617
Cdd:cd03261  225 RA 226
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1036-1256 3.63e-44

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 159.11  E-value: 3.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1036 TFGEV-VFNYPTR--PDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1111
Cdd:cd03369    3 EHGEIeVENLSVRyaPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAakeanihafieslpnkysTKVGDKGTQLSGGQKQRIAIARALV 1191
Cdd:cd03369   83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1192 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:cd03369  142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
392-616 4.04e-44

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 168.54  E-value: 4.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT---EGMVSVDGQDIRTINVRFLRE 468
Cdd:COG1123    5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 IIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPHKFDtlvgERGAQLSGGQKQRIAIARA 544
Cdd:COG1123   84 RIGMVFQDPmtQLNPVTVGDQIAEALENlgLSRAEARARVLELLE---AVGLERRLD----RYPHQLSGGQRQRVAIAMA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  545 LVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELM 616
Cdd:COG1123  157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
392-618 6.50e-44

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 159.46  E-value: 6.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRfLREIIG 471
Cdd:COG1131    1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRN 548
Cdd:COG1131   77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  549 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:COG1131  150 PELLILDEPTSGLDPEArRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
390-610 1.04e-43

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 157.96  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  390 GNLEFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 469
Cdd:cd03369    5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFATTIAENI-RYGREnvTMDEIEKAVKeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:cd03369   84 LTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  549 PKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 610
Cdd:cd03369  144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1035-1255 1.07e-43

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 156.70  E-value: 1.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLG 1114
Cdd:cd03247    1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILFDCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkGTQLSGGQKQRIAIARALVRQP 1194
Cdd:cd03247   79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1255
Cdd:cd03247  118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
392-610 2.71e-43

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 155.55  E-value: 2.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINvRFLREIIG 471
Cdd:cd03247    1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03247   79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  552 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 610
Cdd:cd03247  120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
392-587 3.12e-43

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 156.86  E-value: 3.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiI 470
Cdd:cd03293    1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANA----YDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 543
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYPH-----------QLSGGMRQRVALAR 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 42741659  544 ALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 587
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1046-1255 3.89e-43

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 156.53  E-value: 3.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILFD- 1124
Cdd:cd03259    9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1125 CSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:cd03259   87 LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPH-------ELSGGQQQRVALARALAREPSLLLLDEPLS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1205 ALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1255
Cdd:cd03259  160 ALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
54-348 5.51e-43

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 158.95  E-value: 5.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   54 GTLAAIIHGAGLPLMMLVFGEMTDIfanagnledlmsnITNRSDINDTGffmnLEEDMTRYAYYYSGIGAGVLVAAYIQV 133
Cdd:cd18780    1 GTIALLVSSGTNLALPYFFGQVIDA-------------VTNHSGSGGEE----ALRALNQAVLILLGVVLIGSIATFLRS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  134 SFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWK 213
Cdd:cd18780   64 WLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  214 LTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAI 293
Cdd:cd18780  144 LTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLAR 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  294 TANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFfsvLIGAFSVGQA 348
Cdd:cd18780  224 ASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSF---LLYTLTVAMS 274
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
392-587 6.18e-43

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 157.56  E-value: 6.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiI 470
Cdd:COG1116    8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFA-TTIAENIRYGRENVTMDEiEKAVKEANAY-------DFIMKLPHkfdtlvgergaQLSGGQKQRIAIA 542
Cdd:COG1116   83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYPH-----------QLSGGMRQRVAIA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659  543 RALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 587
Cdd:COG1116  151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
392-617 6.38e-43

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 157.27  E-value: 6.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREII 470
Cdd:COG1124    2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEP---------VlfATTIAENIRYGRENVTMDEIEKAVKEAN-AYDFIMKLPHkfdtlvgergaQLSGGQKQRIA 540
Cdd:COG1124   82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  541 IARALVRNPKILLLDEATSALDteseAVVQVA-LD-----KARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHD 613
Cdd:COG1124  149 IARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224

                 ....
gi 42741659  614 ELMK 617
Cdd:COG1124  225 DLLA 228
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
392-610 2.76e-42

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 154.21  E-value: 2.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIG 471
Cdd:cd03259    1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:cd03259   76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEG----LLNRYPHELSGGQQQRVALARALARE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  549 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 610
Cdd:cd03259  149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1040-1253 2.90e-42

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 154.43  E-value: 2.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPT-RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGKVLLDGKEIKRLN----VQWLRA 1111
Cdd:COG1136   10 LTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelARLRRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQEPILFDC-SIAENIA----YGDNSRVVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAI 1186
Cdd:COG1136   87 HIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAI 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1253
Cdd:COG1136  156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1044-1255 3.65e-42

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 154.20  E-value: 3.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1044 YPTRPD-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL---RAHLGIVSQE 1119
Cdd:cd03257   11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1120 PI-----LFdcSIAENIA-----YGDNSRvvsQEEIVRAAKEANIH-----AFIESLPNkystkvgdkgtQLSGGQKQRI 1184
Cdd:cd03257   91 PMsslnpRM--TIGEQIAeplriHGKLSK---KEARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQRQRV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1185 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:cd03257  155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
392-616 4.48e-42

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 154.38  E-value: 4.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:cd03295    1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFA-TTIAENI-------RYGREnvtmdEIEKAVKEANAydfIMKLPHKfdTLVGERGAQLSGGQKQRIAIAR 543
Cdd:cd03295   79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  544 ALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRL-STVRNADVIAGFDDGVIVEKGNHDELM 616
Cdd:cd03295  149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1035-1253 7.45e-42

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 153.01  E-value: 7.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPT-RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlrAHL 1113
Cdd:cd03293    1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1114 GIVSQEPILFD-CSIAENIAYGDNSRVVSqeeivRAAKEANIHAFIEslpnkystKVGDKGT------QLSGGQKQRIAI 1186
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLELQGVP-----KAEARERAEELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQN--GRVKE 1253
Cdd:cd03293  143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
109-333 7.83e-42

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 155.39  E-value: 7.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  109 EDMTRYAYYYSGIGAGVLVAAYIQVsfWCLA-AGRQIHK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGI 186
Cdd:cd18572   33 EAFYRAVLLLLLLSVLSGLFSGLRG--GCFSyAGTRLVRrLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  187 GDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIA 266
Cdd:cd18572  111 STNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRS 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  267 FGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLT 333
Cdd:cd18572  191 FATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVT 257
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1049-1256 8.72e-42

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 157.18  E-value: 8.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSI 1127
Cdd:COG3842   17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFpHLTV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:COG3842   95 AENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALARALAPEPRVLLLDEPL 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1204 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGT 1256
Cdd:COG3842  164 SALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1053-1204 9.74e-42

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 150.11  E-value: 9.74e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILF-DCSIAENI 1131
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   1132 AYGDNSrvvsqEEIVRAAKEANIHAFIE--SLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:pfam00005   81 RLGLLL-----KGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
392-604 2.00e-41

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 150.42  E-value: 2.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRT--INVRFLREI 469
Cdd:cd03229    1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFAT-TIAENIRYGrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRN 548
Cdd:cd03229   78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  549 PKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 604
Cdd:cd03229  119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
392-618 2.46e-41

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 154.83  E-value: 2.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TEGMVSVDGQDIRTINVRFLR 467
Cdd:COG0444    2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  468 EI----IGVVSQEPvlFA---------TTIAENIRYgRENVTMDEIEKAVKEA-------NAYDFIMKLPHkfdtlvger 527
Cdd:COG0444   82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPH--------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  528 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQVA-LD-----KARKGRTTIVIAHRLSTVRN-ADVIA- 599
Cdd:COG0444  150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
                        250       260
                 ....*....|....*....|.
gi 42741659  600 --GfddGVIVEKGNHDELMKE 618
Cdd:COG0444  224 myA---GRIVEEGPVEELFEN 241
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1034-1262 2.52e-41

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 152.65  E-value: 2.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1034 NVTFGevvfnyPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1113
Cdd:COG1124    8 SVSYG------QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1114 GIVSQEPIL-------FDCSIAE--NIAYGDNSrvvsQEEIVRAAKEANIH-AFIESLPNkystkvgdkgtQLSGGQKQR 1183
Cdd:COG1124   82 QMVFQDPYAslhprhtVDRILAEplRIHGLPDR----EERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1184 IAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:COG1124  147 VAIARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222

                 ....*.
gi 42741659 1257 HQQLLA 1262
Cdd:COG1124  223 VADLLA 228
PLN03232 PLN03232
ABC transporter C family member; Provisional
114-645 2.80e-41

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 166.30  E-value: 2.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   114 YAYYYSGIGAGvLVAAYIQVSFW----CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDK 189
Cdd:PLN03232  952 YIVVYALLGFG-QVAVTFTNSFWlissSLHAAKRLHD---AMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANL 1027
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   190 IGMFFQSMATFFTGFIVgftRGWKLTLVILAISPVLGLSAAVW---------AKILSSFTDKELlaYAKAGavaeEVLAA 260
Cdd:PLN03232 1028 MNMFMNQLWQLLSTFAL---IGTVSTISLWAIMPLLILFYAAYlyyqstsreVRRLDSVTRSPI--YAQFG----EALNG 1098
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   261 IRTVIAFGGQKKELERYNKNLEEAKRIGIKkAITAN-------ISIGAAFLLIYASYALaFWYGTT-----------LVL 322
Cdd:PLN03232 1099 LSSIRAYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAV-LRNGNAenqagfastmgLLL 1176
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   323 SGEYSIGQVLTvffSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGhkpdnikgNLEFRNVHFSYp 402
Cdd:PLN03232 1177 SYTLNITTLLS---GVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY- 1244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   403 sRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFA 481
Cdd:PLN03232 1245 -RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENIRYGRENVTMDeIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 561
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   562 DTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELM-KEKGIYFKLVTMQTAGNEVELENA 640
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHSTGPANAQYLSNL 1482

                  ....*
gi 42741659   641 ADESK 645
Cdd:PLN03232 1483 VFERR 1487
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
392-606 4.63e-41

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 150.37  E-value: 4.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFLREI 469
Cdd:cd03262    1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFA-TTIAENIRYGRENVT-MDEIEKavkEANAYDFIMK--LPHKFDtlvgERGAQLSGGQKQRIAIARAL 545
Cdd:cd03262   78 VGMVFQQFNLFPhLTVLENITLAPIKVKgMSKAEA---EERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARAL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  546 VRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 606
Cdd:cd03262  151 AMNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
51-365 8.82e-41

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 152.70  E-value: 8.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   51 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSnitnrsdindtgffmnleedmtrYAYYYSGIGAGVLVAAY 130
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLW-----------------------IALLLLLLALLRALLSY 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  131 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 210
Cdd:cd07346   58 LRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  211 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 290
Cdd:cd07346  138 NWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  291 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFSVLIGAFS-VGQASPSIEAFANARGAAYEI 365
Cdd:cd07346  218 AARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLAYLGMLFGpIQRLANLYNQLQQALASLERI 292
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1049-1263 9.82e-41

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 150.53  E-value: 9.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILF 1123
Cdd:COG1126   13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 -DCSIAENIAYGdnSRVV---SQEEIVRAAKEanihafieslpnkYSTKVG--DKG----TQLSGGQKQRIAIARALVRQ 1193
Cdd:COG1126   90 pHLTVLENVTLA--PIKVkkmSKAEAEERAME-------------LLERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1194 PHILLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG1126  155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1040-1263 1.28e-40

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 158.14  E-value: 1.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGKVLLDGKEIKRLNVQWLRAHLGIV 1116
Cdd:COG1123   10 LSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRRIGMV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1117 SQEPI--LFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQP 1194
Cdd:COG1123   89 FQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMALALDP 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG1123  162 DLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
392-608 1.80e-40

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 149.05  E-value: 1.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN---VRFLRE 468
Cdd:COG2884    2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 IIGVVSQE-PVLFATTIAENIRY-----GRENvtmDEIEKAVKEAnaydfIMK--LPHKFDTLVgergAQLSGGQKQRIA 540
Cdd:COG2884   80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  541 IARALVRNPKILLLDEATSALDTE-SEAVVQVaLDKARKGRTTIVIA-HRLSTVRNAD--VIAgFDDGVIVE 608
Cdd:COG2884  148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1034-1261 2.46e-40

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 149.81  E-value: 2.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1034 NVTFGevvfnYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1113
Cdd:COG1120    6 NLSVG-----YGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1114 GIVSQEPIL-FDCSIAENIAYG-----DNSRVVSQE--EIVRAA-KEANIHAFIE-SLpnkystkvgdkgTQLSGGQKQR 1183
Cdd:COG1120   78 AYVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLADrPV------------DELSGGERQR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1184 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:COG1120  146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225

                 .
gi 42741659 1261 L 1261
Cdd:COG1120  226 L 226
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
711-1008 2.60e-40

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 151.16  E-value: 2.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTriddPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 790
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVI----PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  791 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 870
Cdd:cd07346   77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  871 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 950
Cdd:cd07346  155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  951 FSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHI 1008
Cdd:cd07346  235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
392-618 2.92e-40

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 149.81  E-value: 2.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:COG1120    2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVL-FATTIAENIRYGR---------ENVTMDEI-EKAVKEANAYDFIMKLphkFDTlvgergaqLSGGQKQRIA 540
Cdd:COG1120   79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  541 IARALVRNPKILLLDEATSALDteseavV--QVA-LD-----KARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGN 611
Cdd:COG1120  148 IARALAQEPPLLLLDEPTSHLD------LahQLEvLEllrrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221

                 ....*..
gi 42741659  612 HDELMKE 618
Cdd:COG1120  222 PEEVLTP 228
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
393-604 3.97e-40

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 145.85  E-value: 3.97e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  393 EFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 472
Cdd:cd00267    1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  473 VSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 552
Cdd:cd00267   78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659  553 LLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNA-DVIAGFDDG 604
Cdd:cd00267  103 LLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
392-610 5.62e-40

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 152.17  E-value: 5.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFlrei 469
Cdd:COG3842    6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtgLPPEKRN---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALV 546
Cdd:COG3842   79 VGMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVALARALA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  547 RNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLS---TVrnADVIAGFDDGVIVEKG 610
Cdd:COG3842  152 PEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1040-1253 7.08e-40

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 148.70  E-value: 7.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLnvqwlRAHLGIVSQ 1118
Cdd:COG1116   13 VSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDRGVVFQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1119 EPILFD-CSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQ 1193
Cdd:COG1116   88 EPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIARALAND 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1194 PHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVFQN--GRVKE 1253
Cdd:COG1116  157 PEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
120-625 2.27e-39

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 160.11  E-value: 2.27e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    120 GIGAGVLVAAY-IQVSFWCLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMA 198
Cdd:TIGR00957 1015 GILQGFAVFGYsMAVSIGGIQASRVLHQ---DLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLF 1091
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    199 TFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKilSSFTDKELLAYAKAGAVAE--EVLAAIRTVIAFGGQKKELER 276
Cdd:TIGR00957 1092 NVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA--SSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQ 1169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    277 YNKNLEEAKRiGIKKAITAN--ISIGAAFL-----LIYASYALAFWYGTTLVLSGeysigqvLTVFFSVLIGAFSVGQAS 349
Cdd:TIGR00957 1170 SDLKVDENQK-AYYPSIVANrwLAVRLECVgncivLFAALFAVISRHSLSAGLVG-------LSVSYSLQVTFYLNWLVR 1241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    350 PSIEAFANArgAAYEIFKIIDNKPSIDSYSKSGHKPDNI---KGNLEFRNVHFSYpsRKEVK-ILKGLNLKVQSGQTVAL 425
Cdd:TIGR00957 1242 MSSEMETNI--VAVERLKEYSETEKEAPWQIQETAPPSGwppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGI 1317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    426 VGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI----RYGRENVTMdeie 501
Cdd:TIGR00957 1318 VGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEVWW---- 1393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    502 kAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRT 581
Cdd:TIGR00957 1394 -ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT 1472
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 42741659    582 TIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKL 625
Cdd:TIGR00957 1473 VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1046-1263 2.91e-39

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 146.19  E-value: 2.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQE 1119
Cdd:cd03258   14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1120 PILFDC-SIAENIAYgdnsrvvsQEEIVRAAKeANIHAFIESLPN--KYSTKVGDKGTQLSGGQKQRIAIARALVRQPHI 1196
Cdd:cd03258   91 FNLLSSrTVFENVAL--------PLEIAGVPK-AEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1197 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:cd03258  162 LLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
399-1272 7.78e-39

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 158.54  E-value: 7.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    399 FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrflreiIGVVSQEPV 478
Cdd:TIGR01271  431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    479 LFATTIAENIRYGrenVTMDEIE--KAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 556
Cdd:TIGR01271  498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    557 ATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIY------------ 622
Cdd:TIGR01271  575 PFTHLDvvTEKE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdn 653
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    623 -------------------------------------------------------------FKLV--TMQTAgNEVELEN 639
Cdd:TIGR01271  654 fsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVqmGPQKA-QATTIED 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    640 AADE--------------------------------SKSEIDALEMSSNDSRSSLIRKR---STRRSVRGSQAQD----- 679
Cdd:TIGR01271  733 AVREpserkfslvpedeqgeeslprgnqyhhglqhqAQRRQSVLQLMTHSNRGENRREQlqtSFRKKSSITQQNElasel 812
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    680 ----RKLSTKEALD------------------ESIPPVSFWR------IMKLNLTEWPYFVVGVFCAIINGGLQPAFaII 731
Cdd:TIGR01271  813 diysRRLSKDSVYEiseeineedlkecfaderENVFETTTWNtylryiTTNRNLVFVLIFCLVIFLAEVAASLLGLW-LI 891
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    732 FSKIIGVFTRIDDPETKRQNSNLFSLL-------------------FLALGiisfitfFLQGFTFGKAGEILTKRLRYMV 792
Cdd:TIGR01271  892 TDNPSAPNYVDQQHANASSPDVQKPVIitptsayyifyiyvgtadsVLALG-------FFRGLPLVHTLLTVSKRLHEQM 964
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    793 FRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIGSRLAVITQ-NIANLGTGIIISFIYGWqltlLLLAIVPIIAIA 871
Cdd:TIGR01271  965 LHSVLQAPMAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIF 1038
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    872 GVVEMKML-SGQALKdKKELEGSGKIATEAIENFR---TVVSLTQEQKFEHMYAQSLQVPYRN-----------SLRKAH 936
Cdd:TIGR01271 1039 IMLRAYFLrTSQQLK-QLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwflylstlrwfQMRIDI 1117
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    937 IFGITFSftqAMMYFSYA----GCFRFGAYL-VAHKLMSFEDVLLVFSAVVFGAM-AVGQVSSF---APDYAKAKISAAH 1007
Cdd:TIGR01271 1118 IFVFFFI---AVTFIAIGtnqdGEGEVGIILtLAMNILSTLQWAVNSSIDVDGLMrSVSRVFKFidlPQEEPRPSGGGGK 1194
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1008 I----IMIIEKTPLIDSYSTEGLMpntlegnvTFGEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1083
Cdd:TIGR01271 1195 YqlstVLVIENPHAQKCWPSGGQM--------DVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL 1265
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1084 ERFYDPlAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHAFIESLPN 1163
Cdd:TIGR01271 1266 LRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPD 1341
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1164 KYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1243
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF 1421
                         1050      1060
                   ....*....|....*....|....*....
gi 42741659   1244 VVFQNGRVKEHGTHQQLLAQKGIYFSMVS 1272
Cdd:TIGR01271 1422 LVIEGSSVKQYDSIQKLLNETSLFKQAMS 1450
PTZ00243 PTZ00243
ABC transporter; Provisional
408-1271 1.32e-38

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 157.63  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   408 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVsvdgqdirtinvrFLREIIGVVSQEPVLFATTIAEN 487
Cdd:PTZ00243  674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGN 740
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   488 IRYGRENVTMDeIEKAVK----EANaydfIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 563
Cdd:PTZ00243  741 ILFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   564 E-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMkEKGIYFKLvTMQTAGNEVELENAAD 642
Cdd:PTZ00243  816 HvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL-AAELKENKDSKEGDAD 893
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   643 ESKSEIDALE--MSSNDSRSSLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPvsfWRimklnlTEWPYFVvgvFCaii 720
Cdd:PTZ00243  894 AEVAEVDAAPggAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVP---WS------TYVAYLR---FC--- 958
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   721 nGGLQPAFAIIFSKIIGVFTRID----------DPETKRQNSNLFSLLFLA-LGIISFITFFLQGFTFGKAGeilTKRLR 789
Cdd:PTZ00243  959 -GGLHAAGFVLATFAVTELVTVSsgvwlsmwstRSFKLSAATYLYVYLGIVlLGTFSVPLRFFLSYEAMRRG---SRNMH 1034
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   790 YMVFRSMLRQDVSWFDdpknTT--GALTTRLANDAaqvkGAIGSRLAVITQNIANLGTGIIIS-FIYGWQLTLLLLAIVP 866
Cdd:PTZ00243 1035 RDLLRSVSRGTMSFFD----TTplGRILNRFSRDI----DILDNTLPMSYLYLLQCLFSICSSiLVTSASQPFVLVALVP 1106
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   867 ------------------IIAIAGVVEMKMLS--GQALKDKKELEGSGK---IATEAIENFRTVVSLTQEQKFEHMYAqS 923
Cdd:PTZ00243 1107 cgylyyrlmqfynsanreIRRIKSVAKSPVFTllEEALQGSATITAYGKahlVMQEALRRLDVVYSCSYLENVANRWL-G 1185
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   924 LQVPY---------------RNSLRKAH--IFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAM 986
Cdd:PTZ00243 1186 VRVEFlsnivvtvialigviGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDM 1265
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   987 AvgQVSSFAPDYAKAKISAAHIImiieKTPLIDSYSTEGLMPNTLE-GNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQ 1064
Cdd:PTZ00243 1266 P--ELDEEVDALERRTGMAADVT----GTVVIEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPRE 1337
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1065 TLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEE 1144
Cdd:PTZ00243 1338 KVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAE 1414
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1145 IVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALV-RQPHILLLDEATSALDTESEKVVQEALDKARE 1223
Cdd:PTZ00243 1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFS 1494
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*....
gi 42741659  1224 GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL-LAQKGIYFSMV 1271
Cdd:PTZ00243 1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
393-610 1.79e-38

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 147.25  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   393 EFRNVHFSYP-SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 469
Cdd:PRK11153    3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 -IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPhkfdtlvgergAQLSGGQ 535
Cdd:PRK11153   83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659   536 KQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:PRK11153  146 KQRVAIARALASNPKVLLCDEATSALDPAtTRSILELLKDINRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1051-1271 1.80e-38

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 144.67  E-value: 1.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN 1130
Cdd:cd03288   35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IaygDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:cd03288  115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1211 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK-GIYFSMV 1271
Cdd:cd03288  192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
1040-1264 1.95e-38

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 144.88  E-value: 1.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1040 VVFNYPtRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-RLNVQWLRAHLGIVSQ 1118
Cdd:TIGR04520    6 VSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKVGMVFQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1119 EPilfD----CSIAEN-IAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARA 1189
Cdd:TIGR04520   85 NP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRVAIAGV 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   1190 LVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:TIGR04520  151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
392-615 2.41e-38

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 144.41  E-value: 2.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD--P---TEGMVSVDGQDI--RTINVR 464
Cdd:COG1117   12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  465 FLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFImklphKfDTLvGERGAQLSGGQKQ 537
Cdd:COG1117   89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-----K-DRL-KKSALGLSGGQQQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  538 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKgRTTIVI-------AHRLStvrnaDVIAGFDDGVIVEKG 610
Cdd:COG1117  162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235

                 ....*
gi 42741659  611 NHDEL 615
Cdd:COG1117  236 PTEQI 240
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1046-1250 2.91e-38

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 141.17  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN--VQWLRAHLGIVSQEPILF 1123
Cdd:cd03229    9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 -DCSIAENIAYGdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:cd03229   89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1203 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:cd03229  128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
109-349 3.03e-38

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 145.35  E-value: 3.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  109 EDMTRYAYYYSGIGAGVLV----AAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE 184
Cdd:cd18573   34 EIFGLSLKTFALALLGVFVvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGK 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  185 GIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTV 264
Cdd:cd18573  114 SLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTV 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  265 IAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVF--FSVLIGA 342
Cdd:cd18573  194 RAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSFlmYAVYVGS 272

                 ....*..
gi 42741659  343 fSVGQAS 349
Cdd:cd18573  273 -SVSGLS 278
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1049-1263 3.88e-38

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 142.90  E-value: 3.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlRAHLGIVSQEPILF-DCSI 1127
Cdd:COG1131   12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEAnIHAFieSLPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:COG1131   91 RENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1208 TESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG1131  164 PEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
392-620 5.30e-38

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 142.69  E-value: 5.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIiG 471
Cdd:COG4555    2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRN 548
Cdd:COG4555   78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  549 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 620
Cdd:COG4555  151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
392-606 6.30e-38

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 140.23  E-value: 6.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 471
Cdd:cd03230    1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRYgrenvtmdeiekavkeanaydfimklphkfdtlvgergaqlSGGQKQRIAIARALVRNPK 550
Cdd:cd03230   77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  551 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 606
Cdd:cd03230  116 LLILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1049-1260 7.69e-38

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 142.87  E-value: 7.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--PLA---GKVLLDGKEI--KRLNVQWLRAHLGIVSQEPI 1121
Cdd:COG1117   23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQKPN 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1122 LFDCSIAENIAYG-----DNSRVVsQEEIVRAA-KEANihafiesLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPH 1195
Cdd:COG1117  103 PFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPE 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1196 ILLLDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVFQNGRVKEHGTHQQL 1260
Cdd:COG1117  175 VLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
392-604 1.10e-37

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 140.68  E-value: 1.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKEV--KILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLyDPTEGMVSVDGQdirtinvrflre 468
Cdd:cd03250    1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 iIGVVSQEPVLFATTIAENIRYGREnvtMDEIE-KAVKEANA--YDFIMkLPHKFDTLVGERGAQLSGGQKQRIAIARAL 545
Cdd:cd03250   68 -IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  546 VRNPKILLLDEATSALDTESEAVV--QVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDG 604
Cdd:cd03250  143 YSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
714-1006 1.15e-37

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 143.47  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  714 GVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPEtkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVF 793
Cdd:cd18557    1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD----VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  794 RSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGV 873
Cdd:cd18557   77 SSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  874 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 950
Cdd:cd18557  155 IygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  951 FSYAGCFRFGAYLVAHK------LMSFedvlLVFSAVVfgAMAVGQVSSFAPDYAKAkISAA 1006
Cdd:cd18557  232 LSLLLVLWYGGYLVLSGqltvgeLTSF----ILYTIMV--ASSVGGLSSLLADIMKA-LGAS 286
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
392-607 1.38e-37

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 141.73  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 469
Cdd:COG3638    3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 -IGVVSQEPVLFA-TTIAENI---RYGREN--------VTMDEIEKAvkeanaYDFIMK--LPHKFDtlvgERGAQLSGG 534
Cdd:COG3638   81 rIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllglFPPEDRERA------LEALERvgLADKAY----QRADQLSGG 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  535 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKAR-KGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 607
Cdd:COG3638  151 QQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
392-562 1.59e-37

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 144.83  E-value: 1.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFlREIiG 471
Cdd:COG3839    4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLF-ATTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:COG3839   79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLED----LLDRKPKQLSGGQRQRVALGRALVRE 151
                        170
                 ....*....|....
gi 42741659  549 PKILLLDEATSALD 562
Cdd:COG3839  152 PKVFLLDEPLSNLD 165
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1035-1262 1.87e-37

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 141.28  E-value: 1.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1114
Cdd:cd03295    1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILF-DCSIAENIAYGDNSRVVSQEEIVRAAKE--ANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALV 1191
Cdd:cd03295   79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADEllALVGLDPAEFADRYP-------HELSGGQQQRVGVARALA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1192 RQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:cd03295  152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1039-1250 1.97e-37

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 138.15  E-value: 1.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1039 EVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ 1118
Cdd:cd00267    4 NLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1119 epilfdcsiaeniaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILL 1198
Cdd:cd00267   81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1199 LDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGR 1250
Cdd:cd00267  104 LDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
393-621 2.75e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 141.67  E-value: 2.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   393 EFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 472
Cdd:PRK13632    9 KVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   473 VSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIARA 544
Cdd:PRK13632   88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659   545 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKG-RTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGI 621
Cdd:PRK13632  157 LALNPEIIIFDESTSMLDPKGkREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1044-1256 7.28e-37

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 142.52  E-value: 7.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1044 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGKVLLDGKEIKRLNVQWLRA---HLGIV 1116
Cdd:COG1135   11 FPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1117 SQEPILFD-CSIAENIAY-----GdnsrvVSQEEIVRAAKEanihaFIESlpnkystkVG--DKG----TQLSGGQKQRI 1184
Cdd:COG1135   88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEIRKRVAE-----LLEL--------VGlsDKAdaypSQLSGGQKQRV 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1185 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:COG1135  150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1037-1266 1.14e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 140.13  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1037 FGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIV 1116
Cdd:PRK13632   10 VENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1117 SQEPilfD-----CSIAENIAYGDNSRVVSQEE----IVRAAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIA 1187
Cdd:PRK13632   89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1188 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1265
Cdd:PRK13632  155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234

                  .
gi 42741659  1266 I 1266
Cdd:PRK13632  235 I 235
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1051-1262 1.52e-36

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 138.57  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV---QWLRAHLGIVSQEPILFDC-S 1126
Cdd:COG1127   19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 IAENIAYG-DNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:COG1127   99 VFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1202 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:COG1127  168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
392-619 1.58e-36

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 138.47  E-value: 1.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 469
Cdd:cd03256    1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 -IGVVSQEPVLFA-TTIAENIRYGR-----------ENVTMDEIEKAVKEANAYDFimklphkfDTLVGERGAQLSGGQK 536
Cdd:cd03256   79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGL--------LDKAYQRADQLSGGQQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  537 QRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKAR-KGRTTIVIAHRLSTVR-NADVIAGFDDGVIVEKGNHD 613
Cdd:cd03256  151 QRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINReEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230

                 ....*.
gi 42741659  614 ELMKEK 619
Cdd:cd03256  231 ELTDEV 236
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
404-618 1.71e-36

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 141.41  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  404 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI---IGVVSQEPvlF 480
Cdd:COG4608   28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  481 A---------TTIAENIRYgRENVTMDEIEKAVKEA------NAyDFIMKLPHKFdtlvgergaqlSGGQKQRIAIARAL 545
Cdd:COG4608  106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARAL 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  546 VRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:COG4608  173 ALNPKLIVCDEPVSALDVSIQAqVLNLLEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1035-1250 5.87e-36

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 135.67  E-value: 5.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPTRPDI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPLAGKVLLDGKeikrlnvqwlr 1110
Cdd:cd03250    1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1111 ahLGIVSQEPILFDCSIAENIAYG---DNSRVvsqEEIVRAAkeanihAF---IESLPNKYSTKVGDKGTQLSGGQKQRI 1184
Cdd:cd03250   68 --IAYVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKAC------ALepdLEILPDGDLTEIGEKGINLSGGQKQRI 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1185 AIARALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVFQNGR 1250
Cdd:cd03250  137 SLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1040-1262 1.06e-35

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 136.09  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV---QWLRAHLGIV 1116
Cdd:cd03261    6 LTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRMGML 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1117 SQEPILFDC-SIAENIAYG--DNSRvVSQEEIVRAAKE----ANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARA 1189
Cdd:cd03261   83 FQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVLEkleaVGLRGAEDLYP-----------AELSGGMKKRVALARA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1190 LVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:cd03261  151 LALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1057-1263 1.13e-35

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 137.00  E-value: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1057 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA----HLGIVSQEPILF-DCSIAENI 1131
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1132 AYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:cd03294  124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1208 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:cd03294  193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1052-1261 1.32e-35

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 135.54  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAEN 1130
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:cd03299   92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR-------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1211 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:cd03299  165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1049-1260 1.32e-35

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 135.44  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIkrLNVQWLRAHLGIVSQEPILF-DCSI 1127
Cdd:cd03300   12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:cd03300   90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1208 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:cd03300  163 LKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1040-1251 1.56e-35

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 134.92  E-value: 1.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRPD-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHLG 1114
Cdd:cd03255    6 LSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQE----PILfdcSIAENIAYGDNSRVVSQEEIVRAAKEAnihafIES--LPNKYSTKVGdkgtQLSGGQKQRIAIAR 1188
Cdd:cd03255   86 FVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQRVAIAR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1189 ALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVFQNGRV 1251
Cdd:cd03255  154 ALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1040-1263 1.79e-35

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 136.68  E-value: 1.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1040 VVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1119
Cdd:PRK13635   11 ISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1120 PilfD-----CSIAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARAL 1190
Cdd:PRK13635   90 P---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1191 VRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK13635  156 ALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
PLN03130 PLN03130
ABC transporter C family member; Provisional
117-666 2.09e-35

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 147.58  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   117 YYSGIGAGVlvaAYIQV------SFW----CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGI 186
Cdd:PLN03130  954 FYNLIYALL---SFGQVlvtllnSYWlimsSLYAAKRLHD---AMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV 1027
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   187 GDKIGMF----FQSMATFFtgfIVGFTRgwklTLVILAISPVLGL---------SAAVWAKILSSFTDKELlaYAKAGav 253
Cdd:PLN03130 1028 AVFVNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLfygaylyyqSTAREVKRLDSITRSPV--YAQFG-- 1096
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   254 aeEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIkkaitANIS-----------IGAAFLLIYASYAL---------- 312
Cdd:PLN03130 1097 --EALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTL-----VNMSsnrwlairletLGGLMIWLTASFAVmqngraenqa 1169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   313 AFWYGTTLVLSGEYSIGQVLTvffSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGhkpdnikgNL 392
Cdd:PLN03130 1170 AFASTMGLLLSYALNITSLLT---AVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSG--------SI 1238
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   393 EFRNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PLN03130 1239 KFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   552 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL-MKEKGIYFKLVTMQT 630
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQSTG 1475
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 42741659   631 AGNEVELENAADESKSEidalEMSSNDSRSSLIRKR 666
Cdd:PLN03130 1476 AANAQYLRSLVFGGDED----RLAREESKALDGQRK 1507
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1049-1265 2.13e-35

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 135.37  E-value: 2.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvQWLRAHLGIVSQEPILFD-CSI 1127
Cdd:COG4555   13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPDERGLYDrLTV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEAnIHAFIesLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:COG4555   92 RENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1208 TESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1265
Cdd:COG4555  165 VMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
414-616 3.02e-35

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 135.85  E-value: 3.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  414 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI----IGVVSQEPVLFA-TTIAENI 488
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  489 RYGRENVTMDEIEKAVKEANAY------DFIMKLPHkfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:cd03294  124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  563 TESEAVVQVALDK--ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 616
Cdd:cd03294  193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
392-616 4.90e-35

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 134.06  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNV--HFSypsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIR--TINVRFLR 467
Cdd:PRK09493    2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   468 EIIGVVSQEPVLFATTIA-ENIRYGRENVtmdeieKAVKEANAYDFIMKLPHKfdtlVG--ERG----AQLSGGQKQRIA 540
Cdd:PRK09493   77 QEAGMVFQQFYLFPHLTAlENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659   541 IARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELM 616
Cdd:PRK09493  147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1049-1251 5.79e-35

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 133.04  E-value: 5.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILF-DC 1125
Cdd:cd03262   12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 SIAENIAYGD-NSRVVSQEEIVRAAKEanihafieslpnkYSTKVG--DKGT----QLSGGQKQRIAIARALVRQPHILL 1198
Cdd:cd03262   92 TVLENITLAPiKVKGMSKAEAEERALE-------------LLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVML 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1199 LDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:cd03262  159 FDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
392-586 7.44e-35

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 132.92  E-value: 7.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI---RTINVRFLRE 468
Cdd:cd03292    1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 IIGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLvgerGAQLSGGQKQRIAIARAL 545
Cdd:cd03292   79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 42741659  546 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIA 586
Cdd:cd03292  152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
727-995 8.84e-35

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 135.33  E-value: 8.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  727 AFAIIFSKIIGVFT-RIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFD 805
Cdd:cd18573   14 SVPFAIGKLIDVASkESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  806 dpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALK 885
Cdd:cd18573   94 --KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQ 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  886 DKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVA 965
Cdd:cd18573  172 VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA 251
                        250       260       270
                 ....*....|....*....|....*....|
gi 42741659  966 HklmsfedvllvfsavvfGAMAVGQVSSFA 995
Cdd:cd18573  252 S-----------------GELTVGDLTSFL 264
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
147-362 2.20e-34

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 133.76  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  147 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLG 226
Cdd:cd18576   71 LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  227 LSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLI 306
Cdd:cd18576  151 LVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  307 YASYALAFWYGTTLVLSGEYSIGQVLT-VFFSVLIGAfSVGQASPSIEAFANARGAA 362
Cdd:cd18576  231 FGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
392-616 2.24e-34

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 139.82  E-value: 2.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRK--------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLyDPTEGMVSVDGQDIRTIN- 462
Cdd:COG4172  276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  463 --VRFLREIIGVVSQEPvlFAT-----TIAENIRYG----RENVTMDEIEKAVKEA-----------NAYdfimklPHKF 520
Cdd:COG4172  355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  521 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQ---VALDK---ARKGRTTIVIAHRLSTVRN 594
Cdd:COG4172  427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqiLDLLRdlqREHGLAYLFISHDLAVVRA 491
                        250       260
                 ....*....|....*....|...
gi 42741659  595 -ADVIAGFDDGVIVEKGNHDELM 616
Cdd:COG4172  492 lAHRVMVMKDGKVVEQGPTEQVF 514
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
1046-1263 2.76e-34

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 135.27  E-value: 2.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGKVLLDGKEIK-RLNVQwlRAHLGIVSQEPI 1121
Cdd:COG1118   11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1122 LF-DCSIAENIAYGDNSRVVSQEEIVRAAKEaNIHAF-IESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1199
Cdd:COG1118   86 LFpHMTVAENIAFGLRVRPPSKAEIRARVEE-LLELVqLEGLADRYPS-------QLSGGQRQRVALARALAVEPEVLLL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1200 DEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG1118  158 DEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
392-615 7.76e-34

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 134.12  E-value: 7.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRT-INVRFLReiI 470
Cdd:COG1118    3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----------ANAYdfimklPHkfdtlvgergaQLSGGQKQ 537
Cdd:COG1118   78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------PS-----------QLSGGQRQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  538 RIAIARALVRNPKILLLDEATSALDTeseavvqvaldKARK-------------GRTTIVIAH-RLSTVRNADVIAGFDD 603
Cdd:COG1118  141 RVALARALAVEPEVLLLDEPFGALDA-----------KVRKelrrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQ 209
                        250
                 ....*....|..
gi 42741659  604 GVIVEKGNHDEL 615
Cdd:COG1118  210 GRIEQVGTPDEV 221
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
392-615 1.00e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 131.74  E-value: 1.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFL--REI 469
Cdd:PRK13639    2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 IGVVSQEP--VLFATTIAENIRYGRENV--TMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAI 541
Cdd:PRK13639   80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   542 ARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK13639  149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
392-618 1.16e-33

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 130.21  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiIG 471
Cdd:COG1121    7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVL---FATTIAENI---RYGRENVTM-------DEIEKAVKEANAYDFImklphkfDTLVGErgaqLSGGQKQR 538
Cdd:COG1121   79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  539 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVR-NADVIAGFDDGVIVEkGNHDELM 616
Cdd:COG1121  148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226

                 ..
gi 42741659  617 KE 618
Cdd:COG1121  227 TP 228
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
714-1001 1.26e-33

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 131.99  E-value: 1.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  714 GVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISF--ITFFLQGFTFGKAGEILTKRLRYM 791
Cdd:cd18780    1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVVARLRKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  792 VFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIA 871
Cdd:cd18780   81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  872 GVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYF 951
Cdd:cd18780  159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  952 SYAGCFRFGAYLVAHK------LMSFedVLLVFSAvvfgAMAVGQVSSFAPDYAKA 1001
Cdd:cd18780  239 AIVLVLWYGGRLVIDGelttglLTSF--LLYTLTV----AMSFAFLSSLYGDFMQA 288
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1035-1255 1.46e-33

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 129.40  E-value: 1.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRA 1111
Cdd:COG2884    2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQK 1181
Cdd:COG2884   80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1182 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVFQNGRVKEHG 1255
Cdd:COG2884  144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
392-617 4.36e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 129.75  E-value: 4.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK13635    6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIAR 543
Cdd:PRK13635   85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   544 ALVRNPKILLLDEATSALDTE--SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMK 617
Cdd:PRK13635  154 VLALQPDIIILDEATSMLDPRgrREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
409-626 5.02e-33

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 128.87  E-value: 5.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI 488
Cdd:cd03288   36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  489 RYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 568
Cdd:cd03288  116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  569 VQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELM-KEKGIYFKLV 626
Cdd:cd03288  195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
393-610 5.25e-33

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 126.01  E-value: 5.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  393 EFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 472
Cdd:cd03214    1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  473 VSQepvlfattiaenirygrenvtmdeiekAVKEANAYDFIMKLphkFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 552
Cdd:cd03214   78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  553 LLDEATSALDTESeavvQVALDK------ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 610
Cdd:cd03214  120 LLDEPTSHLDIAH----QIELLEllrrlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
396-587 5.44e-33

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 126.99  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  396 NVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIrtiNVRFLREIIGVVSQ 475
Cdd:cd03226    4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  476 EP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03226   79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42741659  552 LLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAH 587
Cdd:cd03226  148 LIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
410-617 6.37e-33

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 127.84  E-value: 6.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIGVVSQEPVLFA-TTIAENI 488
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  489 RYGRENVTMD--EIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 566
Cdd:cd03299   93 AYGLKKRKVDkkEIERKVLEIAE---MLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659  567 AVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMK 617
Cdd:cd03299  166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1049-1256 7.02e-33

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 131.99  E-value: 7.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSI 1127
Cdd:PRK09452   26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1128 AENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK09452  104 FENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1208 TESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:PRK09452  177 YKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1051-1251 8.13e-33

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 127.87  E-value: 8.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEPILFD-CS 1126
Cdd:COG3638   17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRIGMIFQQFNLVPrLS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 IAENI---AYGDNS------RVVSQEEIVRAakeaniHAFIES--LPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPH 1195
Cdd:COG3638   97 VLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGGQQQRVAIARALVQEPK 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1196 ILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:COG3638  167 LILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1044-1263 1.87e-32

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 129.02  E-value: 1.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1044 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GKVLLDGKEIKRLNVQWLRA----HLGI 1115
Cdd:COG0444   11 FPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1116 VSQEP---------ILFdcSIAENI-AYGDNSRVVSQEEIVRAAKEANIH---AFIESLPNkystkvgdkgtQLSGGQKQ 1182
Cdd:COG0444   91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPH-----------ELSGGMRQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1183 RIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1255
Cdd:COG0444  158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233

                 ....*...
gi 42741659 1256 THQQLLAQ 1263
Cdd:COG0444  234 PVEELFEN 241
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1049-1260 1.97e-32

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 129.81  E-value: 1.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILFD-CSI 1127
Cdd:COG3839   15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYPhMTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:COG3839   93 YENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1204 SALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGTHQQL 1260
Cdd:COG3839  162 SNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
392-618 2.82e-32

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 125.81  E-value: 2.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIrtINVRFLREIIG 471
Cdd:cd03300    1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPhKFDTLVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:cd03300   76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  549 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS---TVrnADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:cd03300  149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
392-615 3.62e-32

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 126.43  E-value: 3.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEvkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDI---RTINV 463
Cdd:PRK14239    6 LQVSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   464 RfLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDE-IEKAVKEANAYDFIMKLPHkfDTLVGergaqLSGGQK 536
Cdd:PRK14239   83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRLH--DSALG-----LSGGQQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   537 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK14239  155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1040-1251 5.68e-32

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 122.89  E-value: 5.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGIVSQE 1119
Cdd:cd03230    6 LSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1120 PILF-DCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtQLSGGQKQRIAIARALVRQPHILL 1198
Cdd:cd03230   82 PSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1199 LDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:cd03230  119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
392-610 6.37e-32

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 124.29  E-value: 6.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRtiNVRFLREIIG 471
Cdd:cd03301    1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:cd03301   76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQIEH----LLDRKPKQLSGGQRQRVALGRAIVRE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  549 PKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKG 610
Cdd:cd03301  149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1046-1245 1.18e-31

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 123.36  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlRAHLGIVSQEPILF-D 1124
Cdd:COG4133   11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1125 CSIAENIA-----YGdnsRVVSQEEIVRAAKEANIHAFIEslpnkysTKVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1199
Cdd:COG4133   90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSPAPLWLL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659 1200 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1245
Cdd:COG4133  156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1046-1263 1.29e-31

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 131.35  E-value: 1.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEPil 1122
Cdd:COG4172  295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1123 FDC-----SIAENIAYGdnsRVVSQEEIVRAAKEANIhafIESLpnkysTKVG-DKGT------QLSGGQKQRIAIARAL 1190
Cdd:COG4172  372 FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARAL 440
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1191 VRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG4172  441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1034-1263 1.48e-31

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 124.43  E-value: 1.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1034 NVTFGevvfnYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLnvqwlRAHL 1113
Cdd:COG1121   11 NLTVS-----YGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1114 GIVSQE-------PIlfdcSIAENIAYGDNSRV-----VSQE--EIVRAA-KEANIHAFIeslpnkySTKVGdkgtQLSG 1178
Cdd:COG1121   78 GYVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrPSRAdrEAVDEAlERVGLEDLA-------DRPIG----ELSG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1179 GQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFqNGRVKEHGT 1256
Cdd:COG1121  143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGP 221

                 ....*..
gi 42741659 1257 HQQLLAQ 1263
Cdd:COG1121  222 PEEVLTP 228
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
392-598 1.94e-31

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 122.59  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFlREIIG 471
Cdd:COG4133    3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIR-----YGREnVTMDEIEKAVKEanaydfiMKLPHKFDTLVGergaQLSGGQKQRIAIARAL 545
Cdd:COG4133   79 YLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659  546 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVI 598
Cdd:COG4133  147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1034-1255 2.34e-31

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 121.39  E-value: 2.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1034 NVTFGevvfnYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1113
Cdd:cd03214    4 NLSVG-----YGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1114 GIVSQepilfdcsiaeniaygdnsrvvsqeeivrAAKEANIHAFIeslpnkystkvgDKG-TQLSGGQKQRIAIARALVR 1192
Cdd:cd03214   76 AYVPQ-----------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQ 114
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1193 QPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1255
Cdd:cd03214  115 EPPILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1049-1262 2.68e-31

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 122.93  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPILF-DC 1125
Cdd:cd03224   12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 SIAENIAYGDNSRVvsqeeivRAAKEANIHAFIESLPNKYsTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:cd03224   91 TVEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1206 LdteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVFQNGRVKEHGTHQQLLA 1262
Cdd:cd03224  163 L---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
cbiO PRK13637
energy-coupling factor transporter ATPase;
406-618 2.82e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 124.77  E-value: 2.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFLREIIGVVSQEP--VLFA 481
Cdd:PRK13637   19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLPhkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 559
Cdd:PRK13637   99 ETIEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659   560 ALD--TESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:PRK13637  174 GLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
392-608 3.82e-31

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 122.54  E-value: 3.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 466
Cdd:COG4181    9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  467 REIIGVVSQEPVLFATTIAEnirygrENVTM--------DEIEKAVKEANAYDfimklphkfdtlVGERG----AQLSGG 534
Cdd:COG4181   89 ARHVGFVFQSFQLLPTLTAL------ENVMLplelagrrDARARARALLERVG------------LGHRLdhypAQLSGG 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  535 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVIVE 608
Cdd:COG4181  151 EQQRVALARAFATEPAILFADEPTGNLDAAtGEQIIDLLFELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
1053-1260 5.63e-31

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 125.23  E-value: 5.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEPilFDC---- 1125
Cdd:COG4608   34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnpr 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 -SIAENIAYG-DNSRVVSqeeivRAAKEANIHAFIES--LP----NKYStkvgdkgTQLSGGQKQRIAIARALVRQPHIL 1197
Cdd:COG4608  112 mTVGDIIAEPlRIHGLAS-----KAERRERVAELLELvgLRpehaDRYP-------HEFSGGQRQRIGIARALALNPKLI 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1198 LLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:COG4608  180 VCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
cbiO PRK13650
energy-coupling factor transporter ATPase;
1040-1263 6.78e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 123.30  E-value: 6.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1040 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1119
Cdd:PRK13650   10 LTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1120 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQ 1193
Cdd:PRK13650   90 PdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  1194 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK13650  159 PKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1048-1251 8.74e-31

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 128.21  E-value: 8.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV-QWLRAHLGIVSQEPILF-DC 1125
Cdd:COG1129   15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 SIAENIAYGD---NSRVVSQEEIVRAAKEAnihafIESL-----PNkysTKVGDkgtqLSGGQKQRIAIARALVRQPHIL 1197
Cdd:COG1129   95 SVAENIFLGReprRGGLIDWRAMRRRAREL-----LARLgldidPD---TPVGD----LSVAQQQLVEIARALSRDARVL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1198 LLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:COG1129  163 ILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
392-562 1.01e-30

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 125.44  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-------RTINVR 464
Cdd:PRK09452   15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNTV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 FlreiigvvsQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPHkFDTLVGERGAQLSGGQKQRIAI 541
Cdd:PRK09452   92 F---------QSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAI 155
                         170       180
                  ....*....|....*....|.
gi 42741659   542 ARALVRNPKILLLDEATSALD 562
Cdd:PRK09452  156 ARAVVNKPKVLLLDESLSALD 176
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
392-615 1.50e-30

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 127.44  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 470
Cdd:COG1129    5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFAT-TIAENIRYGRENVT---MD--EIEKAVKEANAYdfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARA 544
Cdd:COG1129   82 AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  545 LVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:COG1129  155 LSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
393-595 1.61e-30

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 120.33  E-value: 1.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  393 EFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiIGV 472
Cdd:cd03235    1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  473 VSQEPVL---FATTIAENIRYGREN----------VTMDEIEKAVKEANAYDFImklphkfDTLVGErgaqLSGGQKQRI 539
Cdd:cd03235   73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  540 AIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRNA 595
Cdd:cd03235  142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
757-970 1.78e-30

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 122.65  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  757 LLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVI 836
Cdd:cd18572   40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  837 TQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVE---MKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTQE 913
Cdd:cd18572  118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYgryYRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATE 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  914 QKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMS 970
Cdd:cd18572  195 EREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
392-627 1.94e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 121.68  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDI--RTINVR 464
Cdd:PRK14258    8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 FLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQ 537
Cdd:PRK14258   85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   538 RIAIARALVRNPKILLLDEATSALDTESEAVVQ--VALDKARKGRTTIVIAHRLSTV-RNADVIAGFddgviveKGNHDE 614
Cdd:PRK14258  158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVEslIQSLRLRSELTMVIVSHNLHQVsRLSDFTAFF-------KGNENR 230
                         250
                  ....*....|....*
gi 42741659   615 L--MKEKGIYFKLVT 627
Cdd:PRK14258  231 IgqLVEFGLTKKIFN 245
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
392-618 1.94e-30

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 120.23  E-value: 1.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-RFLREII 470
Cdd:cd03224    1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNP 549
Cdd:cd03224   78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  550 KILLLDEATSALdteSEAVVQV---ALDKARKGRTTIVI----AHRLSTVrnADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:cd03224  152 KLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
392-618 2.16e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 122.12  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVK---ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-NVRFLR 467
Cdd:PRK13633    5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   468 EIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRI 539
Cdd:PRK13633   85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   540 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMK 617
Cdd:PRK13633  154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233

                  .
gi 42741659   618 E 618
Cdd:PRK13633  234 E 234
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
392-607 2.18e-30

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 117.91  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 470
Cdd:cd03216    1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPK 550
Cdd:cd03216   78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  551 ILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 607
Cdd:cd03216  103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1051-1255 2.46e-30

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 119.56  E-value: 2.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLnvqwlRAHLGIVSQEPIL---FDCSI 1127
Cdd:cd03235   13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQRRSIdrdFPISV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEANIHAFieslpnkysTKVGDKG------TQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:cd03235   88 RDVVLMGLYGHKGLFRRLSKADKAKVDEAL---------ERVGLSEladrqiGELSGGQQQRVLLARALVQDPDLLLLDE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1202 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFqNGRVKEHG 1255
Cdd:cd03235  159 PFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1051-1251 4.13e-30

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 119.98  E-value: 4.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI---KRLNVQWLRAHLGIVSQEPILFD-CS 1126
Cdd:cd03256   15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGMIFQQFNLIErLS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 IAENIAYGDNSRV---------VSQEEIVRAakeanIHAFIES-LPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHI 1196
Cdd:cd03256   95 VLENVLSGRLGRRstwrslfglFPKEEKQRA-----LAALERVgLLDKAYQRAD----QLSGGQQQRVAIARALMQQPKL 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1197 LLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1251
Cdd:cd03256  166 ILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1035-1231 4.61e-30

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 119.05  E-value: 4.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRA 1111
Cdd:cd03292    1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQE-PILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAI 1186
Cdd:cd03292   79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALPA-----------ELSGGEQQRVAI 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 42741659 1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1231
Cdd:cd03292  148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1048-1260 5.01e-30

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 119.75  E-value: 5.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCS 1126
Cdd:cd03296   13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 IAENIAYG----DNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:cd03296   91 VFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEP 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1203 TSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:cd03296  164 FGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1053-1251 5.76e-30

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 118.55  E-value: 5.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQWLRAHLGIVSQEPILF-D 1124
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1125 CSIAENIAYGdnSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:cd03297   90 LNVRENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42741659 1205 ALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:cd03297  161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1040-1252 8.16e-30

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 118.13  E-value: 8.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRPDIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlnvQWLRAHLGIVSQE 1119
Cdd:cd03226    5 ISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1120 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHIL 1197
Cdd:cd03226   80 VdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1198 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK 1252
Cdd:cd03226  149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
cbiO PRK13650
energy-coupling factor transporter ATPase;
392-596 8.82e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 120.22  E-value: 8.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIAR 543
Cdd:PRK13650   85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   544 ALVRNPKILLLDEATSALDTES--EAVVQVALDKARKGRTTIVIAHRLSTVRNAD 596
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGrlELIKTIKGIRDDYQMTVISITHDLDEVALSD 208
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1053-1263 1.07e-29

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 119.50  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA-----GKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILFDC 1125
Cdd:PRK14243   26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGD--NSRVVSQEEIV-RAAKEAnihafieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:PRK14243  106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1203 TSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK14243  179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
386-627 1.26e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.46  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   386 DNIkgnLEFRNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF 465
Cdd:PRK13647    2 DNI---IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQ 537
Cdd:PRK13647   77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   538 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG----- 610
Cdd:PRK13647  146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksll 225
                         250
                  ....*....|....*..
gi 42741659   611 NHDELMKEKGIYFKLVT 627
Cdd:PRK13647  226 TDEDIVEQAGLRLPLVA 242
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
408-610 1.35e-29

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 117.78  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  408 KILKGLNLKVQ---SGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ---DIR-TINVRFLREIIGVVSQEPVLF 480
Cdd:cd03297    8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  481 A-TTIAENIRYGRENVTMDEIEKAVKEANAYdfiMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 559
Cdd:cd03297   88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659  560 ALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 610
Cdd:cd03297  161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1035-1256 1.71e-29

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 117.92  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVfnyptrpdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLG 1114
Cdd:cd03219    8 KRFGGLV----------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVS--QEPILF-DCSIAENI----------AYGDNSRVVSQEEIVRAAKEanIHAFIEsLPNKYSTKVGDkgtqLSGGQK 1181
Cdd:cd03219   77 IGRtfQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAEE--LLERVG-LADLADRPAGE----LSYGQQ 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1182 QRIAIARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:cd03219  150 RRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1053-1272 1.83e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.07  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP--ILFDCSIAEN 1130
Cdd:PRK13647   21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1131 IAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:PRK13647  101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1207 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG-----THQQLLAQKGIYFSMVS 1272
Cdd:PRK13647  170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVA 242
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1048-1251 2.27e-29

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 115.22  E-value: 2.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqwlrahlgivsqepilfdcsi 1127
Cdd:cd03216   11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP--------------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 aeniaygdnsrvvsqeeivRAAKEANIhAFIeslpnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL- 1206
Cdd:cd03216   70 -------------------RDARRAGI-AMV---------------YQLSVGERQMVEIARALARNARLLILDEPTAALt 114
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 42741659 1207 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:cd03216  115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1022-1280 2.49e-29

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 127.37  E-value: 2.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1022 STEGLMPNTLE--------GN-VTFGEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG 1092
Cdd:TIGR00957  615 SHEELEPDSIErrtikpgeGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1093 KVLLDGKeikrlnvqwlrahLGIVSQEPILFDCSIAENIAYGDNSrvvsQEEIVRAAKEA-NIHAFIESLPNKYSTKVGD 1171
Cdd:TIGR00957  694 HVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKAL----NEKYYQQVLEAcALLPDLEILPSGDRTEIGE 756
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1172 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVFQN 1248
Cdd:TIGR00957  757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSG 836
                          250       260       270
                   ....*....|....*....|....*....|..
gi 42741659   1249 GRVKEHGTHQQLLAQKGIYFSMVSVQAGTKRQ 1280
Cdd:TIGR00957  837 GKISEMGSYQELLQRDGAFAEFLRTYAPDEQQ 868
cbiO PRK13642
energy-coupling factor transporter ATPase;
392-615 4.12e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 118.27  E-value: 4.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIAR 543
Cdd:PRK13642   85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   544 ALVRNPKILLLDEATSALDT--ESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK13642  154 IIALRPEIIILDESTSMLDPtgRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1057-1263 4.39e-29

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 116.78  E-value: 4.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1057 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAhLGIVSQEPILFD-CSIAENIAYGD 1135
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVAQNIGLGL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1136 NSR----VVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1207
Cdd:COG3840   97 RPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1208 TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG3840  166 QEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1046-1209 5.96e-29

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 115.66  E-value: 5.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPIL 1122
Cdd:COG4136   10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1123 FD-CSIAENIAYG---DNSRVVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILL 1198
Cdd:COG4136   88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
                        170
                 ....*....|.
gi 42741659 1199 LDEATSALDTE 1209
Cdd:COG4136  157 LDEPFSKLDAA 167
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
392-608 6.52e-29

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 117.21  E-value: 6.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    392 LEFRNVHFSYPS------RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN--- 462
Cdd:TIGR02769    3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    463 -VRFLREIIGVVSQEPVLF--ATTIAENIRYGRENVT-MDEIEKAVKEANAYDfIMKLPhkfDTLVGERGAQLSGGQKQR 538
Cdd:TIGR02769   83 rRAFRRDVQLVFQDSPSAVnpRMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659    539 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVE 608
Cdd:TIGR02769  159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
cbiO PRK13640
energy-coupling factor transporter ATPase;
386-626 6.74e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 117.59  E-value: 6.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   386 DNIkgnLEFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TEGMVSVDGQDIRTIN 462
Cdd:PRK13640    3 DNI---VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   463 VRFLREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANA----YDFIMKLPhkfdtlvgergAQLSGG 534
Cdd:PRK13640   79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   535 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALD-KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG-- 610
Cdd:PRK13640  148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGsp 227
                         250       260
                  ....*....|....*....|
gi 42741659   611 ----NHDELMKEKGIYFKLV 626
Cdd:PRK13640  228 veifSKVEMLKEIGLDIPFV 247
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
392-619 1.05e-28

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 116.34  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGM-VSVDGQDIRTINVRFLREII 470
Cdd:COG1119    4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVS---------QEPVL-------FATTiaeniryGR-ENVTMDEIEKAVKEANAydfiMKLPHKFDTLVGergaQLSG 533
Cdd:COG1119   81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARELLEL----LGLAHLADRPFG----TLSQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  534 GQKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVaLDK-ARKGRTTIV-IAHRLStvrnaDVIAGFD------DG 604
Cdd:COG1119  146 GEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLAL-LDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDG 219
                        250
                 ....*....|....*
gi 42741659  605 VIVEKGNHDELMKEK 619
Cdd:COG1119  220 RVVAAGPKEEVLTSE 234
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
386-617 1.30e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 116.39  E-value: 1.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   386 DNIkgnLEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF 465
Cdd:PRK13648    5 NSI---IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQ 537
Cdd:PRK13648   81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   538 RIAIARALVRNPKILLLDEATSALDTE--SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK13648  150 RVAIAGVLALNPSVIILDEATSMLDPDarQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229

                  ..
gi 42741659   616 MK 617
Cdd:PRK13648  230 FD 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
392-617 1.37e-28

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 115.23  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflrEI-- 469
Cdd:cd03219    1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIar 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 --IGVVSQEPVLFAT-TIAENIRYG-----RENVTMDEIEKAVKEANAYDF----IMKLPHKFDTLVGErgaqLSGGQKQ 537
Cdd:cd03219   75 lgIGRTFQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  538 RIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:cd03219  151 RLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEV 230

                 ..
gi 42741659  616 MK 617
Cdd:cd03219  231 RN 232
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1048-1255 1.65e-28

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 114.27  E-value: 1.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKrlNVQWLRAHLGIVSQEPILF-DCS 1126
Cdd:cd03301   11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYpHMT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 IAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:cd03301   89 VYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1207 DTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1255
Cdd:cd03301  162 DAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
409-615 2.56e-28

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 115.23  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI---RTIN-----VRFLREIIGVVSQEPVLF 480
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   481 A-TTIAENIRYGreNVTMDEIEKAVKEANAYDFIMKLphkfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILLLDE 556
Cdd:PRK11264   98 PhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILFDE 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659   557 ATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK11264  171 PTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1047-1256 4.94e-28

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 116.82  E-value: 4.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1047 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPLAGKVLLDGKEIKRLNVQWLRA---HLGIVSQE- 1119
Cdd:PRK11153   15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHf 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1120 PILFDCSIAENIAY-----GdnsrvVSQEEIvraakEANIHAFIEslpnkystKVG--DKG----TQLSGGQKQRIAIAR 1188
Cdd:PRK11153   92 NLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRVAIAR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1189 ALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGT 1256
Cdd:PRK11153  154 ALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
392-611 4.95e-28

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 112.26  E-value: 4.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHF---SYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLM-----QRLYDPTEGMVSVDGQDIRTINv 463
Cdd:cd03213    4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLnalagRRTGLGVSGEVLINGRPLDKRS- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  464 rfLREIIGVVSQEPVLFAT-TIAENIrygrenvtmdeiekavkeanayDFIMKLphkfdtlvgeRGaqLSGGQKQRIAIA 542
Cdd:cd03213   80 --FRKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIA 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  543 RALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTvrnaDVIAGFDDGVIVEKGN 611
Cdd:cd03213  124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1049-1261 6.48e-28

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 113.65  E-value: 6.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK--RLNVQWLRAHLGIVSQEPILFDCS 1126
Cdd:PRK09493   13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1127 IA-ENIAYGDNSrvvsqeeiVRAAKEANIHAFIESLPNK--YSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:PRK09493   93 TAlENVMFGPLR--------VRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1204 SALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLL 1261
Cdd:PRK09493  165 SALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
714-987 8.32e-28

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 114.89  E-value: 8.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  714 GVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFItfflQGFTFGKAGEILTKRLRYMVF 793
Cdd:cd18576    1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  794 RSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGV 873
Cdd:cd18576   77 RHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  874 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 950
Cdd:cd18576  155 LfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLF 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 42741659  951 FSYAGCFRFGAYLVAHKLMSFEDV--LLVFSAVVFGAMA 987
Cdd:cd18576  232 GAIVAVLWYGGRLVLAGELTAGDLvaFLLYTLFIAGSIG 270
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
392-587 8.63e-28

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 112.60  E-value: 8.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 471
Cdd:cd03263    1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRY-----GRENVTMDEiekavkEANAYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARAL 545
Cdd:cd03263   79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42741659  546 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAH 587
Cdd:cd03263  149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
100-362 9.51e-28

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 114.50  E-value: 9.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  100 DTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDV 179
Cdd:cd18575   24 DQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  180 SKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAV---WAKILSSFTDKELlayAKAGAVAEE 256
Cdd:cd18575  104 TLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRASQDRL---ADLSAFAEE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  257 VLAAIRTVIAFGGQKKELERYNKNLEEA-----KRIGIKKAITAnisigAAFLLIYASYALAFWYGTTLVLSGEYSIGQv 331
Cdd:cd18575  181 TLSAIKTVQAFTREDAERQRFATAVEAAfaaalRRIRARALLTA-----LVIFLVFGAIVFVLWLGAHDVLAGRMSAGE- 254
                        250       260       270
                 ....*....|....*....|....*....|..
gi 42741659  332 LTVF-FSVLIGAFSVGQASPSIEAFANARGAA 362
Cdd:cd18575  255 LSQFvFYAVLAAGSVGALSEVWGDLQRAAGAA 286
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
409-608 1.74e-27

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 113.24  E-value: 1.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN---VRFLREIIGVVSQEP---VLFAT 482
Cdd:PRK10419   27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPRK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   483 TIAENIRYG-RENVTMDEIEKAVKEANAYDfIMKLPhkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 561
Cdd:PRK10419  107 TVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 42741659   562 DTESEAVVQVALDKARKGRTT--IVIAHRLSTV-RNADVIAGFDDGVIVE 608
Cdd:PRK10419  183 DLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
cbiO PRK13642
energy-coupling factor transporter ATPase;
1040-1262 1.77e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 113.65  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1040 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1119
Cdd:PRK13642   10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1120 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHIL 1197
Cdd:PRK13642   90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGIIALRPEII 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  1198 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK13642  163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
392-564 2.08e-27

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 112.05  E-value: 2.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIG 471
Cdd:cd03296    3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFA-TTIAENIRYG------RENVTMDEIEKAVKEanaydfIMKLPHkFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:cd03296   78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWLADRYPAQLSGGQRQRVALARA 150
                        170       180
                 ....*....|....*....|
gi 42741659  545 LVRNPKILLLDEATSALDTE 564
Cdd:cd03296  151 LAVEPKVLLLDEPFGALDAK 170
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
385-619 2.09e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 113.40  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   385 PDNIkgnLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ--DIRTIN 462
Cdd:PRK13636    2 EDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   463 VRFLREIIGVVSQEP--VLFATTIAENIRYGRENVTM--DEIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQR 538
Cdd:PRK13636   77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   539 IAIARALVRNPKILLLDEATSALDTE--SEaVVQVALDKARKGRTTIVIA-HRLSTVR-NADVIAGFDDGVIVEKGNHDE 614
Cdd:PRK13636  150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228

                  ....*
gi 42741659   615 LMKEK 619
Cdd:PRK13636  229 VFAEK 233
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1053-1260 2.33e-27

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 112.56  E-value: 2.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILFDC 1125
Cdd:PRK14239   21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGDNSRVVSQEEIVRAAKEANIHAfiESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:PRK14239  101 SIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1206 LDTESEKVVQEALDKAREGRTCIVIAHRL---STIqnADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK14239  179 LDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
cbiO PRK13646
energy-coupling factor transporter ATPase;
392-619 2.57e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 113.34  E-value: 2.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYP--SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI----RTINVRF 465
Cdd:PRK13646    3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDeIEKAvkEANAYDFIMKLPHKFDTLvGERGAQLSGGQKQRIAIAR 543
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659   544 ALVRNPKILLLDEATSALDTESEAVVQVALDKAR--KGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:PRK13646  159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1035-1260 3.82e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 112.15  E-value: 3.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1035 VTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1113
Cdd:PRK13648    8 IVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1114 GIVSQEPI-LFDCSIAE-NIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIA 1187
Cdd:PRK13648   86 GIVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1188 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK13648  155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
392-607 4.32e-27

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 118.67  E-value: 4.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKE-VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 466
Cdd:PRK10535    5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   467 REIIGVVSQEPVLFATTIAEnirygrENVTMDEI----EKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIA 542
Cdd:PRK10535   85 REHFGFIFQRYHLLSHLTAA------QNVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   543 RALVRNPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNADVIAGFDDGVIV 607
Cdd:PRK10535  157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
392-615 5.05e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 113.52  E-value: 5.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRK-------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI------ 458
Cdd:PRK11308    6 LQAIDLKKHYPVKRglfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpe 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   459 ------RTINVRFL--------REIIGVVSQEPVLFATTIAENIRygRENVtMDEIEKAVKEANAYDfimKLPHKFdtlv 524
Cdd:PRK11308   86 aqkllrQKIQIVFQnpygslnpRKKVGQILEEPLLINTSLSAAER--REKA-LAMMAKVGLRPEHYD---RYPHMF---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   525 gergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIV-IAHRLSTVRNadvIAgfD 602
Cdd:PRK11308  156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEH---IA--D 223
                         250
                  ....*....|....*....
gi 42741659   603 D------GVIVEKGNHDEL 615
Cdd:PRK11308  224 EvmvmylGRCVEKGTKEQI 242
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
1052-1263 5.40e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 114.05  E-value: 5.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAEN 1130
Cdd:PRK11432   21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1131 IAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:PRK11432   99 VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  1211 EKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK11432  172 RRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
392-615 6.33e-27

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 113.26  E-value: 6.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRN--VHFSYPSRKE--------VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI 461
Cdd:PRK15079    9 LEVADlkVHFDIKDGKQwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   462 NVRFLREI---IGVVSQEPV-------LFATTIAENIRYGRENVTMDEIEKAVKEANAY-----DFIMKLPHKFdtlvge 526
Cdd:PRK15079   89 KDDEWRAVrsdIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   527 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDD 603
Cdd:PRK15079  163 -----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYL 237
                         250
                  ....*....|..
gi 42741659   604 GVIVEKGNHDEL 615
Cdd:PRK15079  238 GHAVELGTYDEV 249
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
391-616 7.00e-27

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 110.23  E-value: 7.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  391 NLEFRNVHFSYPSRkevkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVrFLREIi 470
Cdd:COG3840    1 MLRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFA-TTIAENI--------RYGRENVTmdEIEKAVKEANAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAI 541
Cdd:COG3840   74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  542 ARALVRNPKILLLDEATSALD----TESEAVV-QVAldkARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:COG3840  141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVdELC---RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217

                 .
gi 42741659  616 M 616
Cdd:COG3840  218 L 218
cbiO PRK13637
energy-coupling factor transporter ATPase;
1053-1256 7.23e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 112.06  E-value: 7.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEP--ILFDCSIA 1128
Cdd:PRK13637   23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENIAYGDNSRVVSQEEIVRAAKEAnihafIESLPNKYSTkVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK13637  103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1208 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:PRK13637  177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
392-562 8.62e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 109.80  E-value: 8.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK10247    8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVLFATTIAENIRYGRenvtmdEIEKAVKEANAY-DFIMK--LPhkfDTLVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:PRK10247   85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
                         170
                  ....*....|....
gi 42741659   549 PKILLLDEATSALD 562
Cdd:PRK10247  156 PKVLLLDEITSALD 169
cbiO PRK13644
energy-coupling factor transporter ATPase;
1040-1262 1.25e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 110.85  E-value: 1.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1040 VVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-VQWLRAHLGIVSQ 1118
Cdd:PRK13644    7 VSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1119 EP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEAnihaFIESLPNKYSTKvgdKGTQLSGGQKQRIAIARALVRQPHI 1196
Cdd:PRK13644   85 NPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPEC 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1197 LLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK13644  158 LIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
392-562 1.31e-26

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 112.89  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRflreI 469
Cdd:PRK11432    7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQR----D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 IGVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALV 546
Cdd:PRK11432   80 ICMVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
                         170
                  ....*....|....*.
gi 42741659   547 RNPKILLLDEATSALD 562
Cdd:PRK11432  153 LKPKVLLFDEPLSNLD 168
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1052-1262 2.26e-26

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 109.45  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI---KRLNVQW-----LRAHLGIVSQEPILF 1123
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNFNLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DC-SIAENIAYGDnsrVVSQEEIVRAAkeanihafiESLPNKYSTKVGDKGTQ------LSGGQKQRIAIARALVRQPHI 1196
Cdd:PRK11264   98 PHrTVLENIIEGP---VIVKGEPKEEA---------TARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1197 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK11264  166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1042-1261 2.42e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 109.74  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1042 FNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEI--KRLNVQWLRAHLG 1114
Cdd:PRK14258   15 FYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRRQVS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1115 IVSQEPILFDCSIAENIAYGdnsrvvsqEEIVRAAKEANIHAFIES------LPNKYSTKVGDKGTQLSGGQKQRIAIAR 1188
Cdd:PRK14258   92 MVHPKPNLFPMSVYDNVAYG--------VKIVGWRPKLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1189 ALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQN-----GRVKEHGTHQQL 1260
Cdd:PRK14258  164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKI 243

                  .
gi 42741659  1261 L 1261
Cdd:PRK14258  244 F 244
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1039-1264 2.95e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 109.78  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1039 EVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL--RAHLGIV 1116
Cdd:PRK13639    6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1117 SQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQP 1194
Cdd:PRK13639   84 FQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENK-------PPHHLSGGQKKRVAIAGILAMKP 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  1195 HILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:PRK13639  157 EIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1039-1264 3.44e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 109.94  E-value: 3.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1039 EVVFNYPTRPDipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI--KRLNVQWLRAHLGIV 1116
Cdd:PRK13636   10 ELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1117 SQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALVRQP 1194
Cdd:PRK13636   88 FQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVMEP 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1195 HILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:PRK13636  161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1051-1249 3.50e-26

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 114.90  E-value: 3.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLL-DGKEIkrlnvqwlrahLgIVSQEPILFDCSIAE 1129
Cdd:COG4178  377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1130 NIAYGDNSRVVSQEEIVRAAKEANIHAFIESLpnkysTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1209
Cdd:COG4178  445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42741659 1210 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNG 1249
Cdd:COG4178  520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
391-613 3.85e-26

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 108.56  E-value: 3.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  391 NLEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG------QDIRTINVR 464
Cdd:COG4161    2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  465 FLREIIGVVSQE----PVLfatTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLvgerGAQLSGGQKQRIA 540
Cdd:COG4161   79 LLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRVA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  541 IARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 613
Cdd:COG4161  152 IARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1051-1261 3.98e-26

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 109.09  E-value: 3.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FDCSIAE 1129
Cdd:PRK13548   16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1130 NIAYG--DNSRVVSQ-EEIVRAA-KEANIHAFIESLpnkYstkvgdkgTQLSGGQKQRIAIARALVR------QPHILLL 1199
Cdd:PRK13548   96 VVAMGraPHGLSRAEdDALVAAAlAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLAQlwepdgPPRWLLL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1200 DEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:PRK13548  165 DEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
1035-1256 4.07e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.45  E-value: 4.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1035 VTFGEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQW 1108
Cdd:PRK13649    3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1109 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA-NIHAFIESLPNKystkvgdKGTQLSGGQKQRIA 1185
Cdd:PRK13649   83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1186 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:PRK13649  156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1052-1253 4.10e-26

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 108.29  E-value: 4.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGKVLLDGKEIKRLN----VQWLRAHLGIVSQE----P 1120
Cdd:COG4181   27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1121 ILfdcSIAEN------IAYGDNSRVVSQEEIVRAAKEANIHAFieslPNkystkvgdkgtQLSGGQKQRIAIARALVRQP 1194
Cdd:COG4181  104 TL---TALENvmlpleLAGRRDARARARALLERVGLGHRLDHY----PA-----------QLSGGEQQRVALARAFATEP 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1195 HILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1253
Cdd:COG4181  166 AILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
404-610 5.05e-26

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 107.74  E-value: 5.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  404 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL-MQRLYDP--TEGMVSVDGQDIRTINVRFlreIIGVVSQEPVLF 480
Cdd:cd03234   17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGgtTSGQILFNGQPRKPDQFQK---CVAYVRQDDILL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  481 AT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHkfDTLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 558
Cdd:cd03234   94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  559 SALDTESE-AVVQVALDKARKGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKG 610
Cdd:cd03234  172 SGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
406-616 5.16e-26

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 108.52  E-value: 5.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-------------NVRFLREIIGV 472
Cdd:PRK10619   17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   473 VSQEPVLFA-TTIAENIRygRENVTMDEIEKAVKEANAYDFIMKLPHKfDTLVGERGAQLSGGQKQRIAIARALVRNPKI 551
Cdd:PRK10619   97 VFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   552 LLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGF-DDGVIVEKGNHDELM 616
Cdd:PRK10619  174 LLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1048-1249 5.65e-26

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 107.42  E-value: 5.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAH----LGIVSQEPILF 1123
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 DCSIAENIAYGDNSRVVSQEEIVRAAkeaNIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:cd03290   92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 42741659 1204 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNG 1249
Cdd:cd03290  169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
cbiO PRK13641
energy-coupling factor transporter ATPase;
392-610 5.66e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 109.53  E-value: 5.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYP--SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIR----TINVRF 465
Cdd:PRK13641    3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEIEKAVKeanAYDFIMKLPHKfDTLVGERGAQLSGGQKQRIAIAR 543
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659   544 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHrlstvrNADVIAGFDDGVIV-EKG 610
Cdd:PRK13641  159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
cbiO PRK13649
energy-coupling factor transporter ATPase;
392-619 5.67e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.06  E-value: 5.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI----NVRF 465
Cdd:PRK13649    3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQ--EPVLFATTIAENIRYGREN--VTMDEIEKAVKEANAYDFIMklphkfDTLVGERGAQLSGGQKQRIAI 541
Cdd:PRK13649   83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   542 ARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKG------NHD 613
Cdd:PRK13649  157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGkpkdifQDV 236

                  ....*.
gi 42741659   614 ELMKEK 619
Cdd:PRK13649  237 DFLEEK 242
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1044-1260 7.57e-26

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 106.82  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1044 YPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILF 1123
Cdd:cd03263   10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 D-CSIAENIAYgdNSRV--VSQEEIvraakEANIHAFIE--SLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILL 1198
Cdd:cd03263   88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRvlGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659 1199 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:cd03263  157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1056-1255 7.64e-26

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 106.81  E-value: 7.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1056 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAENIAYG 1134
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1135 DNSRV----VSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:cd03298   95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 42741659 1211 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:cd03298  164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
cbiO PRK13640
energy-coupling factor transporter ATPase;
1035-1256 8.25e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 108.73  E-value: 8.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1035 VTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GKVLLDGKEIKRLNVQWLRA 1111
Cdd:PRK13640    6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1112 HLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIA 1185
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1186 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1051-1263 8.27e-26

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 113.63  E-value: 8.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA----HLGIVSQEPI- 1121
Cdd:COG4172   24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1122 ----LFdcSIAENIAygdnsrvvsqeEIVRA-----AKEANIHAfIESLpnkysTKVG--DKGT-------QLSGGQKQR 1183
Cdd:COG4172  104 slnpLH--TIGKQIA-----------EVLRLhrglsGAAARARA-LELL-----ERVGipDPERrldayphQLSGGQRQR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1184 IAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:COG4172  165 VMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240

                 ....*..
gi 42741659 1257 HQQLLAQ 1263
Cdd:COG4172  241 TAELFAA 247
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
392-610 1.29e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 107.31  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDIRTINVRFL 466
Cdd:PRK14247    4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   467 REIIGVVSQEPVLFAT-TIAENIRYG----RENVTMDEIEKAVKEANAYdfiMKLPHKFDTLVGERGAQLSGGQKQRIAI 541
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   542 ARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKG 610
Cdd:PRK14247  158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
1056-1264 1.53e-25

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 109.82  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1056 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQWLRAHLGIVSQEPILF-DCSIAEN 1130
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1131 IAYG-----DNSRVVSQEEIVRAAkeaNIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:TIGR02142   96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659   1206 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:TIGR02142  162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1049-1262 1.60e-25

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 106.60  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRAHLGI--VSQEPILF-DC 1125
Cdd:COG0410   15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 SIAENIAYGdnSRVVSQEEIVRAAKEANIHAFieslPN-KysTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:COG0410   94 TVEENLLLG--AYARRDRAEVRADLERVYELF----PRlK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1205 ALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:COG0410  166 GL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
408-564 1.62e-25

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 109.79  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   408 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLReiIGVVSQEPVLFA-TTIAE 486
Cdd:PRK10851   16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   487 NIRYG------RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK10851   94 NIAFGltvlprRERPNAAAIKAKVTQLLE---MVQLAH----LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166

                  ....
gi 42741659   561 LDTE 564
Cdd:PRK10851  167 LDAQ 170
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
127-345 1.66e-25

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 108.28  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  127 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 206
Cdd:cd18552   54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  207 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR 286
Cdd:cd18552  134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  287 IGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvltvFFSVLIGAFSV 345
Cdd:cd18552  214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
cbiO PRK13644
energy-coupling factor transporter ATPase;
392-618 2.01e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 107.38  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN-VRFLREII 470
Cdd:PRK13644    2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQEP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQRIAIARALV 546
Cdd:PRK13644   80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659   547 RNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:PRK13644  153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
1051-1264 2.28e-25

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 106.81  E-value: 2.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA---HLGIVSQEpilfdcsi 1127
Cdd:TIGR02769   25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQD-------- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1128 aeniAYGDNSRVVSQEEIVR-----------AAKEANIHAFIE--SLPNKYSTKVGdkgTQLSGGQKQRIAIARALVRQP 1194
Cdd:TIGR02769   97 ----SPSAVNPRMTVRQIIGeplrhltsldeSEQKARIAELLDmvGLRSEDADKLP---RQLSGGQLQRINIARALAVKP 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659   1195 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:TIGR02769  170 KLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
392-610 2.34e-25

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 105.35  E-value: 2.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTvALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRtINVRFLREIIG 471
Cdd:cd03264    1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRY-----GRENVTMD-EIEKAVKEANAYDFimklphkfdtlVGERGAQLSGGQKQRIAIARA 544
Cdd:cd03264   76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  545 LVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:cd03264  145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
392-610 2.42e-25

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 105.83  E-value: 2.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-RFLREII 470
Cdd:COG0410    4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnAYDFimklphkFDTLvGER----GAQLSGGQKQRIAIARAL 545
Cdd:COG0410   81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYEL-------FPRL-KERrrqrAGTLSGGEQQMLAIGRAL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  546 VRNPKILLLDEATSALdteSEAVVQV---ALDKARKGRTTIVIahrlstV-RNADVIAGF-DDGVIVEKG 610
Cdd:COG0410  152 MSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILL------VeQNARFALEIaDRAYVLERG 212
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
1053-1263 2.55e-25

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 109.03  E-value: 2.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydP------LAGKVLLDGKeikrlNVQWLRAH---LGI 1115
Cdd:COG4148   11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PdsgrirLGGEVLQDSA-----RGIFLPPHrrrIGY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1116 VSQEPILFD-CSIAENIAYG-----DNSRVVSQEEIVRAAKeanihafIESLPNKYStkvgdkgTQLSGGQKQRIAIARA 1189
Cdd:COG4148   82 VFQEARLFPhLSVRGNLLYGrkrapRAERRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1190 LVRQPHILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG4148  148 LLSSPRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
392-562 2.60e-25

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 106.87  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflReii 470
Cdd:COG4525    4 LTVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFA-TTIAENIRYGrenVTMDEIEKAVKEANAYDFImklphkfdTLVGERGA------QLSGGQKQRIAIAR 543
Cdd:COG4525   79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIAR 147
                        170
                 ....*....|....*....
gi 42741659  544 ALVRNPKILLLDEATSALD 562
Cdd:COG4525  148 ALAADPRFLLMDEPFGALD 166
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1052-1272 2.97e-25

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 106.86  E-value: 2.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENI 1131
Cdd:cd03289   19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1132 -AYGDNSrvvsQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:cd03289   98 dPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1211 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVS 1272
Cdd:cd03289  174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
391-615 3.32e-25

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 108.96  E-value: 3.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   391 NLEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdiRTINVRFLREII 470
Cdd:PRK11000    3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVR 547
Cdd:PRK11000   78 GMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQLAH----LLDRKPKALSGGQRQRVAIGRTLVA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659   548 NPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK11000  151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1053-1263 3.42e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 108.13  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK---RLNVQWLRAHLGIVSQEPilfdcsiae 1129
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP--------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1130 niaYGD-NSR-VVSQ--EE-------IVRAAKEANIHAFIEslpnkystKVGDKGTQ-------LSGGQKQRIAIARALV 1191
Cdd:PRK11308  102 ---YGSlNPRkKVGQilEEpllintsLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAIARALM 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1192 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK11308  171 LDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1034-1251 3.54e-25

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 106.28  E-value: 3.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1034 NVT--FGEVVfnyptrpdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRA 1111
Cdd:COG0411    9 GLTkrFGGLV----------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVS--QEPILF-DCSIAENIAYG--------------DNSRVVSQEEIVRAAKEANIHAFieSLPNKYSTKVGDkgt 1174
Cdd:COG0411   78 RLGIARtfQNPRLFpELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERV--GLADRADEPAGN--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1175 qLSGGQKQRIAIARALVRQPHILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:COG0411  153 -LSYGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGR 230

                 .
gi 42741659 1251 V 1251
Cdd:COG0411  231 V 231
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
121-337 4.64e-25

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 106.75  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  121 IGAGVL--VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMA 198
Cdd:cd18542   46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  199 TFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 278
Cdd:cd18542  126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFD 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  279 KNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFS 337
Cdd:cd18542  206 KENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
392-615 5.31e-25

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 108.77  E-value: 5.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKilkGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-------RTINVR 464
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvppyqRPINMM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 FlreiigvvsQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----ANAYDFIMKLPHkfdtlvgergaQLSGGQKQ 537
Cdd:PRK11607   97 F---------QSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   538 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKGNHDE 614
Cdd:PRK11607  157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEE 236

                  .
gi 42741659   615 L 615
Cdd:PRK11607  237 I 237
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
392-602 5.34e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 106.02  E-value: 5.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKilkGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD--PT---EGMVSVDGQDI--RTINVR 464
Cdd:PRK14243   11 LRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 FLREIIGVVSQEPVLFATTIAENIRYG-REN---VTMDE-IEKAVKEANAYDFIMklphkfDTLvGERGAQLSGGQKQRI 539
Cdd:PRK14243   88 EVRRRIGMVFQKPNPFPKSIYDNIAYGaRINgykGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   540 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFD 602
Cdd:PRK14243  161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
1053-1249 5.35e-25

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 104.86  E-value: 5.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLrahlgIVSQEPILFD-CSIAENI 1131
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1132 AYGDNS-----RVVSQEEIVRAakeaniHAFIESLpnkysTKVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:TIGR01184   76 ALAVDRvlpdlSKSERRAIVEE------HIALVGL-----TEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 42741659   1206 LDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNG 1249
Cdd:TIGR01184  145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
391-562 6.01e-25

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 108.01  E-value: 6.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   391 NLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRfLREIi 470
Cdd:PRK11650    3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRDI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQEPVLFA-TTIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLphkfDTLVGERGAQLSGGQKQRIAIARALVR 547
Cdd:PRK11650   79 AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
                         170
                  ....*....|....*
gi 42741659   548 NPKILLLDEATSALD 562
Cdd:PRK11650  152 EPAVFLFDEPLSNLD 166
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1047-1255 7.21e-25

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 105.17  E-value: 7.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1047 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVL-LDGKEIKRLNVQWLRAHLGIVS---QEPIL 1122
Cdd:COG1119   13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWELRKRIGLVSpalQLRFP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1123 FDCSIAENIAYGDNS-----RVVSQEEIVRAakEANIHAF-IESLPNK-YSTkvgdkgtqLSGGQKQRIAIARALVRQPH 1195
Cdd:COG1119   93 RDETVLDVVLSGFFDsiglyREPTDEQRERA--RELLELLgLAHLADRpFGT--------LSQGEQRRVLIARALVKDPE 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1196 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVFQNGRVKEHG 1255
Cdd:COG1119  163 LLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAG 225
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1049-1255 7.38e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 104.99  E-value: 7.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP-IL 1122
Cdd:PRK14247   15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1123 FDCSIAENIAYGD--NSRVVSQEEIVRAAKEANIHAfieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:PRK14247   95 PNLSIFENVALGLklNRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1201 EATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVFQNGRVKEHG 1255
Cdd:PRK14247  172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1038-1261 1.05e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 104.74  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1038 GEVVFN----YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---LAGKVLLDGKEIKRLNVQ 1107
Cdd:PRK14246    7 AEDVFNisrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1108 WLRAHLGIVSQEPILF-DCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFieSLPNKYSTKVGDKGTQLSGGQKQRIAI 1186
Cdd:PRK14246   87 KLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTI 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:PRK14246  165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
392-610 1.10e-24

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 110.16  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPS-RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTT----VQLMQRLYDPTEGMVSVDGQDIRTINVRFL 466
Cdd:COG4172    7 LSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  467 REI----IGVVSQEPV-----LFatTI----AENIRYGReNVTMDEIEKAVKE-------------ANAYdfimklPHkf 520
Cdd:COG4172   87 RRIrgnrIAMIFQEPMtslnpLH--TIgkqiAEVLRLHR-GLSGAAARARALEllervgipdperrLDAY------PH-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  521 dtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAvvQVaLD-----KARKGRTTIVIAHRLSTVRN- 594
Cdd:COG4172  156 ---------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQA--QI-LDllkdlQRELGMALLLITHDLGVVRRf 223
                        250
                 ....*....|....*.
gi 42741659  595 ADVIAGFDDGVIVEKG 610
Cdd:COG4172  224 ADRVAVMRQGEIVEQG 239
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1050-1232 1.26e-24

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 107.61  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1050 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlnVQWLRAHLGIVSQEPILF-DCSIA 1128
Cdd:PRK11607   32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENIAYGdnsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1208
Cdd:PRK11607  110 QNIAFG-----LKQDKLPKAEIASRVNEMLGLVHMQEFAK--RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
                         170       180
                  ....*....|....*....|....*.
gi 42741659  1209 ESEKVVQ-EALD-KAREGRTCIVIAH 1232
Cdd:PRK11607  183 KLRDRMQlEVVDiLERVGVTCVMVTH 208
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
711-1008 1.52e-24

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 105.21  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIgvftriDDPETKRQNSNLFSLLfLALGIISFITFFLQGFTFGKAGEILTKRLRY 790
Cdd:cd18551    1 LILALLLSLLGTAASLAQPLLVKNLI------DALSAGGSSGGLLALL-VALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  791 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKgaigsrlAVITQNIANLGTGII-------ISFIYGWQLTLLLLA 863
Cdd:cd18551   74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  864 IVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFS 943
Cdd:cd18551  145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  944 FTQAMMYFSYAGCFRFGAYLVAHKLMSFED----VLLVFSAVvfgaMAVGQVSSFAPDYAKAKISAAHI 1008
Cdd:cd18551  225 LMGLAVQLALLVVLGVGGARVASGALTVGTlvafLLYLFQLI----TPLSQLSSFFTQLQKALGALERI 289
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
406-622 1.53e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 106.09  E-value: 1.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVD----GQDIRTI------------NVRFLREI 469
Cdd:PRK13631   38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 IGVVSQEP--VLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPHKFDtlvgERGA-QLSGGQKQRIAIARALV 546
Cdd:PRK13631  118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL----ERSPfGLSGGQKRRVAIAGILA 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659   547 RNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGIY 622
Cdd:PRK13631  193 IQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
1035-1262 1.63e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 105.10  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1035 VTFGEVVFNYptRPDIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNV 1106
Cdd:PRK13634    3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1107 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEAnihafIE--SLPNKYSTKvgdKGTQLSGGQKQ 1182
Cdd:PRK13634   81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1183 RIAIARALVRQPHILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1258
Cdd:PRK13634  153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231

                  ....
gi 42741659  1259 QLLA 1262
Cdd:PRK13634  232 EIFA 235
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1052-1255 1.90e-24

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 102.66  E-value: 1.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFD-CSIAEN 1130
Cdd:cd03264   15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IAY-----GDNSRVVsQEEIVRAAKEANihafiesLPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:cd03264   93 LDYiawlkGIPSKEV-KARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1206 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:cd03264  161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
410-615 2.65e-24

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 102.45  E-value: 2.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVrflREIIGVVSQEPvlfattIAEN 487
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREV---RRRIGIVFQDL------SVDD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  488 IRYGRENVTM---------DEIEKAVKEANAYdfiMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEAT 558
Cdd:cd03265   87 ELTGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  559 SALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:cd03265  160 IGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1052-1263 2.82e-24

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 103.51  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-------------RLNVQWLRAHLGIVSQ 1118
Cdd:PRK10619   20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1119 EPILFD-CSIAENI--AYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPH 1195
Cdd:PRK10619  100 HFNLWShMTVLENVmeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPV-------HLSGGQQQRVSIARALAMEPE 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1196 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLLAQ 1263
Cdd:PRK10619  173 VLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLFGN 242
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1051-1263 2.91e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 104.01  E-value: 2.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQW-LRAHLGIVSQEPilfDCSIA- 1128
Cdd:PRK13633   24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNP---DNQIVa 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ----ENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:PRK13633  101 tiveEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFD 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1201 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK13633  170 EPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
392-619 3.45e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 104.33  E-value: 3.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI----RTINVRF 465
Cdd:PRK13634    3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHK------FDtlvgergaqLSGGQKQ 537
Cdd:PRK13634   83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   538 RIAIARALVRNPKILLLDEATSALDTES--EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 614
Cdd:PRK13634  153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGrkEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232

                  ....*
gi 42741659   615 LMKEK 619
Cdd:PRK13634  233 IFADP 237
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
142-365 3.59e-24

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 104.05  E-value: 3.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  142 RQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAI 221
Cdd:cd18551   66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  222 SPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 301
Cdd:cd18551  146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  302 AFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 365
Cdd:cd18551  226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
390-588 4.18e-24

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 108.74  E-value: 4.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  390 GNLEFRNVHFSYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSV-DGQDirtinVRFLre 468
Cdd:COG4178  361 GALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR-----VLFL-- 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 iigvvSQEPVLFATTIAENIRY--GRENVTMDEIEKAVKEANaydfimkLPH---KFDTlVGERGAQLSGGQKQRIAIAR 543
Cdd:COG4178  432 -----PQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGHlaeRLDE-EADWDQVLSLGEQQRLAFAR 498
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 42741659  544 ALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 588
Cdd:COG4178  499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
394-696 4.43e-24

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 107.84  E-value: 4.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  394 FRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirtiNVRflreiIGVV 473
Cdd:COG0488    1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  474 SQEPVLFAT-TIAENIRYGRENV--TMDEIEKAVKEANAYDFIM----KLPHKFDTLVG---ERGA-------------- 529
Cdd:COG0488   67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAKLAEPDEDLerlaELQEEFEALGGweaEARAeeilsglgfpeedl 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  530 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqvaldKARKGrTTIVIAH-R--LSTVrnADV 597
Cdd:COG0488  147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV--ATR 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  598 IAGFDDGVIVE-KGNHDELMkekgiyfklvtmqtagnevelenaadESKSEIDALEMSSNDSRSSLIRK------RSTRR 670
Cdd:COG0488  219 ILELDRGKLTLyPGNYSAYL--------------------------EQRAERLEQEAAAYAKQQKKIAKeeefirRFRAK 272
                        330       340
                 ....*....|....*....|....*...
gi 42741659  671 SVRGSQAQDRKlstK--EALDESIPPVS 696
Cdd:COG0488  273 ARKAKQAQSRI---KalEKLEREEPPRR 297
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1043-1232 4.61e-24

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 103.02  E-value: 4.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1043 NYP-TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEikrlnVQWLRAHLGIVSQEPI 1121
Cdd:COG4525   12 RYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGVVFQKDA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1122 LFD-CSIAENIAYGDNSRVVSQEEIVRAAKEanihafieslpnkYSTKVGDKGT------QLSGGQKQRIAIARALVRQP 1194
Cdd:COG4525   87 LLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIARALAADP 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42741659 1195 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1232
Cdd:COG4525  154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
PTZ00243 PTZ00243
ABC transporter; Provisional
375-626 4.75e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 110.25  E-value: 4.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   375 IDSYSKSGHKPDNIK-GNLEFRNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS 452
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   453 VDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLS 532
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYS 1447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   533 GGQKQRIAIARALV-RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 611
Cdd:PTZ00243 1448 VGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
                         250
                  ....*....|....*.
gi 42741659   612 HDEL-MKEKGIYFKLV 626
Cdd:PTZ00243 1528 PRELvMNRQSIFHSMV 1543
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
392-615 5.24e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 103.34  E-value: 5.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK13652    4 IETRDLCYSYSGSKEA--LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEP--VLFATTIAENIRYGRENVTMDE------IEKAVKEANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 543
Cdd:PRK13652   82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   544 ALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK13652  151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
711-1008 5.91e-24

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 103.67  E-value: 5.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGglqpAFAIIFSKIIGVFtrIDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRL 788
Cdd:cd18542    1 YLLAILALLLAT----ALNLLIPLLIRRI--IDSviGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  789 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPII 868
Cdd:cd18542   75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  869 AIAGVVEMKMLsGQALKDKKELEGS-GKIATEAIENFRTVVSLTQE----QKFEHMYAQslqvpYRN-SLRKAHIFGITF 942
Cdd:cd18542  153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDlNIKLAKLLAKYW 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  943 SFTQAMMYFSYAGCFRFGAYLVAHKLMSFeDVLLVFSAVVFG-AMAVGQVSSFAPDYAKAKISAAHI 1008
Cdd:cd18542  227 PLMDFLSGLQIVLVLWVGGYLVINGEITL-GELVAFISYLWMlIWPVRQLGRLINDMSRASASAERI 292
cbiO PRK13641
energy-coupling factor transporter ATPase;
1043-1264 6.33e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 103.37  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1043 NYPTRPDIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK----RLNVQWLRAHLG 1114
Cdd:PRK13641    9 DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1115 IVSQ--EPILFDCSIAENIAYGDNSRVVSQEEivraAKEANIhafieslpnKYSTKVG------DKGT-QLSGGQKQRIA 1185
Cdd:PRK13641   89 LVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1186 IARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK13641  156 IAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD 235

                  .
gi 42741659  1264 K 1264
Cdd:PRK13641  236 K 236
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
396-604 6.59e-24

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 101.25  E-value: 6.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  396 NVHFSYPSrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMV--------SVDGQDIRTINvrflR 467
Cdd:cd03290    5 NGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRN----R 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  468 EIIGVVSQEPVLFATTIAENIRYGreNVTMDEIEKAVKEANAYD-FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALV 546
Cdd:cd03290   79 YSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  547 RNPKILLLDEATSALDTE-SEAVVQVALDKARKG--RTTIVIAHRLSTVRNADVIAGFDDG 604
Cdd:cd03290  157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
392-613 6.83e-24

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 102.01  E-value: 6.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG------QDIRTINVRF 465
Cdd:PRK11124    3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEAnaydfiMKLphkFDTLVGERGA-----QLSGGQKQR 538
Cdd:PRK11124   80 LRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKL---LERLRLKPYAdrfplHLSGGQQQR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   539 IAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 613
Cdd:PRK11124  150 VAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1052-1260 8.24e-24

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 104.78  E-value: 8.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAEN 1130
Cdd:PRK10851   17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1131 IAYG---------DNSRVVSQE-----EIVRaakeanihafIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHI 1196
Cdd:PRK10851   95 IAFGltvlprrerPNAAAIKAKvtqllEMVQ----------LAHLADRYPA-------QLSGGQKQRVALARALAVEPQI 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1197 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK10851  158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
392-610 8.55e-24

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 100.91  E-value: 8.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSY-PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREII 470
Cdd:cd03266    2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFA-TTIAENIRY--GRENVTMDEIEKAVKEanaydFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVR 547
Cdd:cd03266   81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE-----LADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  548 NPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 610
Cdd:cd03266  154 DPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1052-1255 8.84e-24

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 100.82  E-value: 8.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlRAHLGIVSQEPILF-DCSIAEN 1130
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IAYGDNSRVVSQEEIVRAAKEanihaFIESLpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:cd03269   91 LVYLAQLKGLKKEEARRRIDE-----WLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659 1211 EKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:cd03269  164 VELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1051-1255 9.14e-24

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 100.32  E-value: 9.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGKVLLDGKEIKRlnvQWLRAHLGIVSQEPILFDC-SI 1127
Cdd:cd03213   23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYgdnsrvvsqeeivrAAKeanihafiesLpnkystkvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:cd03213  100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1208 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHG 1255
Cdd:cd03213  144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
413-610 1.22e-23

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 100.26  E-value: 1.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  413 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIGVVSQEPVLFA-TTIAENIRYG 491
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  492 R------ENVTMDEIEKAVKEANAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT-- 563
Cdd:cd03298   95 LspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPal 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 42741659  564 ESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:cd03298  164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
410-616 1.38e-23

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 104.73  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI----IGVVSQEPVLFA-TTI 484
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   485 AENIRYGREnvtMDEIEKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 564
Cdd:PRK10070  124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   565 SEAVVQVALDK--ARKGRTTIVIAHRL-STVRNADVIAGFDDGVIVEKGNHDELM 616
Cdd:PRK10070  199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1051-1264 1.45e-23

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 101.63  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FDCSIAE 1129
Cdd:PRK11231   16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1130 NIAYGDNSRV-----VSQE--EIVRAAKEAnihAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:PRK11231   96 LVAYGRSPWLslwgrLSAEdnARVNQAMEQ---TRINHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1203 TSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:PRK11231  166 TTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
112-352 1.87e-23

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 102.00  E-value: 1.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  112 TRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIG 191
Cdd:cd18784   36 SRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLN 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  192 MFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQK 271
Cdd:cd18784  116 IFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  272 KELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvltvFFSVLIGAFSVGQASPS 351
Cdd:cd18784  196 GEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSCLES 271

                 .
gi 42741659  352 I 352
Cdd:cd18784  272 V 272
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
1049-1255 1.91e-23

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 99.60  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlrAHLGIVSQEPILFD-CSI 1127
Cdd:cd03268   12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPnLTA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAKEANIHAfieslpnkystkVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:cd03268   90 RENLRLLARLLGIRKKRIDEVLDVVGLKD------------SAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1207 DTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:cd03268  158 DPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
392-593 1.91e-23

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 105.88  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL---YDPTEGMVSVDGQDirtinVRF--- 465
Cdd:COG3845    6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKST---LMKILyglYQPDSGEILIDGKP-----VRIrsp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  466 ---LREIIGVVSQEPVLFAT-TIAENIRYGRENVT-----MDEIEKAVKE-ANAYDFIMKLphkfDTLVGergaQLSGGQ 535
Cdd:COG3845   75 rdaIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DLSVGE 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  536 KQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVaLDK-ARKGRTTIVIAHRLSTVR 593
Cdd:COG3845  147 QQRVEILKALYRGARILILDEPTAVLtPQEADELFEI-LRRlAAEGKSIIFITHKLREVM 205
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1040-1251 1.95e-23

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 101.32  E-value: 1.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1040 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRA-HLGIVSQ 1118
Cdd:COG1101    9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAkYIGRVFQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1119 EPILFDC---SIAEN--IAYGDNSRvvsqEEIVRAAKEANIHAFIES-------LPNKYSTKVGdkgtQLSGGQKQRIAI 1186
Cdd:COG1101   88 DPMMGTApsmTIEENlaLAYRRGKR----RGLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1251
Cdd:COG1101  160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
405-610 2.89e-23

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 99.21  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  405 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-RTINVRflrEIIGVVSQEPVLFAT- 482
Cdd:cd03268   11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEAL---RRIGALIEAPGFYPNl 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  483 TIAENIR-----YGRENVTMDEIEKAVKEANAydfimklPHKfdtlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEA 557
Cdd:cd03268   88 TARENLRllarlLGIRKKRIDEVLDVVGLKDS-------AKK-------KVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  558 TSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:cd03268  154 TNGLDPDGiKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
392-610 3.41e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 100.30  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDIRTINVRFL 466
Cdd:PRK14267    5 IETVNLRVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   467 --REIIGVVSQEPVLFA-TTIAENIRYG-------RENVTMDE-IEKAVKEANAYDFIMklphkfDTLvGERGAQLSGGQ 535
Cdd:PRK14267   82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWDEVK------DRL-NDYPSNLSGGQ 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   536 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR-LSTVRNADVIAGFDDGVIVEKG 610
Cdd:PRK14267  155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
392-616 3.58e-23

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 100.68  E-value: 3.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSY------PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF 465
Cdd:COG4167    5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  466 LREIIGVVSQEPvlfATTIAENIRYG-------RENVTMDEIEKAVKeanaydfImklphkFDTL--VGERGAQ------ 530
Cdd:COG4167   85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHanfyph 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  531 -LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 606
Cdd:COG4167  149 mLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEV 228
                        250
                 ....*....|
gi 42741659  607 VEKGNHDELM 616
Cdd:COG4167  229 VEYGKTAEVF 238
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
409-615 4.56e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 100.12  E-value: 4.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ------DIRTINVRFLREIIGVVSQEPVLFA- 481
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENIRYGRENVTMD---EIEKAVKEANAYDFIMKLPHkfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 558
Cdd:PRK14246  105 LSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWKEVY--DRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659   559 SALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK14246  182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
424-565 5.82e-23

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 102.10  E-value: 5.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  424 ALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG---QDIRT-INVRFLREIIGVVSQEPVLFAT-TIAENIRYGRenvtmd 498
Cdd:COG4148   29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFPHlSVRGNLLYGR------ 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  499 eieKAVKEANAYDfimklphKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 565
Cdd:COG4148  103 ---KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
405-606 6.08e-23

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 98.66  E-value: 6.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  405 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ----DI-----RTI-NVRflREIIGVVS 474
Cdd:COG4778   22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREIlALR--RRTIGYVS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  475 QepvlFATTIAeniRYGRENVTMDE-IEKAVKEANAYDFIMKLPHKFDtlVGERGAQL-----SGGQKQRIAIARALVRN 548
Cdd:COG4778  100 Q----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIAD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  549 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHrlstvrNADVIAGFDDGVI 606
Cdd:COG4778  171 PPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH------DEEVREAVADRVV 223
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1057-1261 6.18e-23

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 102.80  E-value: 6.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1057 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHLGIVSQE-PILFDCSIAENI 1131
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1132 AYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1211
Cdd:PRK10070  128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1212 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:PRK10070  201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1052-1255 6.27e-23

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 98.59  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFD-CSIAEN 1130
Cdd:cd03266   20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTAREN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IAY-GDnsrvvsqeeiVRAAKEANIHAFIESLPNKYSTK--VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:cd03266   99 LEYfAG----------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42741659 1208 TESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:cd03266  169 VMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1051-1254 6.52e-23

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 99.39  E-value: 6.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEikrlnVQWLRAHLGIVSQ-EPILFDCSIAE 1129
Cdd:PRK11248   15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1130 NIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1209
Cdd:PRK11248   90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1210 SEKVVQEALDK--AREGRTCIVIAHrlsTIQNA-----DLIVVFQN-GRVKEH 1254
Cdd:PRK11248  163 TREQMQTLLLKlwQETGKQVLLITH---DIEEAvfmatELVLLSPGpGRVVER 212
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
1049-1256 6.58e-23

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 99.37  E-value: 6.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPLAGKVLLDGKEIKRLNVQwLRAHLGI-VS-QEPIlf 1123
Cdd:COG0396   12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPV-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 dcsiaeniaygdnsRV--VSQEEIVRAAKEAN------IHAFIESLpNKYSTKVG----------DKGtqLSGGQKQRIA 1185
Cdd:COG0396   88 --------------EIpgVSVSNFLRTALNARrgeelsAREFLKLL-KEKMKELGldedfldryvNEG--FSGGEKKRNE 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1186 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:COG0396  151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
1041-1267 7.10e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 101.08  E-value: 7.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1041 VFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFY-----DPLAGKVLLDGKEIK 1102
Cdd:PRK13631   30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdkkNNHELITNPYSKKIK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1103 rlNVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKeanihafieslpnKYSTKVGDKGT------ 1174
Cdd:PRK13631  110 --NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK-------------FYLNKMGLDDSylersp 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1175 -QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1251
Cdd:PRK13631  175 fGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKI 254
                         250
                  ....*....|....*.
gi 42741659  1252 KEHGTHQQLLAQKGIY 1267
Cdd:PRK13631  255 LKTGTPYEIFTDQHII 270
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
410-587 7.24e-23

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 98.69  E-value: 7.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLreiigVVSQEPVLFA-TTIAENI 488
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    489 RYGRENVTMD----EIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 564
Cdd:TIGR01184   76 ALAVDRVLPDlsksERRAIVEEHIALVGLTEAADK-------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
                          170       180
                   ....*....|....*....|....*
gi 42741659    565 SEAVVQVALDK--ARKGRTTIVIAH 587
Cdd:TIGR01184  149 TRGNLQEELMQiwEEHRVTVLMVTH 173
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
408-619 9.03e-23

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 99.32  E-value: 9.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   408 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVL-FATTIAE 486
Cdd:PRK11231   16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   487 NIRYGRE------NVTMDEIEKAVKEAnaydfiMKLPHkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK11231   96 LVAYGRSpwlslwGRLSAEDNARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   561 LDTESeavvQVALDK-----ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:PRK11231  169 LDINH----QVELMRlmrelNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
392-619 9.79e-23

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 98.37  E-value: 9.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-RTINVRFLREII 470
Cdd:TIGR03410    1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    471 GVVSQEPVLFAT-TIAENIRYGREnvTMDEIEKAVKeanayDFIMKL-PHKFDTLvGERGAQLSGGQKQRIAIARALVRN 548
Cdd:TIGR03410   78 AYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659    549 PKILLLDEATSALD----TESEAVVQvaLDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:TIGR03410  150 PKLLLLDEPTEGIQpsiiKDIGRVIR--RLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1050-1250 1.05e-22

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 98.28  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1050 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdgkeikRLNVQW-------------LRAH-LGI 1115
Cdd:COG4778   24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV------RHDGGWvdlaqaspreilaLRRRtIGY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1116 VSQ---------------EPILfdcsiaeniaygdnSRVVSQEEIVRAAKEA----NIHafiESL----PNKYStkvgdk 1172
Cdd:COG4778   98 VSQflrviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLP---ERLwdlpPATFS------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1173 gtqlsGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:COG4778  155 -----GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
1052-1232 1.84e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 98.38  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEIKRLNVQWL--RAHLGIVSQEPILF- 1123
Cdd:PRK14267   19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIAYGD--NSRVVSQEEIVRAAKEANIHAfieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PRK14267   99 HLTIYDNVAIGVklNGLVKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
                         170       180       190
                  ....*....|....*....|....*....|.
gi 42741659  1202 ATSALDTESEKVVQEALDKAREGRTCIVIAH 1232
Cdd:PRK14267  176 PTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1052-1251 1.94e-22

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 97.34  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE---RFYDPLAGKVLLDGKEIKRlnVQWLRaHLGIVSQEPILFDC-SI 1127
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSR--VVSQEEI--VRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:cd03234   99 RETLTYTAILRlpRKSSDAIrkKRVEDVLLRDLALTRIGGNLVK-------GISGGERRRVSIAVQLLWDPKVLILDEPT 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1204 SALDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVFQNGRV 1251
Cdd:cd03234  172 SGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1057-1264 1.97e-22

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 97.35  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1057 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILFD-CSIAENIAYGD 1135
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1136 NSRV---VSQEEIVRA-AKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1207
Cdd:PRK10771   97 NPGLklnAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1208 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:PRK10771  166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
711-981 2.32e-22

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 99.03  E-value: 2.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRqnsnLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 790
Cdd:cd18552    1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  791 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 870
Cdd:cd18552   77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  871 AGVV---EMKMLSgqalkdKKELEGSGKIAT---EAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSF 944
Cdd:cd18552  155 PIRRigkRLRKIS------RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPL 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 42741659  945 TQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAV 981
Cdd:cd18552  229 MELLGAIAIALVLWYGGYQVISGELTPGEFISFITAL 265
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1051-1262 3.01e-22

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 96.84  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRAHLGI--VSQEPILF-DCSI 1127
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1128 AENIAYGDNSRVVSQEEIVRAAkEANIHAF-IESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:cd03218   93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1207 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:cd03218  165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1044-1263 3.16e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 98.34  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1044 YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP--I 1121
Cdd:PRK13652   11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1122 LFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PRK13652   91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1202 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK13652  164 PTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
365-589 3.37e-22

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 104.22  E-value: 3.37e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    365 IFKIIDnKPSIDSYSKSGHKPDNIKGNLEFRNVHFS--YPSRKEV--------------KILKGLNLKVQSGQTVALVGN 428
Cdd:TIGR01271 1175 VFKFID-LPQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMdvqgltakyteagrAVLQDLSFSVEGGQRVGLLGR 1253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    429 SGCGKSTTVQLMQRLYDpTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRyGRENVTMDEIEKAVKEAN 508
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVG 1331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    509 AYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 588
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411

                   .
gi 42741659    589 L 589
Cdd:TIGR01271 1412 V 1412
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
413-616 3.39e-22

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 99.80  E-value: 3.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    413 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG---QDIRT-INVRFLREIIGVVSQEPVLFA-TTIAEN 487
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    488 IRYGRENVTMDEieKAVKEANAYDfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 567
Cdd:TIGR02142   96 LRYGMKRARPSE--RRISFERVIE-LLGIGH----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 42741659    568 VVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELM 616
Cdd:TIGR02142  169 EILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
392-618 3.73e-22

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 97.06  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQR-LYDPTEGMVSVDGQDI--RTINVR--- 464
Cdd:COG0396    1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDIleLSPDERara 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  465 --FL-----REIIGV-VSQepvlFATTIAENIRygRENVTMDEIEKAVKEANAydfIMKLPHKFdtlvGERG--AQLSGG 534
Cdd:COG0396   78 giFLafqypVEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  535 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKGN 611
Cdd:COG0396  145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224

                 ....*..
gi 42741659  612 HdELMKE 618
Cdd:COG0396  225 K-ELALE 230
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
409-564 4.02e-22

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 96.01  E-value: 4.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TEGMVSVDGQDIRTINVRfLREIiGVVSQEPVLFA-TTI 484
Cdd:COG4136   16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRI-GILFQDDLLFPhLSV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  485 AENIRYG-RENVTM----DEIEKAVKEANaydfimkLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATS 559
Cdd:COG4136   94 GENLAFAlPPTIGRaqrrARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALLLDEPFS 162

                 ....*
gi 42741659  560 ALDTE 564
Cdd:COG4136  163 KLDAA 167
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
392-608 6.09e-22

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 96.65  E-value: 6.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflrEII- 470
Cdd:COG0411    5 LEVRGLTKRF---GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIAr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 -GVVS--QEPVLFAT-TIAENIRYGRENVTMDEIEKAV--------KEANAYDFIM------KLPHKFDTLVGErgaqLS 532
Cdd:COG0411   79 lGIARtfQNPRLFPElTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  533 GGQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDG-VIVE 608
Cdd:COG0411  155 YGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
393-622 6.98e-22

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 96.31  E-value: 6.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  393 EFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 472
Cdd:COG4604    3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  473 VSQEPVlFAT--TIAENIRYGR-----ENVTmDEIEKAVKEANAYDFIMKLPHKF-DtlvgergaQLSGGQKQRIAIARA 544
Cdd:COG4604   80 LRQENH-INSrlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  545 LVRNPKILLLDEATSALDTesEAVVQV--ALDKA--RKGRTTIVIAHRLstvrN-----ADVIAGFDDGVIVEKGNHDEL 615
Cdd:COG4604  150 LAQDTDYVLLDEPLNNLDM--KHSVQMmkLLRRLadELGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEI 223
                        250
                 ....*....|
gi 42741659  616 MKE---KGIY 622
Cdd:COG4604  224 ITPevlSDIY 233
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1046-1253 7.42e-22

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 96.68  E-value: 7.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN----------VQWL------ 1109
Cdd:PRK10419   21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1110 ----RAHLGIVSQEPI--LFDCSIAENIAygdnsRVvsqEEIVRAAKEANIHAfiESLPnkystkvgdkgTQLSGGQKQR 1183
Cdd:PRK10419  101 avnpRKTVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSVL--DKRP-----------PQLSGGQLQR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1184 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1253
Cdd:PRK10419  160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
409-622 8.14e-22

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 96.85  E-value: 8.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDpTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI 488
Cdd:cd03289   19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  489 R-YGRENvtMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 567
Cdd:cd03289   98 DpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  568 VVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIY 622
Cdd:cd03289  176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
392-589 8.45e-22

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 100.85  E-value: 8.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 470
Cdd:PRK10762    5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQEPVLFAT-TIAENIRYGRENVT-MDEIE--KAVKEANAYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALV 546
Cdd:PRK10762   82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 42741659   547 RNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRL 589
Cdd:PRK10762  158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRL 201
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1046-1261 8.77e-22

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 99.53  E-value: 8.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FD 1124
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 CSIAENIAYGDN---SRVVSQEEIVRAAKEanihafiESLPNKYSTKVGDKG-TQLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:PRK09536   92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1201 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:PRK09536  165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1051-1247 1.07e-21

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 95.17  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN 1130
Cdd:PRK10247   21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1131 IAYGDNSRVVSQEEivrAAKEANIHAFieSLPNKYSTKvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:PRK10247  101 LIFPWQIRNQQPDP---AIFLDDLERF--ALPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 42741659  1211 EKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVFQ 1247
Cdd:PRK10247  173 KHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
392-610 1.08e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 100.55  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRK--------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPTEGMVSVDGQDIRTINV 463
Cdd:PRK15134  276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   464 RFL---REIIGVVSQEP---------VLfaTTIAENIRYGRENVTMDEIEKAVKEAnaydfiMK-------LPHKFDtlv 524
Cdd:PRK15134  355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------MEevgldpeTRHRYP--- 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   525 gergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVqVALDKARKGR---TTIVIAHRLSTVRNA--DVIA 599
Cdd:PRK15134  424 ----AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQQKhqlAYLFISHDLHVVRALchQVIV 498
                         250
                  ....*....|.
gi 42741659   600 gFDDGVIVEKG 610
Cdd:PRK15134  499 -LRQGEVVEQG 508
PTZ00243 PTZ00243
ABC transporter; Provisional
1044-1278 1.08e-21

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 102.55  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1044 YPTRPDIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVlldgkeikrlnvqWLRAHLGIVSQEPILF 1123
Cdd:PTZ00243  668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIAYGDNSRVVSQEEIVRAAKeanIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:PTZ00243  734 NATVRGNILFFDEEDAARLADAVRVSQ---LEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1204 SALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVSVQAGTK 1278
Cdd:PTZ00243  811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKENK 885
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
708-1264 1.71e-21

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 101.91  E-value: 1.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    708 WPYFVVGVFCAI--INGGLQPafaIIFSKIIGVFtridDPETKRQNSNLFsllFLALGI-ISFI--TFFLQGFTFG--KA 780
Cdd:TIGR01271   80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASY----DPFNAPEREIAY---YLALGLcLLFIvrTLLLHPAIFGlhHL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    781 GEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVItqnIANLGTGIIISFIygWQLT-- 858
Cdd:TIGR01271  150 GMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVW---IAPLQVILLMGLI--WELLev 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    859 --------LLLLAIVPiiAIAGVVEMKMLSGQALKDKKELegsgKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRN 930
Cdd:TIGR01271  223 ngfcglgfLILLALFQ--ACLGQKMMPYRDKRAGKISERL----AITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKL 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    931 SlRKAhifGITFSFTQAMMYFSyaGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIM 1010
Cdd:TIGR01271  297 T-RKI---AYLRYFYSSAFFFS--GFFVVFLSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAIT 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1011 IIEKTPLIDSYSTEGLMPNTLE---GNVT------FGEVV--------------------FNYPTRPDIPVLQGLSLEVK 1061
Cdd:TIGR01271  371 KIQDFLCKEEYKTLEYNLTTTEvemVNVTaswdegIGELFekikqnnkarkqpngddglfFSNFSLYVTPVLKNISFKLE 450
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1062 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnvqwlrahLGIVSQEPILFDCSIAENIAYG---DNSR 1138
Cdd:TIGR01271  451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGlsyDEYR 517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1139 VVSqeeIVRAAK-EANIHAFieslPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEA 1217
Cdd:TIGR01271  518 YTS---VIKACQlEEDIALF----PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 42741659   1218 -LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:TIGR01271  591 cLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1049-1262 2.25e-21

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 95.46  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI---KRlNVQWLRAHLGIVSQEP--ILF 1123
Cdd:PRK13638   13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKR-GLLALRQQVATVFQDPeqQIF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIAYGDNSRVVSQEEIVRAAKEAnihafieslpnkySTKVGDKGTQ------LSGGQKQRIAIARALVRQPHIL 1197
Cdd:PRK13638   92 YTDIDSDIAFSLRNLGVPEAEITRRVDEA-------------LTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1198 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK13638  159 LLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
392-589 2.28e-21

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 95.15  E-value: 2.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVH--FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIrTinvrFLRE- 468
Cdd:COG1101    2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-T----KLPEy 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 ----IIGVVSQEPVL---FATTIAEN------------IRYGRENVTMDEIEKAVKEANaydfiMKLPHKFDTLVGerga 529
Cdd:COG1101   77 krakYIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG---- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  530 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRL 589
Cdd:COG1101  148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
cbiO PRK13643
energy-coupling factor transporter ATPase;
1043-1256 2.47e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 95.96  E-value: 2.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1043 NYPTRPDIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKV----LLDGKEIKRLNVQWLRAHLG 1114
Cdd:PRK13643    8 NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRKKVG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1115 IVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEaniHAFIESLPNKYSTKvgdKGTQLSGGQKQRIAIARALVR 1192
Cdd:PRK13643   88 VVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAM 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1193 QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:PRK13643  162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
711-971 2.78e-21

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 95.92  E-value: 2.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFtrIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 790
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAIDDY--IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  791 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 870
Cdd:cd18544   79 DLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  871 AGVVeMKMLSGQALKDKKEL--EGSGKIAtEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAM 948
Cdd:cd18544  157 ATYL-FRKKSRKAYREVREKlsRLNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELL 234
                        250       260
                 ....*....|....*....|...
gi 42741659  949 MYFSYAGCFRFGAYLVAHKLMSF 971
Cdd:cd18544  235 SSLALALVLWYGGGQVLSGAVTL 257
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
392-610 3.29e-21

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 94.45  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK13548    3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVL-FATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVR- 547
Cdd:PRK13548   80 VLPQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAALA---QVDLAH----LAGRDYPQLSGGEQQRVQLARVLAQl 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659   548 -----NPKILLLDEATSALD-TESEAVVQVALDKARK-GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 610
Cdd:PRK13548  153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
392-562 3.47e-21

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 93.76  E-value: 3.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-RFLREII 470
Cdd:cd03218    1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYDFIMKLPHKFdtlvgerGAQLSGGQKQRIAIARALVR 547
Cdd:cd03218   78 GYLPQEASIFRKlTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALAT 150
                        170
                 ....*....|....*
gi 42741659  548 NPKILLLDEATSALD 562
Cdd:cd03218  151 NPKFLLLDEPFAGVD 165
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1048-1263 3.62e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 98.83  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQ-WLRAHLGIVSQEPILF-DC 1125
Cdd:PRK11288   15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGD--NSR-VVSQEEIVRAAKEANIHAFIESLPNkysTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:PRK11288   95 TVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  1203 TSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNGR-VKEHG-----THQQLLAQ 1263
Cdd:PRK11288  168 TSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRyVATFDdmaqvDRDQLVQA 236
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1051-1264 3.74e-21

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 95.31  E-value: 3.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnvqwlrahLGIVSQEPILFDCSIAEN 1130
Cdd:cd03291   51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IAYG---DNSRVVSqeeIVRAAK-EANIHAFieslPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:cd03291  118 IIFGvsyDEYRYKS---VVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1207 DTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:cd03291  191 DVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1048-1254 3.77e-21

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.98  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEIKR-LNVQwlrahLGIVSQEPILFDcs 1126
Cdd:COG0488  326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL-------AGELEPDSGTVKLgETVK-----IGYFDQHQEELD-- 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 iaeniaygDNSRVVsqEEIVRAA---KEANIHAFIESL---PNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:COG0488  392 --------PDKTVL--DELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLD 457
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1201 EATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVFQNGRVKEH 1254
Cdd:COG0488  458 EPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
146-335 4.46e-21

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 95.10  E-value: 4.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  146 KIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVL 225
Cdd:cd18590   70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  226 GLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 305
Cdd:cd18590  150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
                        170       180       190
                 ....*....|....*....|....*....|
gi 42741659  306 IYASYALAFWYGTTLVLSGEYSIGQVLTVF 335
Cdd:cd18590  230 QLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1034-1207 5.19e-21

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 96.45  E-value: 5.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1034 NVTFGEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpLAGKVLLDGKEIKRLnvqwlr 1110
Cdd:PRK11650    3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1111 ahlgivsqEPILFDC-------------SIAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkg 1173
Cdd:PRK11650   72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR---------- 133
                         170       180       190
                  ....*....|....*....|....*....|....
gi 42741659  1174 tQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK11650  134 -ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1036-1251 5.72e-21

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 98.18  E-value: 5.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1036 TFGEVVFNyptrpdipvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-VQWLRAHLG 1114
Cdd:COG3845   14 RFGGVVAN----------DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1115 IVSQEPILFDC-SIAENIAYGDNSRVVSQEEIVRAAKEanihafIESLPNKY------STKVGDkgtqLSGGQKQRIAIA 1187
Cdd:COG3845   84 MVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEIL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1188 RALVRQPHILLLDEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1251
Cdd:COG3845  154 KALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
392-649 7.03e-21

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 94.79  E-value: 7.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINvrflREIIG 471
Cdd:COG4152    2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT-TIAENIRY-GR-ENVTMDEIEKAVKEanaydfIMKlphKFDtlVGERGA----QLSGGQKQRIAIARA 544
Cdd:COG4152   75 YLPEERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADE------WLE---RLG--LGDRANkkveELSKGNQQKVQLIAA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  545 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEKGIy 622
Cdd:COG4152  144 LLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR- 222
                        250       260
                 ....*....|....*....|....*..
gi 42741659  623 fKLVTMQTAGNEVELENAADESKSEID 649
Cdd:COG4152  223 -NTLRLEADGDAGWLRALPGVTVVEED 248
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
392-604 7.15e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 98.08  E-value: 7.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQDIRTINVRFL 466
Cdd:PRK13549    6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKST---LMKVLsgvypHGTYEGEIIFEGEELQASNIRDT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   467 REI-IGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:PRK13549   80 ERAgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659   545 LVRNPKILLLDEATSALdTESEAVVQVAL--DKARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 604
Cdd:PRK13549  158 LNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
cbiO PRK13643
energy-coupling factor transporter ATPase;
392-618 7.57e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 94.42  E-value: 7.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEV--KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRF 465
Cdd:PRK13643    2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   466 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKE-----ANAYDFIMKLPHkfdtlvgergaQLSGGQK 536
Cdd:PRK13643   82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSPF-----------ELSGGQM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   537 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 614
Cdd:PRK13643  151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230

                  ....
gi 42741659   615 LMKE 618
Cdd:PRK13643  231 VFQE 234
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1052-1262 1.13e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 93.62  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG-----KVLLDGKEI-KRLNVQWLRAHLGIVSQEPILFDC 1125
Cdd:PRK14271   36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGDNSRVVSQEEIVRAAKEANIHAFieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:PRK14271  116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1206 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK14271  194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1052-1258 1.21e-20

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 92.38  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDG------KEIKRLNVQWLRAHLGIVSQE----PI 1121
Cdd:PRK11124   17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1122 LfdcSIAENIAYGDnSRV--VSQEEIVRAAKEA----NIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPH 1195
Cdd:PRK11124   97 L---TVQQNLIEAP-CRVlgLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1196 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1258
Cdd:PRK11124  162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
1052-1256 1.22e-20

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 92.20  E-value: 1.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlRAHLGI--VSQEPILF-DCSIA 1128
Cdd:TIGR03410   15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1129 ENIAYGDNsrvvsqeeiVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1208
Cdd:TIGR03410   94 ENLLTGLA---------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 42741659   1209 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGT 1256
Cdd:TIGR03410  165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1053-1257 1.25e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 91.86  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEP-ILFDCSIA 1128
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENIAYGDNSRVVSQEEIVRAAKEAnihafieslpnkySTKVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:PRK10908   98 DNVAIPLIIAGASGDDIRRRVSAA-------------LDKVGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1203 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVFQNGRVkeHGTH 1257
Cdd:PRK10908  165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1048-1246 1.29e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 91.14  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlrahlgiVSQEPILFDCSI 1127
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSLPLTV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1128 AENIAYGDNSRVVSQEEIVRAAKEANIHAF----IESLPNKystKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:NF040873   75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALervgLADLAGR---QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 42741659  1204 SALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1246
Cdd:NF040873  148 TGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1051-1257 1.30e-20

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 92.38  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDG------KEIKRLNVQWLRAHLGIVSQE----P 1120
Cdd:COG4161   16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQynlwP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1121 ILfdcSIAENIAYG-----DNSRVVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPH 1195
Cdd:COG4161   96 HL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFPL-----------HLSGGQQQRVAIARALMMEPQ 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1196 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTH 1257
Cdd:COG4161  162 VLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1052-1251 1.49e-20

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 90.57  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV-QWLRAHLGIVSQEP----ILFDCS 1126
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 IAENIAYGDnsrvvsqeeivraakeanihafieslpnkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:cd03215   95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1207 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1251
Cdd:cd03215  136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
1041-1260 1.50e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 94.00  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1041 VFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKV---LLDGKEIKRL------------- 1104
Cdd:PRK13651   11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTkekekvleklviq 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1105 --------NVQWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEanihaFIE--SLPNKYSTKvgdK 1172
Cdd:PRK13651   91 ktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDESYLQR---S 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1173 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVFQNGR 1250
Cdd:PRK13651  163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
                         250
                  ....*....|.
gi 42741659  1251 -VKEHGTHQQL 1260
Cdd:PRK13651  243 iIKDGDTYDIL 253
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
403-610 1.52e-20

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 95.68  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   403 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVL-FA 481
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENIRYGREN-----VTMDE-----IEKAVKEANAYDFIMKlphKFDTlvgergaqLSGGQKQRIAIARALVRNPKI 551
Cdd:PRK09536   92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659   552 LLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 610
Cdd:PRK09536  161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
120-344 2.51e-20

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 93.35  E-value: 2.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  120 GIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMAT 199
Cdd:cd18564   62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  200 FFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNK 279
Cdd:cd18564  142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  280 NLEEAKRIGIK-KAITANISIGAAfLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFSVLIGAFS 344
Cdd:cd18564  222 ENRKSLRAGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYK 285
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1048-1250 2.74e-20

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 96.15  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGKVLLDGKEIKRLNVQWL-RAHLGIVSQEPILF 1123
Cdd:PRK13549   16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 -DCSIAENIAYGD---NSRVVSQEEIVRAAKE--ANIHAFIEslPNkysTKVGDkgtqLSGGQKQRIAIARALVRQPHIL 1197
Cdd:PRK13549   95 kELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDIN--PA---TPVGN----LGLGQQQLVEIAKALNKQARLL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1198 LLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:PRK13549  166 ILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
396-619 2.89e-20

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 92.61  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  396 NVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrflreiIGVVSQ 475
Cdd:cd03291   39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  476 EPVLFATTIAENIRYGrenVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 553
Cdd:cd03291  106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  554 LDEATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:cd03291  183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
109-337 3.43e-20

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 92.47  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  109 EDMTRYAYYYSGIGAGVLVAAYIQVSFWcLAAGRQI-HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIG 187
Cdd:cd18541   37 SQLLRYALLILLLALLIGIFRFLWRYLI-FGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  188 DKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAF 267
Cdd:cd18541  116 PGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAF 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  268 GGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFS 337
Cdd:cd18541  196 VQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD-LVAFNS 264
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
392-618 4.53e-20

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 95.36  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR-FLREII 470
Cdd:PRK11288    5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQE----PVLfatTIAENIRYGRenvtmdeiekavkeanaydfimkLPHKF-----DTLVGERGAQL---------- 531
Cdd:PRK11288   82 AIIYQElhlvPEM---TVAENLYLGQ-----------------------LPHKGgivnrRLLNYEAREQLehlgvdidpd 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   532 ------SGGQKQRIAIARALVRNPKILLLDEATSALDT-ESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDD 603
Cdd:PRK11288  136 tplkylSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKD 215
                         250       260
                  ....*....|....*....|.
gi 42741659   604 GVIVE------KGNHDELMKE 618
Cdd:PRK11288  216 GRYVAtfddmaQVDRDQLVQA 236
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1049-1255 6.77e-20

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 93.17  E-value: 6.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikRLN-VQWLRAHLGIVSQEPILF-DCS 1126
Cdd:PRK11000   15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNdVPPAERGVGMVFQSYALYpHLS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1127 IAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:PRK11000   92 VAENMSFGLKLAGAKKEEINQrvnqVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1203 TSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1255
Cdd:PRK11000  161 LSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
392-610 6.83e-20

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 89.65  E-value: 6.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINvrflREIIG 471
Cdd:cd03269    1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLF-ATTIAENIRYGRENVTMdEIEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVRNPK 550
Cdd:cd03269   74 YLPEERGLYpKMKVIDQLVYLAQLKGL-KKEEARRRIDEWLERLELSEYAN----KRVEELSKGNQQKVQFIAAVIHDPE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  551 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 610
Cdd:cd03269  149 LLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
392-618 7.32e-20

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 89.12  E-value: 7.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQDIR--TINVR 464
Cdd:cd03217    1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  465 FlREIIGVVSQEPVLFA-TTIAENIRYGRENvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIAR 543
Cdd:cd03217   75 A-RLGIFLAFQYPPEIPgVKNADFLRYVNEG------------------------------------FSGGEKKRNEILQ 117
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  544 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKGNhDELMKE 618
Cdd:cd03217  118 LLLLEPDLAILDEPDSGLDIDAlRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
414-616 7.65e-20

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 90.03  E-value: 7.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   414 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIGVVSQEPVLFA-TTIAENIRYG- 491
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   492 RENVTMDEIEKAVKEANAY-----DFIMKLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT--E 564
Cdd:PRK10771   97 NPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalR 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   565 SEAVVQVALDKARKGRTTIVIAHRLS-TVRNAD---VIAgfdDGVIVEKGNHDELM 616
Cdd:PRK10771  166 QEMLTLVSQVCQERQLTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
392-588 8.84e-20

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 87.59  E-value: 8.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDirtiNVRFLreiig 471
Cdd:cd03223    1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 vvSQEPVLFATTIAENIRYGRENVtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03223   70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42741659  552 LLLDEATSALDTESEAVVqvaLDKARKGRTTIV-IAHR 588
Cdd:cd03223  113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1052-1262 8.85e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.77  E-value: 8.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGKVLLDGKEIKRLNVQWL---RAHLGIVSQEP---ILFDC 1125
Cdd:PRK15134  301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGDNsrvVSQEEIVRAAKEANIHAFIEslpnkystKVG-DKGT------QLSGGQKQRIAIARALVRQPHILL 1198
Cdd:PRK15134  380 NVLQIIEEGLR---VHQPTLSAAQREQQVIAVME--------EVGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1199 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK15134  449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1051-1263 9.58e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.77  E-value: 9.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----LAGKVLLDGKEIKRLNVQWLRAHLG----IVSQEPI 1121
Cdd:PRK15134   23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1122 L-------FDCSIAENIA-YGDNSRVVSQEEIVRAAKEANIHafieslpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQ 1193
Cdd:PRK15134  103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1194 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK15134  175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
PLN03232 PLN03232
ABC transporter C family member; Provisional
1042-1276 1.04e-19

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 96.20  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1042 FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdgkeikrlnvqwLRAHLGIVSQEPI 1121
Cdd:PLN03232  622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSW 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1122 LFDCSIAENIAYGDNsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PLN03232  690 IFNATVRENILFGSD---FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1202 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVSVQAG 1276
Cdd:PLN03232  767 PLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
111-337 1.23e-19

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 90.91  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  111 MTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKI 190
Cdd:cd18544   40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  191 GMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ 270
Cdd:cd18544  120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNRE 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  271 KKELERYNKNLEEAKRIGIKkaitaNISIGAAF-----LLIYASYALAFWYGTTLVLSGEYSIGqVLTVFFS 337
Cdd:cd18544  200 KREFEEFDEINQEYRKANLK-----SIKLFALFrplveLLSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQ 265
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1049-1250 1.53e-19

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 93.74  E-value: 1.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGKVLLDGKEIKRLNVQWL-RAHLGIVSQEPILF-D 1124
Cdd:TIGR02633   13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1125 CSIAENIAYGD----NSRVVSQEEIVRAAKEANIHAFIESLPNkySTKVGDKGtqlsGGQKQRIAIARALVRQPHILLLD 1200
Cdd:TIGR02633   93 LSVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 42741659   1201 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:TIGR02633  167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
400-596 1.65e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.67  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   400 SYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirTINVRFLREIIGVVSQEPVl 479
Cdd:NF040873    1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   480 fatTIAENIRYGR-------ENVTMDEiEKAVKEAnaydfIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 552
Cdd:NF040873   73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 42741659   553 LLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTVRNAD 596
Cdd:NF040873  142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1049-1264 2.19e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 91.05  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQepilFD---- 1124
Cdd:PRK13536   53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDnldl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 -CSIAEN-IAYGDNSRVVSQEeivraaKEANIHAFIE--SLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:PRK13536  128 eFTVRENlLVFGRYFGMSTRE------IEAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILD 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1201 EATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1264
Cdd:PRK13536  198 EPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
392-610 2.30e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 93.77  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSR--------KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN- 462
Cdd:PRK10261  314 LQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   463 --VRFLREIIGVVSQEPvlFAT---------TIAENIRY--------GRENVTMDEIEKAVKEANAYDFimklPHKFdtl 523
Cdd:PRK10261  394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   524 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARK-GRTTIVIAHRLSTV-RNADVIAG 600
Cdd:PRK10261  465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
                         250
                  ....*....|
gi 42741659   601 FDDGVIVEKG 610
Cdd:PRK10261  537 MYLGQIVEIG 546
cbiO PRK13645
energy-coupling factor transporter ATPase;
390-625 2.62e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 90.07  E-value: 2.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   390 GNLEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-----RTIN 462
Cdd:PRK13645    5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   463 VRFLREIIGVVSQEP--VLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHKFdtlVGERGAQLSGGQKQRIA 540
Cdd:PRK13645   85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   541 IARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMK 617
Cdd:PRK13645  161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240

                  ....*...
gi 42741659   618 EKGIYFKL 625
Cdd:PRK13645  241 NQELLTKI 248
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1051-1201 2.92e-19

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 88.55  E-value: 2.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPLAGKVLLDGKEIKRLNVqWLRAHLGI--VSQEPIL 1122
Cdd:COG1137   17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1123 F-DCSIAENI-AygdnsrVVSQEEIVRAAKEANIHAFIE--SLpnkysTKVGD-KGTQLSGGQKQRIAIARALVRQPHIL 1197
Cdd:COG1137   90 FrKLTVEDNIlA------VLELRKLSKKEREERLEELLEefGI-----THLRKsKAYSLSGGERRRVEIARALATNPKFI 158

                 ....
gi 42741659 1198 LLDE 1201
Cdd:COG1137  159 LLDE 162
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1050-1253 3.03e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 88.30  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1050 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQW---LRA-HLGIVSQEPILFDC 1125
Cdd:PRK10584   23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIA-ENIAY-----GDNSRvVSQEEIVRAAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1199
Cdd:PRK10584  103 LNAlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1200 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1253
Cdd:PRK10584  171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
392-562 3.60e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 88.58  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTInvrflREIIG 471
Cdd:PRK11247   13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEANAYDfimklphkfdtLVGERGAQLSGGQKQRIAIARALVRNPK 550
Cdd:PRK11247   85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPG 153
                         170
                  ....*....|..
gi 42741659   551 ILLLDEATSALD 562
Cdd:PRK11247  154 LLLLDEPLGALD 165
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
406-587 4.65e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 87.53  E-value: 4.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR---FLR-EIIGVVSQEPVLFA 481
Cdd:PRK10584   22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAenirygRENVTMDEIEKAVKEANAYDFIMKLPHKFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEA 557
Cdd:PRK10584  102 TLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
                         170       180       190
                  ....*....|....*....|....*....|..
gi 42741659   558 TSALDTES-EAVVQVALDKARKGRTT-IVIAH 587
Cdd:PRK10584  174 TGNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
384-585 4.71e-19

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 87.77  E-value: 4.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  384 KPDNIKGNLEfrnvHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV 463
Cdd:cd03267   15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  464 RFLREiIGVV--SQEPVLFATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRI 539
Cdd:cd03267   91 KFLRR-IGVVfgQKTQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 42741659  540 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVI 585
Cdd:cd03267  163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL 208
cbiO PRK13646
energy-coupling factor transporter ATPase;
1035-1264 4.88e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 89.07  E-value: 4.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1035 VTFGEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQW 1108
Cdd:PRK13646    3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1109 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIvraaKEaniHAFIESLPNKYSTKVGDKGT-QLSGGQKQRIA 1185
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEV----KN---YAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1186 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK13646  156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235

                  ..
gi 42741659  1263 QK 1264
Cdd:PRK13646  236 DK 237
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
392-619 5.03e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 89.89  E-value: 5.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 471
Cdd:PRK13536   42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVL-FATTIAEN-IRYGRE-NVTMDEIEKAVkeANAYDFiMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 548
Cdd:PRK13536  118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659   549 PKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:PRK13536  191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
406-618 5.53e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 89.37  E-value: 5.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEG---------------------MVSVDGQDIRTINVR 464
Cdd:PRK13651   19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekekvLEKLVIQKTRFKKIK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 FLREI---IGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHKFDtlvgERGA-QLSGGQKQR 538
Cdd:PRK13651   99 KIKEIrrrVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   539 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTV--RNADVIAgFDDGVIVEKGNHDEL 615
Cdd:PRK13651  174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDI 252

                  ...
gi 42741659   616 MKE 618
Cdd:PRK13651  253 LSD 255
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1052-1256 5.83e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 87.56  E-value: 5.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQW---LRAH-LGIVSQ-EPILFDCS 1126
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1127 IAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESlpnkystKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:PRK11629  104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-------RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42741659  1207 DTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:PRK11629  177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
392-614 8.51e-19

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 91.66  E-value: 8.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdGQdirtiNVRflreiIG 471
Cdd:COG0488  316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVSQEPVLFAT--TIAENIRYGRENVTmdeiekavkEANAYDFIMKL---PHKFDTLVGErgaqLSGGQKQRIAIARALV 546
Cdd:COG0488  382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  547 RNPKILLLDEATSALDTESEAVVQVALDkARKGrTTIVIAH-R--LSTVrnADVIAGFDDGVIVEK-GNHDE 614
Cdd:COG0488  449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDD 516
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
392-587 9.60e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 88.71  E-value: 9.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 471
Cdd:PRK13537    8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQ----EPVLfatTIAENIR-YGRE-NVTMDEIEKAVkeANAYDFiMKLPHKFDTLVGErgaqLSGGQKQRIAIARAL 545
Cdd:PRK13537   84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 42741659   546 VRNPKILLLDEATSALDTESEAVVQVALDK--ARkGRTTIVIAH 587
Cdd:PRK13537  154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTH 196
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1042-1263 1.09e-18

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 87.59  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1042 FNYPT----RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVS 1117
Cdd:COG4167   14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1118 QEPilfdcsiaeNIAYGDNSRVVSQ-EEIVR-------AAKEANIHAFIEslpnkystKVG-------DKGTQLSGGQKQ 1182
Cdd:COG4167   94 QDP---------NTSLNPRLNIGQIlEEPLRlntdltaEEREERIFATLR--------LVGllpehanFYPHMLSSGQKQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1183 RIAIARALVRQPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1254
Cdd:COG4167  157 RVALARALILQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231

                 ....*....
gi 42741659 1255 GTHQQLLAQ 1263
Cdd:COG4167  232 GKTAEVFAN 240
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
413-610 1.39e-18

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 92.38  E-value: 1.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    413 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIGVVSQEPVLFA-TTIAENIRYg 491
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    492 RENVTMDEIEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQV 571
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 42741659    572 ALDKARKGRTTIVIAHRLStvrNADVIAgfDDGVIVEKG 610
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
392-556 1.41e-18

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 86.62  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRT--INVRfLREI 469
Cdd:COG1137    4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKR-ARLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  470 IGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAvkeanaydfimklpHKFDTLVGE---------RGAQLSGGQKQRI 539
Cdd:COG1137   80 IGYLPQEASIFRKlTVEDNILAVLELRKLSKKERE--------------ERLEELLEEfgithlrksKAYSLSGGERRRV 145
                        170
                 ....*....|....*..
gi 42741659  540 AIARALVRNPKILLLDE 556
Cdd:COG1137  146 EIARALATNPKFILLDE 162
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
392-587 1.42e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 87.06  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFlreiiG 471
Cdd:PRK11248    2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQ-EPVLFATTIAENIRYGREnvtMDEIEKAVKEANAYDFIMKlphkfdtlVGERGA------QLSGGQKQRIAIARA 544
Cdd:PRK11248   74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 42741659   545 LVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 587
Cdd:PRK11248  143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1052-1262 1.43e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 87.94  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQ----EPilfDCSI 1127
Cdd:PRK13537   22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1128 AENIaygdnsRVVSQEEIVRAAK-EANIHAFIE--SLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PRK13537   98 RENL------LVFGRYFGLSAAAaRALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1205 ALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK13537  168 GLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
85-330 1.54e-18

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 87.60  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   85 LEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSGigAGVLVAAYIqvSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFD 164
Cdd:cd18574   19 LGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLL--QSLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  165 VHDVGELNTRLTDDVSK--------INEGIgdkigmffQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKIL 236
Cdd:cd18574   95 THRTGELVNRLTADVQEfkssfkqcVSQGL--------RSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  237 SSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR--------IGIKKAITaNISIGAAFLLIYa 308
Cdd:cd18574  167 RKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL- 244
                        250       260
                 ....*....|....*....|..
gi 42741659  309 syalafWYGTTLVLSGEYSIGQ 330
Cdd:cd18574  245 ------YYGGSLVSRGELTAGD 260
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
392-618 1.78e-18

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 90.63  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    392 LEFRNVHFSYPS--RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS-------VDGQDIRTIN 462
Cdd:TIGR03269  280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    463 VRFLREIIGVVSQEPVLFA-TTIAENIRygrENVTM---DEI--EKAV--------KEANAYDFIMKLPHkfdtlvgerg 528
Cdd:TIGR03269  360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPD---------- 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    529 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGV 605
Cdd:TIGR03269  427 -ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
                          250
                   ....*....|...
gi 42741659    606 IVEKGNHDELMKE 618
Cdd:TIGR03269  506 IVKIGDPEEIVEE 518
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
399-621 1.99e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 86.98  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   399 FSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ--DIRTINVRFLREIIGVVSQE 476
Cdd:PRK13638    9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   477 P--VLFATTIAENIRYGREN--VTMDEIEKAVKEANaydfimklphkfdTLVGERGAQ------LSGGQKQRIAIARALV 546
Cdd:PRK13638   86 PeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   547 RNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTV----------RNADVIAGFDDGVIVEKGnhdEL 615
Cdd:PRK13638  153 LQARYLLLDEPTAGLDPAGRTqMIAIIRRIVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EA 229

                  ....*.
gi 42741659   616 MKEKGI 621
Cdd:PRK13638  230 MEQAGL 235
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
395-617 2.09e-18

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 86.77  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   395 RNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR-FLREIIGVV 473
Cdd:PRK10575   15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   474 SQEPVLFATTIAENI------------RYGRENvtmdeiEKAVKEANAYDFIMKLPHKfdtLVGergaQLSGGQKQRIAI 541
Cdd:PRK10575   92 QQLPAAEGMTVRELVaigrypwhgalgRFGAAD------REKVEEAISLVGLKPLAHR---LVD----SLSGGERQRAWI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   542 ARALVRNPKILLLDEATSALD----TESEAVVQvALDKARkGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 616
Cdd:PRK10575  159 AMLVAQDSRCLLLDEPTSALDiahqVDVLALVH-RLSQER-GLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236

                  .
gi 42741659   617 K 617
Cdd:PRK10575  237 R 237
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1051-1251 2.69e-18

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 89.69  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV-QWLRAHLGIVS----QEPILFDC 1125
Cdd:COG1129  266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 SIAENI---AYGDNSR--VVSQEEIVRAAKEanihaFIESLpnkySTKVGDKGT---QLSGGQKQRIAIARALVRQPHIL 1197
Cdd:COG1129  346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659 1198 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1251
Cdd:COG1129  417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
392-621 2.75e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 89.72  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 470
Cdd:PRK15439   12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQEPVLFAT-TIAENIRYG--RENVTMDEIEKAVKEANAYdfiMKLPHKFDTL-VGERgaqlsggqkQRIAIARALV 546
Cdd:PRK15439   89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   547 RNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGI 621
Cdd:PRK15439  157 RDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDII 233
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
757-1253 3.23e-18

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 89.86  E-value: 3.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  757 LLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIgSRLAVI 836
Cdd:COG4615   52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAF-VRLPEL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  837 TQNIANlgtgIIISFIY-GWQLTLLLLAIVPIIAIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSLTQEQK 915
Cdd:COG4615  129 LQSVAL----VLGCLAYlAWLSPPLFLLTLVLLGLGVAGYRLLVR----RARRHLRRAREAEDRLFKHFRALLEGFKELK 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  916 F-----EHMYAQSLQVP---YRNSLRKAH-IFGITFSFTQAMMYFSYAGCFrfgaYLVAHKLMSFEDVLLVFSAVV-FGA 985
Cdd:COG4615  201 LnrrrrRAFFDEDLQPTaerYRDLRIRADtIFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVLVLlFLR 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  986 MAVGQVSSFAPDYAKAKISAAHIimiiEKTPL-IDSYSTEGLMPNTLEGNVTFGE-----VVFNYPTRPDIP--VLQGLS 1057
Cdd:COG4615  277 GPLSQLVGALPTLSRANVALRKI----EELELaLAAAEPAAADAAAPPAPADFQTlelrgVTYRYPGEDGDEgfTLGPID 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1058 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDcsiaeniaygdns 1137
Cdd:COG4615  353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------------- 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1138 RVVSQEEIVRAAKeanIHAFIESLpnKYSTKVGDKG-----TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEK 1212
Cdd:COG4615  420 RLLGLDGEADPAR---ARELLERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR 494
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 42741659 1213 VVQEAL--DKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1253
Cdd:COG4615  495 VFYTELlpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
409-590 3.38e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 85.25  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI----IGVVSQEPVLFATTI 484
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   485 AenirygRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:PRK11629  104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
                         170       180       190
                  ....*....|....*....|....*....|
gi 42741659   563 TE-SEAVVQVALD-KARKGRTTIVIAHRLS 590
Cdd:PRK11629  178 ARnADSIFQLLGElNRLQGTAFLVVTHDLQ 207
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
1052-1218 4.06e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 84.08  E-value: 4.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENI 1131
Cdd:cd03231   15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1132 AY--GDNSRvvsqEEIVRAAKEANIHAFiESLPnkystkvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1209
Cdd:cd03231   95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159

                 ....*....
gi 42741659 1210 SEKVVQEAL 1218
Cdd:cd03231  160 GVARFAEAM 168
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
1052-1251 4.09e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 85.50  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----LAGKVLL-DGKEIKRLNVQWLRahlgivsqepILFDC 1125
Cdd:PRK11247   27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR----------LLPWK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYG--DNSRVVSQE--EIVRAAKEANihafieslpnkystkvgDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PRK11247   97 KVIDNVGLGlkGQWRDAALQalAAVGLADRAN-----------------EWPAALSGGQKQRVALARALIHRPGLLLLDE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1202 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1251
Cdd:PRK11247  160 PLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
711-994 4.18e-18

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 86.30  E-value: 4.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGI--ISFITFFLQGFTFGKAGEILTKRL 788
Cdd:cd18547    1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  789 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPII 868
Cdd:cd18547   81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  869 AIAgvveMKMLSGQALKD-KKELEGSGKI---ATEAIENFRTVVSLTQE----QKFEHMYAQslqvpYRNSLRKAHIF-G 939
Cdd:cd18547  159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  940 ITFSFTQAMMYFSYAGCFRFGAYLvahklmsfedvllvfsaVVFGAMAVGQVSSF 994
Cdd:cd18547  230 LLMPIMNFINNLGYVLVAVVGGLL-----------------VINGALTVGVIQAF 267
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1034-1263 4.27e-18

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 86.32  E-value: 4.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1034 NVT--FGEVVfnyptrpdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlRA 1111
Cdd:COG4152    6 GLTkrFGDKT----------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1112 HLGIVSQEPILF-DCSIAENIAY-----GdnsrvVSQEEIVRAAKEanihaFIE--SLPNKYSTKVGDkgtqLSGGQKQR 1183
Cdd:COG4152   72 RIGYLPEERGLYpKMKVGEQLVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1184 IAIARALVRQPHILLLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:COG4152  138 VQLIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIR 217

                 ..
gi 42741659 1262 AQ 1263
Cdd:COG4152  218 RQ 219
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
1055-1260 4.36e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 87.07  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1055 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-VQWL--RAHLGIVSQEPILF---DCSIA 1128
Cdd:PRK15079   39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENIAygDNSRV----VSQEEIVRAAKEANIH-AFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:PRK15079  119 EIIA--EPLRTyhpkLSRQEVKDRVKAMMLKvGLLPNLINRYPH-------EFSGGQCQRIGIARALILEPKLIICDEPV 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1204 SALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK15079  190 SALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
404-586 4.47e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 84.16  E-value: 4.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   404 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGvvSQEPVLFATT 483
Cdd:PRK13539   12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   484 IAENIRYGRE--NVTMDEIEKAVKeanaydfIMKLPHKFDTlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 561
Cdd:PRK13539   90 VAENLEFWAAflGGEELDIAAALE-------AVGLAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
                         170       180
                  ....*....|....*....|....*
gi 42741659   562 DTESEAVVQvALDKARKGRTTIVIA 586
Cdd:PRK13539  159 DAAAVALFA-ELIRAHLAQGGIVIA 182
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1049-1251 4.59e-18

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 89.78  E-value: 4.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHLGIVSQE-PILF 1123
Cdd:PRK10535   20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIaygDNSRVVSQEEivRAAKEANIHAFIESLpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:PRK10535  100 HLTAAQNV---EVPAVYAGLE--RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 42741659  1204 SALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1251
Cdd:PRK10535  173 GALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1044-1232 4.78e-18

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 88.97  E-value: 4.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1044 YPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlnvqwlRAHLGIVSQEPILF 1123
Cdd:COG0488    8 FGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 D-CSIAENIAYGDNSRVVSQEEIVRA-----------AKEANIHAFIESL-------------------PNKYSTKVGDk 1172
Cdd:COG0488   74 DdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVSE- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659 1173 gtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1232
Cdd:COG0488  153 ---LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
1049-1255 5.51e-18

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 83.73  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPILFD 1124
Cdd:cd03217   12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1125 csiaeniayGdnsrvVSQEEIVRAAKEAnihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:cd03217   91 ---------G-----VKNADFLRYVNEG-----------------------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1205 ALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHG 1255
Cdd:cd03217  134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
1042-1255 5.67e-18

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 84.12  E-value: 5.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1042 FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnVQW-LRAHLGIVSQ-- 1118
Cdd:cd03220   27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1119 --EPILFDCSIaeniaYGdnsrvVSQEEIvrAAKEANIHAFIEsLPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHI 1196
Cdd:cd03220  101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1197 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1255
Cdd:cd03220  164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1051-1256 6.26e-18

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 90.46  E-value: 6.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFD-CSIAE 1129
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1130 NIAYGDNSRVVSQEEivraaKEANIHAFIESlpNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1209
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-----AQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 42741659   1210 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVFQNGRVKEHGT 1256
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1052-1261 9.85e-18

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 84.65  E-value: 9.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FDCSIAEN 1130
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1131 IAYGdnsRVVSQEEIVRAAKEaNIHAFIESLPNKYSTKVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1209
Cdd:PRK10253  102 VARG---RYPHQPLFTRWRKE-DEEAVTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1210 SEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:PRK10253  178 HQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
754-992 1.08e-17

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 85.23  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  754 LFSLLFLALGIISFITFFLqgftFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 833
Cdd:cd18575   41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  834 AVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlKDKkeLEGSGKIATEAIENFRTVVSL 910
Cdd:cd18575  115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  911 TQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVL-LVFSAvVFGAMAVG 989
Cdd:cd18575  192 TREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqFVFYA-VLAAGSVG 270

                 ...
gi 42741659  990 QVS 992
Cdd:cd18575  271 ALS 273
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1053-1260 1.16e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 84.29  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAG-KVLLDGKEIKRL-----NVQWLRAHLGIVSQEPILFD 1124
Cdd:PRK09984   20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGsHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 -CSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLpnkysTKVG------DKGTQLSGGQKQRIAIARALVRQPHIL 1197
Cdd:PRK09984  100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1198 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK09984  175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
1046-1231 1.38e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 82.61  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ-EPILfd 1124
Cdd:PRK13539   11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 cSIAENIAYGDNSRVVSQEEIVRAAKEANIHAfIESLPNKYstkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PRK13539   89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
                         170       180
                  ....*....|....*....|....*..
gi 42741659  1205 ALDTESEKVVQEALdKAREGRTCIVIA 1231
Cdd:PRK13539  157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1052-1256 1.40e-17

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 83.59  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnVQWLrahLGI-VSQEPILfdcSIAEN 1130
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 I-----AYGdnsrvVSQEEIvrAAKEANIHAFIE-----SLPNK-YSTkvgdkgtqlsgGQKQRIAIARALVRQPHILLL 1199
Cdd:COG1134  109 IylngrLLG-----LSRKEI--DEKFDEIVEFAElgdfiDQPVKtYSS-----------GMRARLAFAVATAVDPDILLV 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659 1200 DEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1256
Cdd:COG1134  171 DEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
1046-1233 1.98e-17

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 81.05  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGkvlldGKeIKRLnvqwLRAHLGIVSQEPILFDC 1125
Cdd:cd03223   10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGS-----GR-IGMP----EGEDLLFLPQRPYLPLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1126 SIAENIAYgdnsrvvsqeeivraakeanihafieslPnkystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:cd03223   79 TLREQLIY----------------------------P---------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
                        170       180
                 ....*....|....*....|....*...
gi 42741659 1206 LDTESEKVVQEALDKarEGRTCIVIAHR 1233
Cdd:cd03223  122 LDEESEDRLYQLLKE--LGITVISVGHR 147
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1050-1263 2.62e-17

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 86.78  E-value: 2.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1050 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdgkeikRLNVQWL-----------RA--HLGIV 1116
Cdd:TIGR03269  297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV------RVGDEWVdmtkpgpdgrgRAkrYIGIL 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1117 SQEPILF-DCSIAENIaygdnSRVVSQEEIVRAAKEANIHAF-IESLPNKYSTKVGDKGT-QLSGGQKQRIAIARALVRQ 1193
Cdd:TIGR03269  371 HQEYDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKE 445
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659   1194 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:TIGR03269  446 PRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
711-970 3.11e-17

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 83.61  E-value: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQpafaIIFSKIIGVFT-RIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLR 789
Cdd:cd18541    1 YLLGILFLILVDLLQ----LLIPRIIGRAIdALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  790 YMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIA 869
Cdd:cd18541   77 NDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  870 IAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQ 946
Cdd:cd18541  155 LLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
                        250       260
                 ....*....|....*....|....
gi 42741659  947 AMMYFSYAGCFRFGAYLVAHKLMS 970
Cdd:cd18541  232 LLIGLSFLIVLWYGGRLVIRGTIT 255
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
374-611 3.21e-17

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 87.02  E-value: 3.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    374 SIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPTE--G 449
Cdd:TIGR00955    4 SWRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVKgsG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    450 MVSVDGqdiRTINVRFLREIIGVVSQEPVLFAT-TIAENI------RYGReNVTMDEIEKAVKEanaydFI--MKLPHKF 520
Cdd:TIGR00955   84 SVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    521 DTLVGERGAQ--LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLStvrnADV 597
Cdd:TIGR00955  155 NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPS----SEL 230
                          250
                   ....*....|....
gi 42741659    598 IAGFDDGVIVEKGN 611
Cdd:TIGR00955  231 FELFDKIILMAEGR 244
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1051-1256 3.32e-17

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 82.82  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILfdcsiaen 1130
Cdd:COG4604   15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI-------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 iaygdNSRVVSQE-------------------EIVRAAkeanIHAF-IESLPNKYSTkvgdkgtQLSGGQKQRIAIARAL 1190
Cdd:COG4604   87 -----NSRLTVRElvafgrfpyskgrltaedrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1191 VRQPHILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVFQNGRVKEHGT 1256
Cdd:COG4604  151 AQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
cbiO PRK13645
energy-coupling factor transporter ATPase;
1033-1263 3.45e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 83.52  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1033 GNVTFGEVVFNYPTRP--DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI-----KRLN 1105
Cdd:PRK13645    5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1106 VQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEAnihAFIESLPNKYSTKvgdKGTQLSGGQKQR 1183
Cdd:PRK13645   85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQKRR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1184 IAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG---- 1255
Cdd:PRK13645  159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfe 237
                         250
                  ....*....|
gi 42741659  1256 --THQQLLAQ 1263
Cdd:PRK13645  238 ifSNQELLTK 247
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
147-337 3.70e-17

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 83.71  E-value: 3.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  147 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLG 226
Cdd:cd18563   78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  227 -LSAAVWAKILSSFTdKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 305
Cdd:cd18563  158 wGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
                        170       180       190
                 ....*....|....*....|....*....|..
gi 42741659  306 IYASYALAFWYGTTLVLSGEYSIGqVLTVFFS 337
Cdd:cd18563  237 TSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
405-639 4.40e-17

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 86.01  E-value: 4.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    405 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRL--YDPTEGMV----------------SVDGQDI-------- 458
Cdd:TIGR03269   11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEPCpvcggtle 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    459 ----------RTINVRFLREIigvvsqePVLFATTIAeniRYGRENV------TMDEIEKAVKEA--NAYDFI--MKLPH 518
Cdd:TIGR03269   91 peevdfwnlsDKLRRRIRKRI-------AIMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    519 KFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-A 595
Cdd:TIGR03269  161 RITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlS 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 42741659    596 DVIAGFDDGVIVEKGNHDELMKekgIYFKLVTMQTAGNEVELEN 639
Cdd:TIGR03269  237 DKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGE 277
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
410-592 5.31e-17

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 81.46  E-value: 5.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI---RTINVRFLREIIGVVSQE---------- 476
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhhllmdrtvy 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   477 -----PVLFATTIAENIRYgRENVTMDEIEKAVKEANaydfimkLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 551
Cdd:PRK10908   98 dnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSGGEQQRVGIARAVVNKPAV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 42741659   552 LLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTV 592
Cdd:PRK10908  159 LLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1053-1260 6.00e-17

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 81.26  E-value: 6.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFDCSIA-ENI 1131
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1132 A-----YGdnsrvVSQEEivRAAKEANIHAFIEslpnkystkVGDKGTQL----SGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:cd03265   95 YiharlYG-----VPGAE--RRERIDELLDFVG---------LLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659 1203 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQL 1260
Cdd:cd03265  159 TIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
747-970 6.26e-17

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 82.74  E-value: 6.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  747 TKRQNSNLFSLLFLALGIISFITFFLQG-----FTFGKAGeiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLAND 821
Cdd:cd18784   27 VIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  822 AAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAI 901
Cdd:cd18784  103 TTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETI 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  902 ENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGiTFSFTQAMMYFS-YAGCFRFGAYLVAHKLMS 970
Cdd:cd18784  183 SSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQIS 251
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
392-618 6.61e-17

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 81.67  E-value: 6.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYP-------------------SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS 452
Cdd:COG1134    5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  453 VDGqdirtiNVRFLREIIGVVSQEpvlfaTTIAENIR-----YGrenVTMDEIEKAVKEANAY----DFImklphkfDTL 523
Cdd:COG1134   85 VNG------RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  524 VGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAVVQvalDKARKGRTTIVIAHRLSTVRN-ADVI 598
Cdd:COG1134  144 VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRA 216
                        250       260
                 ....*....|....*....|
gi 42741659  599 AGFDDGVIVEKGNHDELMKE 618
Cdd:COG1134  217 IWLEKGRLVMDGDPEEVIAA 236
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
379-610 7.13e-17

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 81.04  E-value: 7.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  379 SKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQD- 457
Cdd:cd03220    7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVs 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  458 -IRTINVRFLREIIGVvsqepvlfattiaENIR-YGRE-NVTMDEIEKavKEANAYDFiMKLPHKFDTLVGErgaqLSGG 534
Cdd:cd03220   87 sLLGLGGGFNPELTGR-------------ENIYlNGRLlGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSG 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  535 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:cd03220  147 MKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
392-587 7.16e-17

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 78.64  E-value: 7.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdGQDIRtinvrflreiIG 471
Cdd:cd03221    1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  472 VVsqepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 551
Cdd:cd03221   67 YF-------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42741659  552 LLLDEATSALDTESEAVVQVALdKARKGrTTIVIAH 587
Cdd:cd03221   92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1055-1260 8.65e-17

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 81.57  E-value: 8.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1055 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLrAHLGIVS--QEPILF-DCSIAENI 1131
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1132 AYGD----NSRVVS------------QEEIVRAA---------KEANIHAfieslpnkystkvgdkGTqLSGGQKQRIAI 1186
Cdd:PRK11300  102 LVAQhqqlKTGLFSgllktpafrraeSEALDRAAtwlervgllEHANRQA----------------GN-LAYGQQRRLEI 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK11300  165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1050-1251 1.08e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 84.72  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1050 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqwLRAH-LGI--VSQEPILF-DC 1125
Cdd:PRK15439   24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP--AKAHqLGIylVPQEPLLFpNL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNkySTKVGDkgtqlsggqKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:PRK15439  102 SVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG--SLEVAD---------RQIVEILRGLMRDSRILILDEPTAS 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1206 LD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1251
Cdd:PRK15439  171 LTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1047-1231 1.25e-16

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 79.71  E-value: 1.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1047 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCS 1126
Cdd:TIGR01189   10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1127 IAENIAY-----GDNSRVVSQeeivrAAKEANIHAFiESLPnkystkvgdkGTQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:TIGR01189   90 ALENLHFwaaihGGAQRTIED-----ALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDE 153
                          170       180       190
                   ....*....|....*....|....*....|
gi 42741659   1202 ATSALDTESEKVVQEALDkAREGRTCIVIA 1231
Cdd:TIGR01189  154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
GguA NF040905
sugar ABC transporter ATP-binding protein;
392-608 1.30e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.46  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQ-----DIRTi 461
Cdd:NF040905    2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   462 nvrflREIIGVV--SQE----PVLfatTIAENIRYGRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAqlsg 533
Cdd:NF040905   75 -----SEALGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV---- 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   534 GQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVE 608
Cdd:NF040905  143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
88-337 1.31e-16

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 82.07  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   88 LMSNITNR-SDINDTGFFMNLEEdMTRYAYYYSGIGAGVLVAAYIQvSFWCLAAGRQI-HKIRKQFFHAIMRQEIGWFDV 165
Cdd:cd18547   21 LLGKAIDLiIEGLGGGGGVDFSG-LLRILLLLLGLYLLSALFSYLQ-NRLMARVSQRTvYDLRKDLFEKLQRLPLSYFDT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  166 HDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELL 245
Cdd:cd18547   99 HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  246 AYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGE 325
Cdd:cd18547  179 ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGA 258
                        250
                 ....*....|..
gi 42741659  326 YSIGqVLTVFFS 337
Cdd:cd18547  259 LTVG-VIQAFLQ 269
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
392-616 1.40e-16

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 81.37  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVH--FSYPS----RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG---------- 455
Cdd:PRK15112    5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysy 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   456 --QDIRTI-----NVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYdfimklPHkfdtlvgerg 528
Cdd:PRK15112   85 rsQRIRMIfqdpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYY------PH---------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   529 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGV 605
Cdd:PRK15112  149 -MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGE 227
                         250
                  ....*....|.
gi 42741659   606 IVEKGNHDELM 616
Cdd:PRK15112  228 VVERGSTADVL 238
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
409-616 2.07e-16

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 80.80  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFA-TTIAEN 487
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   488 IRYGRE------NVTMDEIEKAVKEANAYDFIMKLP-HKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK10253  102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659   561 LDTESEA-VVQVALDKAR-KGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 616
Cdd:PRK10253  174 LDISHQIdLLELLSELNReKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
73-333 2.29e-16

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 80.98  E-value: 2.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   73 GEMTDIFANAGNLEDLMSNITnrsdindtgfFMNLeedmtryayyysgIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFF 152
Cdd:cd18589   20 GRMTDWIMNKDAPEAFTAAIT----------VMSL-------------LTIASAVSEFVCDLIYNITMSRIHSRLQGLVF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  153 HAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVW 232
Cdd:cd18589   77 AAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  233 AKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYAL 312
Cdd:cd18589  157 GKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVG 236
                        250       260
                 ....*....|....*....|.
gi 42741659  313 AFWYGTTLVLSGEYSIGQVLT 333
Cdd:cd18589  237 ILYYGGQLVTAGTVSSGDLVT 257
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1047-1260 3.23e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 83.75  E-value: 3.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1047 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLR--------------AH 1112
Cdd:PRK10261   26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1113 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSQEEIVRAAKEANIHAFI---ESLPNKYStkvgdkgTQLSGGQKQ 1182
Cdd:PRK10261  106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKRMLDQVRIpeaQTILSRYP-------HQLSGGMRQ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1183 RIAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1254
Cdd:PRK10261  176 RVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVET 250

                  ....*.
gi 42741659  1255 GTHQQL 1260
Cdd:PRK10261  251 GSVEQI 256
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1046-1260 3.37e-16

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 80.19  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL---RAHLGIVSQEPIL 1122
Cdd:PRK11831   16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1123 F-DCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAfieslpnkystkVGDKG------TQLSGGQKQRIAIARALVRQPH 1195
Cdd:PRK11831   96 FtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRAALARAIALEPD 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1196 ILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK11831  164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
1051-1250 3.53e-16

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 76.72  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKvlldgkeikrlnvqwLRAHLGIVSQEPILfdcsiaeN 1130
Cdd:cd03221   14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGE---------------LEPDEGIVTWGSTV-------K 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1131 IAYgdnsrvvsqeeivraakeanihafiesLPnkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:cd03221   65 IGY---------------------------FE------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 42741659 1211 EKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:cd03221  106 IEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
403-567 4.66e-16

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 78.30  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  403 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFAT 482
Cdd:cd03231    9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  483 TIAENIRYGRENVTMDEIEKAVKEANAYDFimklphkFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:cd03231   89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                 ....*
gi 42741659  563 TESEA 567
Cdd:cd03231  158 KAGVA 162
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
407-604 7.82e-16

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 82.18  E-value: 7.82e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    407 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTEGMVSVDGQDIRTINVRFL-REIIGVVSQEPVLFAT- 482
Cdd:TIGR02633   14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPEl 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    483 TIAENIRYGRE----NVTMDEIEkAVKEANAYDFIMKLPHKFDTL-VGERGaqlsGGQKQRIAIARALVRNPKILLLDEA 557
Cdd:TIGR02633   94 SVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 42741659    558 TSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 604
Cdd:TIGR02633  169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
115-556 8.82e-16

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 82.15  E-value: 8.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  115 AYYYSGIGAGVLVAAYIQvsfwclaagRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF 194
Cdd:COG4615   60 LLLLSRLASQLLLTRLGQ---------HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDV--------RTISQAF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  195 QSMATFFTGFIVGFtrgwkLTLVILA-ISPVLGLSAAVWAkILSSFTDKELLAYAKAG----AVAEEVL-AAIRTVIafG 268
Cdd:COG4615  123 VRLPELLQSVALVL-----GCLAYLAwLSPPLFLLTLVLL-GLGVAGYRLLVRRARRHlrraREAEDRLfKHFRALL--E 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  269 GQKkEL----ER----YNKNLE---EAKRIGIKKAITANISIGA-AFLLIYASYALAFWYGTTLV-LSGEYSIGQVLTVF 335
Cdd:COG4615  195 GFK-ELklnrRRrrafFDEDLQptaERYRDLRIRADTIFALANNwGNLLFFALIGLILFLLPALGwADPAVLSGFVLVLL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  336 FsvLIGAfsVGQASPSIEAFANARgAAYEifKIIDNKPSIDSYSKSGHKPDNIKGN-----LEFRNVHFSYPSRKEVK-- 408
Cdd:COG4615  274 F--LRGP--LSQLVGALPTLSRAN-VALR--KIEELELALAAAEPAAADAAAPPAPadfqtLELRGVTYRYPGEDGDEgf 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTiaeni 488
Cdd:COG4615  347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL----- 421
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  489 rYGRENVTMDEiekavkEANAYDFIMKLPHK-------FDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 556
Cdd:COG4615  422 -LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1050-1266 9.99e-16

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 78.00  E-value: 9.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1050 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIkrlnVQW-----LRAHLGIVSQEPILFD 1124
Cdd:PRK11614   18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiMREAVAIVPEGRRVFS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 -CSIAENIAYGD--NSRVVSQEEIVRAakeanihafIESLPNKYSTKVGDKGTqLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PRK11614   94 rMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDE 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1202 ATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1266
Cdd:PRK11614  164 PSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
1021-1263 1.05e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 81.94  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1021 YSTEGLMPNTLEG--NVTFGEVVFNYPTR-----PdipvlqgLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGK 1093
Cdd:PRK10522  307 YKAEFPRPQAFPDwqTLELRNVTFAYQDNgfsvgP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1094 VLLDGKEIKRLNVQWLRAHLGIVSQEPILFDcsiaeniaygdnsRVVSQEEivRAAKEANIHAFIESLPNKYSTKVGD-- 1171
Cdd:PRK10522  380 ILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgr 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1172 -KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQN 1248
Cdd:PRK10522  445 iSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRN 524
                         250
                  ....*....|....*.
gi 42741659  1249 GRVKE-HGTHQQLLAQ 1263
Cdd:PRK10522  525 GQLSElTGEERDAASR 540
GguA NF040905
sugar ABC transporter ATP-binding protein;
1046-1253 1.10e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.76  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGKVLLDGKEIKRLNvqwLRA--HLGIV--SQ 1118
Cdd:NF040905   10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1119 E----PILfdcSIAENIAYGdNSR----VVSQEEIVRAAKEANIHAFIESLPNkysTKVGDKGTqlsgGQKQRIAIARAL 1190
Cdd:NF040905   86 ElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKAL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1191 VRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKE 1253
Cdd:NF040905  155 SKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
407-610 1.20e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 81.37  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   407 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-IGVVSQE-PVLFATTI 484
Cdd:PRK09700   18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   485 AENIRYGRE------NVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 558
Cdd:PRK09700   98 LENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 42741659   559 SALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 610
Cdd:PRK09700  174 SSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
396-607 1.34e-15

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 79.77  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   396 NVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTV-QLMQRLYDP--TEGMVSVDGQDIRTINVRFLREI--- 469
Cdd:PRK09473   19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLLAANgrIGGSATFNGREILNLPEKELNKLrae 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 -IGVVSQEPVlfaTTIAENIRYG-------------------RENVTMDEiekAVKEANAYDFIMKLPHKFdtlvgerga 529
Cdd:PRK09473   98 qISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--------- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   530 qlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTT--IVIAHRLStvrnadVIAGFDDGVIV 607
Cdd:PRK09473  163 --SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLG------VVAGICDKVLV 234
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1049-1262 1.43e-15

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 81.39  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGKVLLD---GKEIKRLNVQwlrAHLG--------- 1114
Cdd:TIGR03269   12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalCEKCGYVERP---SKVGepcpvcggt 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1115 IVSQEPILFDCS------IAENIA---------YGDNSRVV----SQEEIVRAAKEANIHA--FIESLpnKYSTKVGDKG 1173
Cdd:TIGR03269   89 LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEAVGRAvdLIEMV--QLSHRITHIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1174 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1250
Cdd:TIGR03269  167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
                          250
                   ....*....|..
gi 42741659   1251 VKEHGTHQQLLA 1262
Cdd:TIGR03269  247 IKEEGTPDEVVA 258
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
393-772 1.61e-15

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 82.46  E-value: 1.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    393 EFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLydpTEGMVSvdgQDIRTINVRFLRE-- 468
Cdd:TIGR00956  761 HWRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVIT---GGDRLVNGRPLDSsf 834
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    469 --IIGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKavKEANAY-DFIMKL---PHKFDTLVGERGAQLSGGQKQRIAI 541
Cdd:TIGR00956  835 qrSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTI 912
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    542 ARALVRNPKILL-LDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLStvrnADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:TIGR00956  913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFDRLLLLQKGGQTVYFGDL 988
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    620 GI-------YFK---LVTMQTAGNEVE--LE--NAADESKSEIDALEMSSNDSRSSLIRKRSTRRSVRGSQAQDrkLSTK 685
Cdd:TIGR00956  989 GEnshtiinYFEkhgAPKCPEDANPAEwmLEviGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAED--DNDP 1066
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    686 EALDESIPP-------------VSFWRIMKLNlteWPYFVVGVFCAIING-----------GLQPAFAIIFSKIIGVFTR 741
Cdd:TIGR00956 1067 DALSKYAASlwyqfklvlwrtfQQYWRTPDYL---YSKFFLTIFAALFIGftffkvgtslqGLQNQMFAVFMATVLFNPL 1143
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 42741659    742 I-----------DDPETKRQNSNLFS-LLFLALGIISFITFFL 772
Cdd:TIGR00956 1144 IqqylppfvaqrDLYEVRERPSRTFSwLAFIAAQITVEIPYNL 1186
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1047-1261 1.92e-15

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 81.25  E-value: 1.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1047 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----LAGKVLLDGKeikRLNVQWLRAHLGIVSQEPIL 1122
Cdd:TIGR00955   35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1123 FDCSIA-ENIAYgdNSRVVSQEEIVRAAKEANIHAFIE--SLPNKYSTKVGDKGTQ--LSGGQKQRIAIARALVRQPHIL 1197
Cdd:TIGR00955  111 IPTLTVrEHLMF--QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   1198 LLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:TIGR00955  189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
392-615 2.05e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 80.90  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPT------EGMVSVDGQDIRTINVR 464
Cdd:PRK15134    6 LAIENLSVAFRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 FLREI----IGVVSQEPVLFAT---TIAENI-------RYGRENVTMDE---------IEKAVKEANAYdfimklPHkfd 521
Cdd:PRK15134   85 TLRGVrgnkIAMIFQEPMVSLNplhTLEKQLyevlslhRGMRREAARGEilncldrvgIRQAAKRLTDY------PH--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   522 tlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVI 598
Cdd:PRK15134  156 --------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRV 227
                         250
                  ....*....|....*..
gi 42741659   599 AGFDDGVIVEKGNHDEL 615
Cdd:PRK15134  228 AVMQNGRCVEQNRAATL 244
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
742-948 2.08e-15

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 78.15  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  742 IDDPETKRQNSNLFSLLFLaLGIISFITFFLQG-----FTFgkAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTT 816
Cdd:cd18590   23 IDILGGEYQHNAFTSAIGL-MCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  817 RLANDAAQVKGAIGSRLAVITQN-IANLGTgiiISFIYG--WQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKELEGS 893
Cdd:cd18590   98 RLSTDTTLMSRSVALNANVLLRSlVKTLGM---LGFMLSlsWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQDS 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  894 ----GKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAM 948
Cdd:cd18590  171 iakaGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
392-561 2.38e-15

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 76.84  E-value: 2.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-NVRFLREII 470
Cdd:PRK11614    6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPHKfdtlVGERGAQLSGGQKQRIAIARALVRNP 549
Cdd:PRK11614   83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
                         170
                  ....*....|..
gi 42741659   550 KILLLDEATSAL 561
Cdd:PRK11614  157 RLLLLDEPSLGL 168
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1048-1249 3.74e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 80.05  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK----RLNVQwlrAHLGIVSQEPILF 1123
Cdd:PRK10762   15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQELNLI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 D-CSIAENIAYGdnsrvvsqEEIVRA---------AKEANihAFIESLPNKYSTK--VGDkgtqLSGGQKQRIAIARALV 1191
Cdd:PRK10762   92 PqLTIAENIFLG--------REFVNRfgridwkkmYAEAD--KLLARLNLRFSSDklVGE----LSIGEQQMVEIAKVLS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1192 RQPHILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNG 1249
Cdd:PRK10762  158 FESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDG 217
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
396-615 4.35e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 80.28  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   396 NVHFSYpSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN--VRFLREI---- 469
Cdd:PRK10261   19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 --------IGVVSQEPV-----LFAT--TIAENIR----YGREnvtmdeieKAVKEANAYDFIMKLPHKfDTLVGERGAQ 530
Cdd:PRK10261   98 mrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASRE--------EAMVEAKRMLDQVRIPEA-QTILSRYPHQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   531 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA----VVQVALDKARKGrtTIVIAHRLSTVRN-ADVIAGFDDGV 605
Cdd:PRK10261  169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGE 246
                         250
                  ....*....|
gi 42741659   606 IVEKGNHDEL 615
Cdd:PRK10261  247 AVETGSVEQI 256
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
403-586 4.83e-15

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 75.09  E-value: 4.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    403 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFAT 482
Cdd:TIGR01189    9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    483 TIAENIRYGRE--NVTMDEIEKAVKEANaydfimkLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:TIGR01189   89 SALENLHFWAAihGGAQRTIEDALAAVG-------LTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
                          170       180
                   ....*....|....*....|....*.
gi 42741659    561 LDTESEAVVQVALDkARKGRTTIVIA 586
Cdd:TIGR01189  158 LDKAGVALLAGLLR-AHLARGGIVLL 182
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1035-1251 5.13e-15

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 79.30  E-value: 5.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVF-----NYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPLAGKVLLDGKEIKRLNVQ 1107
Cdd:COG3845  251 AEPGEVVLevenlSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPR 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1108 WLRAH-LGIVSQEP-----ILfDCSIAENIAYGDnsrvVSQEEIVRAA--KEANIHAFIESLPNKYSTKVGDKGT---QL 1176
Cdd:COG3845  329 ERRRLgVAYIPEDRlgrglVP-DMSVAENLILGR----YRRPPFSRGGflDRKAIRAFAEELIEEFDVRTPGPDTparSL 403
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1177 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:COG3845  404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1041-1255 5.40e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 79.90  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1041 VFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVS 1117
Cdd:PRK10261  329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1118 QEPI-------LFDCSIAE-----NIAYGD--NSRVVSQEEIVRAAKEaniHAFieSLPNKYstkvgdkgtqlSGGQKQR 1183
Cdd:PRK10261  408 QDPYasldprqTVGDSIMEplrvhGLLPGKaaAARVAWLLERVGLLPE---HAW--RYPHEF-----------SGGQRQR 471
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1184 IAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:PRK10261  472 ICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
409-615 5.76e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 76.67  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGM-----VSVDGQDIRTI-NVRFLREIIGVVSQEPVLFAT 482
Cdd:PRK14271   36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   483 TIAENIRYG-RENVTMDEIE-KAVKEANAYDfiMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK14271  116 SIMDNVLAGvRAHKLVPRKEfRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   561 LDTESEAVVQVALDKARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK14271  194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
402-638 6.52e-15

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 77.43  E-value: 6.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  402 PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIiGVV----SQ-- 475
Cdd:COG4586   30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  476 --EPVLfattiaENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPHKFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 551
Cdd:COG4586  109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  552 LLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV----RNADVIagfDDGVIVEKGNHDELmKEKGIYFKL 625
Cdd:COG4586  176 LFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIealcDRVIVI---DHGRIIYDGSLEEL-KERFGPYKT 251
                        250
                 ....*....|...
gi 42741659  626 VTMQTAGNEVELE 638
Cdd:COG4586  252 IVLELAEPVPPLE 264
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1049-1256 6.86e-15

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 75.83  E-value: 6.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGKVLLDGKEIKRLNVQwLRAHLGI----------- 1115
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1116 -VSQEPILfdcsiaeNIAYgdNSRVVSQEEivraaKEANIHAFIESLPNKySTKVGDKGTQL--------SGGQKQRIAI 1186
Cdd:CHL00131   98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEK-LKLVGMDPSFLsrnvnegfSGGEKKRNEI 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1187 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVFQNGRVKEHGT 1256
Cdd:CHL00131  163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
405-562 1.44e-14

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 74.93  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   405 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF-LREIIGVVSQEPVLFAT- 482
Cdd:PRK10895   14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   483 TIAENIrygrenVTMDEIEKAVKEANAYDFIMKLPHKFDT--LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK10895   94 SVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167

                  ..
gi 42741659   561 LD 562
Cdd:PRK10895  168 VD 169
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
146-343 1.61e-14

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 75.56  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  146 KIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVL 225
Cdd:cd18570   76 RLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  226 GLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 305
Cdd:cd18570  155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42741659  306 IYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF 343
Cdd:cd18570  235 SLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
392-610 1.91e-14

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 73.05  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPT-EGMVSVDGqdiRTINVRFLRe 468
Cdd:cd03232    4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILING---RPLDKNFQR- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 IIGVVSQEPVLFAT-TIAENIRygrenvtmdeiekavkeanaydFIMKLphkfdtlvgeRGaqLSGGQKQRIAIARALVR 547
Cdd:cd03232   80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  548 NPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLStvrnADVIAGFDDGVIVEKG 610
Cdd:cd03232  126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1042-1262 2.18e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 74.83  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1042 FNYPT----RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVS 1117
Cdd:PRK15112   14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1118 QEPI-----------LFDCSIAENIAYGDNSRvvsQEEIVRAAKEANI---HAfieslpNKYSTkvgdkgtQLSGGQKQR 1183
Cdd:PRK15112   94 QDPStslnprqrisqILDFPLRLNTDLEPEQR---EKQIIETLRQVGLlpdHA------SYYPH-------MLAPGQKQR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1184 IAIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1260
Cdd:PRK15112  158 LGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237

                  ..
gi 42741659  1261 LA 1262
Cdd:PRK15112  238 LA 239
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
1048-1255 3.46e-14

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 73.97  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGKVLLDGKEIKrlnVQWLRA-HLGIVSQEP-- 1120
Cdd:PRK10418   14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGrKIATIMQNPrs 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1121 ------ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQP 1194
Cdd:PRK10418   91 afnplhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  1195 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1255
Cdd:PRK10418  160 PFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
87-343 3.46e-14

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 74.74  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   87 DLMSNIT-------NRSDINDTGFFMnleedmtryayyySGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRqe 159
Cdd:cd18548   20 TLMADIIdegiangDLSYILRTGLLM-------------LLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQS-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  160 igwFDVHDVGE-----LNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAK 234
Cdd:cd18548   85 ---FSFAEIDKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  235 ILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAF 314
Cdd:cd18548  162 KAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAIL 241
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 42741659  315 WYGTTLVLSGEYSIGQV-------LTVFFSVLIGAF 343
Cdd:cd18548  242 WFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
144-341 5.14e-14

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 74.06  E-value: 5.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  144 IHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISP 223
Cdd:cd18550   71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  224 VLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAA--IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 301
Cdd:cd18550  151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42741659  302 AFLLIYASYALAFWYGTTLVLSGEYSIGQVltVFFSVLIG 341
Cdd:cd18550  231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
413-618 5.77e-14

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 73.04  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   413 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPTEGMVSVDGQDIRTINVRFLREIIGVVSQE-PVLFATTIAENI-RY 490
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   491 GRENVTMDEIEKAVKE-ANAYDFIMKLPhkfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSALD 562
Cdd:PRK03695   94 QPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659   563 TESeavvQVALDK-----ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:PRK03695  166 VAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1053-1261 6.65e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 73.04  E-value: 6.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHL-----GIVSQEP--- 1120
Cdd:PRK11701   22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1121 ILFDCSIAENIA----------YGD----NSRVVSQEEIVRAAkeanihafIESLPnkystkvgdkgTQLSGGQKQRIAI 1186
Cdd:PRK11701  102 LRMQVSAGGNIGerlmavgarhYGDiratAGDWLERVEIDAAR--------IDDLP-----------TTFSGGMQQRLQI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1187 ARALVRQPHILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQ 1259
Cdd:PRK11701  163 ARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQ 238

                  ..
gi 42741659  1260 LL 1261
Cdd:PRK11701  239 VL 240
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1053-1249 6.87e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 75.98  E-value: 6.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLG--IVSQEPILFD-CSIAE 1129
Cdd:PRK09700   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLTVLE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1130 NIAYGDN-SRVVSQEEIVRAAK---EANIHAFIESLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:PRK09700  100 NLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 42741659  1206 L-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNG 1249
Cdd:PRK09700  176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1047-1232 7.48e-14

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 71.76  E-value: 7.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1047 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRL------NVQWLRAHLGIVS--- 1117
Cdd:PRK13538   11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTelt 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1118 -QEPILFDCSIAeniaygdnsRVVSQEEIVRAAKEANIHAFiESLPNKystkvgdkgtQLSGGQKQRIAIARALVRQPHI 1196
Cdd:PRK13538   91 aLENLRFYQRLH---------GPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPL 150
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 42741659  1197 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAH 1232
Cdd:PRK13538  151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
111-335 7.98e-14

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 73.66  E-value: 7.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  111 MTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKI 190
Cdd:cd18545   39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  191 GMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ 270
Cdd:cd18545  119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  271 KKELERYNKNLEEAKRIGIkKAITANISIGAAFLLIYA-SYALAFWYGTTLVLSGEYSIGqVLTVF 335
Cdd:cd18545  199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG-VLVAF 262
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
767-925 8.37e-14

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 73.73  E-value: 8.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  767 FITFFLQG-FTF------GKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSrlaVITQN 839
Cdd:cd18574   49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  840 IANLG--TGIIISFIY-GWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTQE 913
Cdd:cd18574  124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
                        170
                 ....*....|..
gi 42741659  914 QKFEHMYAQSLQ 925
Cdd:cd18574  201 DRELELYEEEVE 212
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
403-619 9.04e-14

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 71.91  E-value: 9.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  403 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTEGMVSVDGQDIrtinvrflreiigvvSQEpvlf 480
Cdd:COG2401   39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE---- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  481 aTTIAENIryGRENVTMDEIE--KAVKEANAYDFIMKLPHkfdtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEAT 558
Cdd:COG2401  100 -ASLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFC 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  559 SALDTESEAVVQVALDK-ARKGRTTIVIA-HRlstvrnADVIAGFDDGVIVEKGnHDELMKEK 619
Cdd:COG2401  165 SHLDRQTAKRVARNLQKlARRAGITLVVAtHH------YDVIDDLQPDLLIFVG-YGGVPEEK 220
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
413-562 1.04e-13

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 74.14  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   413 LNLKVQ-----SGQTvALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ---DI-RTINVRFLREIIGVVSQEPVLFA-T 482
Cdd:PRK11144   13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   483 TIAENIRYGrenvtMDEIEKAvkeanaydfimklphKFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKILL 553
Cdd:PRK11144   92 KVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLL 151

                  ....*....
gi 42741659   554 LDEATSALD 562
Cdd:PRK11144  152 MDEPLASLD 160
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
410-604 1.09e-13

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 70.54  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-IGVVSQEPV---LFAT-TI 484
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  485 AENIrygrenvtmdeiekavkeanaydfimklphkfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 564
Cdd:cd03215   96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42741659  565 S-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDG 604
Cdd:cd03215  139 AkAEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEG 180
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
419-611 1.23e-13

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 69.71  E-value: 1.23e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     419 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPTEGMVSVDGQDIRTINVRFLREIIgvvsqepvlfattiaenirygrenvtm 497
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659     498 deiekavkeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALD--- 574
Cdd:smart00382   54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 42741659     575 ----KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 611
Cdd:smart00382  108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
382-615 1.39e-13

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 72.49  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   382 GHKPDNIkgnLEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI 461
Cdd:PRK11831    1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   462 NVRFL---REIIGVVSQEPVLFA-TTIAENIRYG-RENVTMDE--IEKAVkeanaydfIMKLphkfdTLVGERGA----- 529
Cdd:PRK11831   75 SRSRLytvRKRMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmp 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   530 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHR----LSTVRNADVIAgfd 602
Cdd:PRK11831  142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVA--- 218
                         250
                  ....*....|...
gi 42741659   603 DGVIVEKGNHDEL 615
Cdd:PRK11831  219 DKKIVAHGSAQAL 231
hmuV PRK13547
heme ABC transporter ATP-binding protein;
396-617 1.57e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 72.55  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   396 NVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPTE-------GMVSVDGQDIRTINVRFLR 467
Cdd:PRK13547    3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   468 EIIGVVSQ--EPVlFATTIAENIRYGR----------ENVTMDEIEKAVKEANAydfimklphkfDTLVGERGAQLSGGQ 535
Cdd:PRK13547   83 RLRAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   536 KQRIAIARAL---------VRNPKILLLDEATSALDTES-----EAVVQVALDkARKGRTTIVIAHRLSTvRNADVIAGF 601
Cdd:PRK13547  151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHqhrllDTVRRLARD-WNLGVLAIVHDPNLAA-RHADRIAML 228
                         250
                  ....*....|....*.
gi 42741659   602 DDGVIVEKGNHDELMK 617
Cdd:PRK13547  229 ADGAIVAHGAPADVLT 244
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
395-573 2.92e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 71.30  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   395 RNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrfLReiIGVVS 474
Cdd:PRK09544    8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   475 QEPVLFAT---TIAENIRYgRENVTMDEIEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIARALVRNPKI 551
Cdd:PRK09544   74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQL 141
                         170       180
                  ....*....|....*....|..
gi 42741659   552 LLLDEATSALDTESeavvQVAL 573
Cdd:PRK09544  142 LVLDEPTQGVDVNG----QVAL 159
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
1026-1261 3.51e-13

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 71.36  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1026 LMPNTLEGNVTFG--EVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKR 1103
Cdd:PRK10575    1 MQEYTNHSDTTFAlrNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1104 LNVQWLRAHLGIVSQE-PILFDCSIAENIA------------YGDNSRVVSQEEIVRAAKEANIHAFIESlpnkystkvg 1170
Cdd:PRK10575   78 WSSKAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS---------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1171 dkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVF 1246
Cdd:PRK10575  148 -----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVAL 221
                         250
                  ....*....|....*
gi 42741659  1247 QNGRVKEHGTHQQLL 1261
Cdd:PRK10575  222 RGGEMIAQGTPAELM 236
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
1053-1249 4.05e-13

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 69.19  E-value: 4.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVKKGQTLALVGSSGCGKSTvvqLLerfyDPLA---------GKVLLDGKEIKrlnvQWLRAHLGIVSQEPILF 1123
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTT---LL----DVLAgrktagvitGEILINGRPLD----KNFQRSTGYVEQQDVHS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1124 DCSIaeniaygdnsrvvsqeeiVRaakeanihafiESLpnKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:cd03232   92 PNLT------------------VR-----------EAL--RFSALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPT 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 42741659 1204 SALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVFQNG 1249
Cdd:cd03232  137 SGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1051-1251 4.40e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 73.23  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-----------VQWLRAHLGIVSQE 1119
Cdd:PRK10982  262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYL 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1120 PILFDCSIAENIAYGDNSRVVSQEEIvraakEANIHAFIESLPNK---YSTKVGdkgtQLSGGQKQRIAIARALVRQPHI 1196
Cdd:PRK10982  342 DIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1197 LLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:PRK10982  413 LMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1036-1262 6.22e-13

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 72.94  E-value: 6.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1036 TFGEVVFN-------YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PLAGKVLLDGKEIK-RLNV 1106
Cdd:TIGR02633  252 EIGDVILEarnltcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDiRNPA 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1107 QWLRAHLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGtQLSGGQKQ 1182
Cdd:TIGR02633  332 QAIRAGIAMVPEDRkrhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQ 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1183 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK----EHG- 1255
Cdd:TIGR02633  411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAl 490

                   ....*..
gi 42741659   1256 THQQLLA 1262
Cdd:TIGR02633  491 TQEQVLA 497
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
1045-1251 6.49e-13

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 69.67  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1045 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlNVQW-----LRAHLGIV--S 1117
Cdd:cd03267   29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1118 QEPILFDCSIAENIAYgdnSRVVSQEEIVRAAKeaNIHAFIESLPnkySTKVGDKGT-QLSGGQKQRIAIARALVRQPHI 1196
Cdd:cd03267  103 KTQLWWDLPVIDSFYL---LAAIYDLPPARFKK--RLDELSELLD---LEELLDTPVrQLSLGQRMRAEIAAALLHEPEI 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659 1197 LLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFQNGRV 1251
Cdd:cd03267  175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
409-615 6.85e-13

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 70.11  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   409 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP----TEGMVSVDGQDIRTINVRflREIIGVVSQEP------- 477
Cdd:PRK10418   18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrsafnpl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   478 VLFATTIAENIR-YGRE--NVTMDEIEKAVKEANAyDFIMKLpHKFdtlvgergaQLSGGQKQRIAIARALVRNPKILLL 554
Cdd:PRK10418   96 HTMHTHARETCLaLGKPadDATLTAALEAVGLENA-ARVLKL-YPF---------EMSGGMLQRMMIALALLCEAPFIIA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   555 DEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 615
Cdd:PRK10418  165 DEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
392-607 8.86e-13

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 72.37  E-value: 8.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVhfSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 470
Cdd:COG3845  258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVSQEPVLFAT----TIAENI---RYGRENVT------MDEIEKAVKEanaydfIMKlphKFD-------TLVGergaQ 530
Cdd:COG3845  336 AYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEE------LIE---EFDvrtpgpdTPAR----S 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  531 LSGGQKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 607
Cdd:COG3845  403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
392-587 9.56e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 68.68  E-value: 9.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREII- 470
Cdd:PRK13538    2 LEARNLACE---RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLy 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 -----GVvsqEPVLfatTIAENIRY---GRENVTMDEIEKAVKEANAYDFiMKLPhkfdtlvgerGAQLSGGQKQRIAIA 542
Cdd:PRK13538   79 lghqpGI---KTEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 42741659   543 RALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAH 587
Cdd:PRK13538  142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
1056-1255 1.07e-12

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 71.06  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1056 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LAGKVLLDGKeiKRLNVQWLRAHLGIVSQEPILF- 1123
Cdd:PRK11144   13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFDAE--KGICLPPEKRRIGYVFQDARLFp 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIAYGDNSRVVSQ-EEIVRAAKeanihafIESLPNKY-STkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PRK11144   90 HYKVRGNLRYGMAKSMVAQfDKIVALLG-------IEPLLDRYpGS--------LSGGEKQRVAIGRALLTAPELLLMDE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1202 ATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVFQNGRVKEHG 1255
Cdd:PRK11144  155 PLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
392-608 1.14e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 72.31  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK10522  323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVLFATTIaeniryGRENvtmdeieKAVKEANAYDFI--MKLPHKFdTLVGERGA--QLSGGQKQRIAIARALVR 547
Cdd:PRK10522  401 AVFTDFHLFDQLL------GPEG-------KPANPALVEKWLerLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALAE 466
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659   548 NPKILLLDEATSALDTESEAVV-QVALDKAR-KGRTTIVIAHRLSTVRNADVIAGFDDGVIVE 608
Cdd:PRK10522  467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
394-586 1.14e-12

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 68.44  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  394 FRNVHF-SYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL------YDPTEGMVSVDGQDIRTINVRFL 466
Cdd:cd03233    6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  467 REIIgVVSQEPVLFAT-TIAEnirygrenvTMDeiekAVKEANAYDFImklphkfdtlvgeRGaqLSGGQKQRIAIARAL 545
Cdd:cd03233   83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42741659  546 VRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIA 586
Cdd:cd03233  134 VSRASVLCWDNSTRGLDSSTAlEILKCIRTMADVLKTTTFVS 175
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1052-1266 1.15e-12

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 69.15  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPILFD-CSIA 1128
Cdd:PRK10895   18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENI-AYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYstkvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK10895   97 DNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  1208 TESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1266
Cdd:PRK10895  170 PISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1051-1233 1.90e-12

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 68.06  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGKVLLDGKEIKRlnvqwlrahlgivsqepilfDCSIA 1128
Cdd:COG2401   44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1129 ENIA-YGDNSRVVsqeEIVRAAKEANIHAFIEslpnKYStkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:COG2401  104 DAIGrKGDFKDAV---ELLNAVGLSDAVLWLR----RFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
                        170       180
                 ....*....|....*....|....*...
gi 42741659 1208 TESEKVVQEALDKA--REGRTCIVIAHR 1233
Cdd:COG2401  169 RQTAKRVARNLQKLarRAGITLVVATHH 196
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
408-619 2.27e-12

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 68.89  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   408 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTEG--------MVSVDGQDIRtiNVRFLREIIGVVSQEP 477
Cdd:PRK09984   18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLAR--DIRKSRANTGYIFQQF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   478 VLF-ATTIAENIRYGRENVT------MDEIEKAVKEaNAYDFIMK--LPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 548
Cdd:PRK09984   96 NLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRvgMVH----FAHQRVSTLSGGQQQRVAIARALMQQ 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   549 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELMKEK 619
Cdd:PRK09984  171 AKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
392-612 4.13e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 67.51  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKST-TVQLMQRL-YDPTEGMVSVDGQDIRTIN------- 462
Cdd:PRK09580    2 LSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   463 -----VRFLREIIGVVSQepvLFATTIAENIRYGRENVTMDEIEKAvkeanayDFI------MKLPHkfDTLVGERGAQL 531
Cdd:PRK09580   79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   532 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG-RTTIVIAH--RLSTVRNADVIAGFDDGVIVE 608
Cdd:PRK09580  147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226

                  ....
gi 42741659   609 KGNH 612
Cdd:PRK09580  227 SGDF 230
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1038-1262 4.85e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 69.96  E-value: 4.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1038 GEVVF---NY----PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLA--GKVLLDGKEIK-RLNVQ 1107
Cdd:PRK13549  256 GEVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKiRNPQQ 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1108 WLRAHLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYST---KVGdkgtQLSGGQ 1180
Cdd:PRK13549  335 AIAQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGN 410
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1181 KQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK--- 1252
Cdd:PRK13549  411 QQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdl 487
                         250
                  ....*....|..
gi 42741659  1253 --EHGTHQQLLA 1262
Cdd:PRK13549  488 inHNLTQEQVME 499
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
127-345 6.51e-12

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 67.98  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  127 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 206
Cdd:cd18565   69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  207 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSftdKELLAYAKAGAVA---EEVLAAIRTVIAFGGQKKELERynknLEE 283
Cdd:cd18565  149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEP---RYRAVREAVGDLNarlENNLSGIAVIKAFTAEDFERER----VAD 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  284 AKRIGIKKAITAnISIGAAF-----LLIYASYALAFWYGTTLVLSGEYSIGQVLTVffsvliGAFSV 345
Cdd:cd18565  222 ASEEYRDANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
757-1008 7.16e-12

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 67.81  E-value: 7.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  757 LLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAI--GSRLA 834
Cdd:cd18548   43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFVmmLLRML 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  835 VITqnIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQE- 913
Cdd:cd18548  121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  914 ---QKFEHMyAQSLqvpYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDV-------LLVFSAVVF 983
Cdd:cd18548  199 yeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMM 274
                        250       260
                 ....*....|....*....|....*
gi 42741659  984 GAMAVGQVSsfapdyaKAKISAAHI 1008
Cdd:cd18548  275 LSMVFVMLP-------RASASAKRI 292
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
391-618 8.30e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 67.84  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   391 NLEFRNVHFSyPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-PTEGM---VSVDGQDIRTINVRFL 466
Cdd:PRK11022    5 NVDKLSVHFG-DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISEKER 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   467 REIIG----VVSQEPVlfaTTIaeNIRYGRENVTMDEIE------KAVKEANAYDFImklphkfdTLVG-----ER---- 527
Cdd:PRK11022   84 RNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRldvy 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   528 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTV-RNADVIAGFDDG 604
Cdd:PRK11022  151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAG 230
                         250
                  ....*....|....
gi 42741659   605 VIVEKGNHDELMKE 618
Cdd:PRK11022  231 QVVETGKAHDIFRA 244
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
121-339 9.04e-12

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 67.51  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  121 IGAGVLVAAYIQvsfWCLAAGRQI----------HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGdKI 190
Cdd:cd18543   41 LVLLLLALGVAE---AVLSFLRRYlagrlslgveHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  191 GMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTdkeLLAYAKAGAVA---EEVLAAIRTVIAF 267
Cdd:cd18543  117 PFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVKAF 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  268 GGQKKELERYNKNLEEAKRIGIKKA-ITANISigAAFLLI-YASYALAFWYGTTLVLSGEYSIGQvLTVFFSVL 339
Cdd:cd18543  194 GRERRELDRFEAAARRLRATRLRAArLRARFW--PLLEALpELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL 264
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1052-1256 1.20e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 66.77  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPLA-------GKVLLDGKEIKRLNVQWL---RAHLGIVSQEP 1120
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1121 ILFdcSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESlpnKYSTKVGDKGTQLSGGQKQRIAIARAL---------V 1191
Cdd:PRK13547   96 FAF--SAREIVLLGRYPHARRAGALTHRDGEIAWQALALA---GATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1192 RQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVFQNGRVKEHGT 1256
Cdd:PRK13547  171 QPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
400-587 1.54e-11

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 68.42  E-value: 1.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    400 SYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGmVSVDGQDIRtinvrflreiIGVVSQEPVL 479
Cdd:TIGR03719   13 VVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-EARPQPGIK----------VGYLPQEPQL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    480 FAT-TIAENI-------------------RYGRENVTMD-------EIEKAVKEANAYDFIMKLPHKFDTLVGERG---- 528
Cdd:TIGR03719   80 DPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALRCPPWdadv 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659    529 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALdKARKGrTTIVIAH 587
Cdd:TIGR03719  160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
ycf16 CHL00131
sulfate ABC transporter protein; Validated
392-618 2.42e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 65.43  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM--QRLYDPTEGMVSVDGQDIRTINVR----- 464
Cdd:CHL00131    8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEerahl 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 --FLR-----EIIGVVSQEpvlFATTIAENIRYGRENVTMDEIEkavkeanAYDFIM-KLPhkfdtLVGERGAQL----- 531
Cdd:CHL00131   85 giFLAfqypiEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   532 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAH--RLSTVRNADVIAGFDDGV 605
Cdd:CHL00131  150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
                         250
                  ....*....|...
gi 42741659   606 IVEKGNhDELMKE 618
Cdd:CHL00131  230 IIKTGD-AELAKE 241
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
410-592 3.08e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 65.67  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRtinvRFLRE-IIGVVSQE-------PVLFA 481
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENiRYGreNVTMDEIEKA-----VKEANAYDFIMKLPHKfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDE 556
Cdd:PRK15056   99 DVVMMG-RYG--HMGWLRRAKKrdrqiVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 42741659   557 ATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTV 592
Cdd:PRK15056  169 PFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
121-343 3.22e-11

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 65.93  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  121 IGAGVLVAAYI-------QVSFWCLAAGRQI-HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE----GIGD 188
Cdd:cd18549   43 IIGAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  189 kigmFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGlsaavwakILSSFTDKEL-----LAYAKAG---AVAEEVLAA 260
Cdd:cd18549  123 ----LFISIITIIGSFIILLTINVPLTLIVFALLPLMI--------IFTIYFNKKMkkafrRVREKIGeinAQLEDSLSG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  261 IRTVIAFGGQKKELERY---NKNLEEAKRIGIkKAITANISIGAAFLLIYasYALAFWYGTTLVLSGEYSIGQVLTvfFS 337
Cdd:cd18549  191 IRVVKAFANEEYEIEKFdegNDRFLESKKKAY-KAMAYFFSGMNFFTNLL--NLVVLVAGGYFIIKGEITLGDLVA--FL 265

                 ....*.
gi 42741659  338 VLIGAF 343
Cdd:cd18549  266 LYVNVF 271
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
392-610 3.30e-11

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 65.33  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEvkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-------- 463
Cdd:PRK11701    7 LSVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaer 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   464 RFL-REIIGVVSQEP-------VLFATTIAENI------RYGRENVT----MDEIEKAVkeanayDFIMKLPHKFdtlvg 525
Cdd:PRK11701   84 RRLlRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATagdwLERVEIDA------ARIDDLPTTF----- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   526 ergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVqvaLDKARK-----GRTTIVIAHRLSTVRN-ADVIA 599
Cdd:PRK11701  153 ------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARL---LDLLRGlvrelGLAVVIVTHDLAVARLlAHRLL 223
                         250
                  ....*....|.
gi 42741659   600 GFDDGVIVEKG 610
Cdd:PRK11701  224 VMKQGRVVESG 234
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
711-995 3.85e-11

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 65.58  E-value: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIgvftriDDPETKRQNSNL--FSLLFLALGIISFITFFLQGFTFGKAGEILTKRL 788
Cdd:cd18543    1 LILALLAALLATLAGLAIPLLTRRAI------DGPIAHGDRSALwpLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  789 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIgSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPII 868
Cdd:cd18543   75 RTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  869 AIAGVVEMKMLSGQALKDKkelEGSGKIATEAIEN---FRTVVSLTQE----QKFEHMyAQSLqvpYRNSLRKAHIFGIT 941
Cdd:cd18543  152 VLVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRErrelDRFEAA-ARRL---RATRLRAARLRARF 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42741659  942 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDvLLVFSAVVfgAMAVGQVSSFA 995
Cdd:cd18543  225 WPLLEALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL--TMLVWPVRMLG 275
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
123-362 4.60e-11

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 65.25  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  123 AGVLVAAYI-QVSFWCL-------AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 194
Cdd:cd18778   43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  195 QSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 274
Cdd:cd18778  123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  275 ERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVltVFFSVLIGAF--SVGQASPSI 352
Cdd:cd18778  203 KRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSLHGLN 280
                        250
                 ....*....|
gi 42741659  353 EAFANARGAA 362
Cdd:cd18778  281 EMLQRALAGA 290
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1062-1246 4.86e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 62.01  E-value: 4.86e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    1062 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVlldgkeikrlnvqwlrahlgivsqepILFDCSIAENIAYGDNSRVVs 1141
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLLLII- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    1142 qeeivraakeanihafieslpnkystkVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1219
Cdd:smart00382   54 ---------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
                           170       180       190
                    ....*....|....*....|....*....|..
gi 42741659    1220 -----KAREGRTCIVIAHRLSTIQNADLIVVF 1246
Cdd:smart00382  107 lllllKSEKNLTVILTTNDEKDLGPALLRRRF 138
PLN03211 PLN03211
ABC transporter G-25; Provisional
1052-1274 5.07e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 67.21  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPLAGKVLLDGKEIKRlnvQWLRaHLGIVSQEPILF-DCSIA 1128
Cdd:PLN03211   83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENIAYGDNSRV---VSQEEIVRAAkEANIHAFieSLPNKYSTKVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PLN03211  159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1205 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLLAqkgiYFSMVSVQ 1274
Cdd:PLN03211  236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1052-1235 5.65e-11

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 67.08  E-value: 5.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGKVLLDGKEIKrlnvqwlrahLGIVSQEPILFDCSIAENI 1131
Cdd:TIGR00954  467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGK----------LFYVPQRPYMTLGTLRDQI 535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1132 AYGDNS-----RVVSQEEIVRAAKEANIHAFIESlpNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:TIGR00954  536 IYPDSSedmkrRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
                          170       180
                   ....*....|....*....|....*....
gi 42741659   1207 DTESEKVVQEALDKAreGRTCIVIAHRLS 1235
Cdd:TIGR00954  614 SVDVEGYMYRLCREF--GITLFSVSHRKS 640
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
715-1005 5.68e-11

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 65.16  E-value: 5.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  715 VFCAIINGGLQPAFAIiFSKIIgvftrIDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMV 792
Cdd:cd18570    8 LLLSLLITLLGIAGSF-FFQIL-----IDDiiPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  793 FRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGAIGSrlAVITQnIANLGTGIIIS---FIYGWQLTLLLLAIVPIIA 869
Cdd:cd18570   82 FKHLLKLPLSFFE--TRKTGEIISRF-NDANKIREAISS--TTISL-FLDLLMVIISGiilFFYNWKLFLITLLIIPLYI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  870 IAGVVEMKMLSGqalKDKKELEGSGKIATEAIENFR---TVVSLTQEQKFehmyAQSLQVPYRNSLRKAHIFGITF---- 942
Cdd:cd18570  156 LIILLFNKPFKK---KNREVMESNAELNSYLIESLKgieTIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSnlqs 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  943 SFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDvLLVFSAVVFGAM-AVGQVSSFAPDYAKAKISA 1005
Cdd:cd18570  229 SIKGLISLIGSLLILWIGSYLVIKGQLSLGQ-LIAFNALLGYFLgPIENLINLQPKIQEAKVAA 291
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1049-1263 6.08e-11

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 65.52  E-value: 6.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--LAGKVLLDGKEI-----KRLNVqwLRA-HLGIVSQE 1119
Cdd:PRK09473   28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1120 PIlfdCSIAENIAYGDN-----------SRVVSQEEIVR---AAKEANIHAFIESLPNKYStkvgdkgtqlsGGQKQRIA 1185
Cdd:PRK09473  106 PM---TSLNPYMRVGEQlmevlmlhkgmSKAEAFEESVRmldAVKMPEARKRMKMYPHEFS-----------GGMRQRVM 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1186 IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1262
Cdd:PRK09473  172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFY 251

                  .
gi 42741659  1263 Q 1263
Cdd:PRK09473  252 Q 252
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1049-1244 7.60e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 66.51  E-value: 7.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEI---KRLNVQWL-----RAHLGIVsqep 1120
Cdd:PRK11147   15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLqqdppRNVEGTV---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1121 ilFDcSIAENIA--------YGDNSRVVSQEE----IVRAAK-------------EANIHAFIESL---PNKystkvgdK 1172
Cdd:PRK11147   84 --YD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------A 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1173 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIV 1244
Cdd:PRK11147  154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1052-1234 8.49e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 63.98  E-value: 8.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnvqwLRahLGIVSQEpILFDCSIAENI 1131
Cdd:PRK09544   19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQK-LYLDTTLPLTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1132 aygdnSRV------VSQEEIVRAAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:PRK09544   87 -----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
                         170       180       190
                  ....*....|....*....|....*....|.
gi 42741659  1206 LDTESEKVVQEALDKAREGRTCIV--IAHRL 1234
Cdd:PRK09544  151 VDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1049-1263 8.55e-11

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 63.66  E-value: 8.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPI--- 1121
Cdd:PRK09580   13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeip 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1122 ------LFDCSIAENIAYGDnsrvvsQEEIVRAAKEANIHAFIESL--PNKYSTKVGDKGtqLSGGQKQRIAIARALVRQ 1193
Cdd:PRK09580   92 gvsnqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  1194 PHILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGTH---QQLLAQ 1263
Cdd:PRK09580  164 PELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
742-970 8.85e-11

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 64.45  E-value: 8.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  742 IDD---PETKRQNSNLFSLLFLALGIISFITFFLQ---GFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALT 815
Cdd:cd18563   26 IDDvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLM 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  816 TRLANDAAQVKGAIGSRLAVITQNIANL-GTGIIIsFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALK-DKKELEGS 893
Cdd:cd18563  104 SRVTSDTDRLQDFLSDGLPDFLTNILMIiGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRqWRRWSRLN 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  894 GKIAtEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRkahIFGITFSFTQAMMYFSYAGCF---RFGAYLVAHKLMS 970
Cdd:cd18563  183 SVLN-DTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR---AEKLWATFFPLLTFLTSLGTLivwYFGGRQVLSGTMT 258
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
392-596 9.27e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 62.66  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 471
Cdd:PRK13540    2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVLFATTIAEN----IRYGRENVTMDEIEKavkeanaydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVR 547
Cdd:PRK13540   79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMS 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 42741659   548 NPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNAD 596
Cdd:PRK13540  145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
743-929 1.37e-10

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 63.64  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  743 DDPETKRQNSNLFSLLflalGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDA 822
Cdd:cd18589   30 DAPEAFTAAITVMSLL----TIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  823 AQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIE 902
Cdd:cd18589  104 EDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFS 183
                        170       180
                 ....*....|....*....|....*..
gi 42741659  903 NFRTVVSLTQEQKFEHMYAQSLQVPYR 929
Cdd:cd18589  184 AMKTVRSFANEEGEAQRYRQRLQKTYR 210
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
401-587 2.02e-10

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 62.43  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  401 YPSRKEVKILKGLNLKVQSG-----QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI----------RTINVR- 464
Cdd:cd03237    1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadYEGTVRd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  465 FLREIIGVVSQEPvLFATTIAEnirygrenvtmdeiekavkeanaydfimklPHKFDTLVGERGAQLSGGQKQRIAIARA 544
Cdd:cd03237   81 LLSSITKDFYTHP-YFKTEIAK------------------------------PLQIEQILDREVPELSGGELQRVAIAAC 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659  545 LVRNPKILLLDEATSALDTESEAVVQVAL----DKARKgrTTIVIAH 587
Cdd:cd03237  130 LSKDADIYLLDEPSAYLDVEQRLMASKVIrrfaENNEK--TAFVVEH 174
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
395-566 2.04e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 64.75  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   395 RNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR-FLREIIGVV 473
Cdd:PRK10982    2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   474 SQE-PVLFATTIAENI---RYGRENVTMDEiEKAVKEANAYdfimklphkFDTL-----VGERGAQLSGGQKQRIAIARA 544
Cdd:PRK10982   79 HQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAKA 148
                         170       180
                  ....*....|....*....|..
gi 42741659   545 LVRNPKILLLDEATSALdTESE 566
Cdd:PRK10982  149 FSYNAKIVIMDEPTSSL-TEKE 169
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
417-590 2.16e-10

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 62.77  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  417 VQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSvDGQDIRTInvrfLREIIGVVSQEpvLFATTIAENIRYGRENVT 496
Cdd:cd03236   23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI----LDEFRGSELQN--YFTKLLEGDVKVIVKPQY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  497 MDEIEKAVKeANAYDFIMKLP--HKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 565
Cdd:cd03236   96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
                        170       180
                 ....*....|....*....|....*.
gi 42741659  566 E-AVVQVALDKARKGRTTIVIAHRLS 590
Cdd:cd03236  175 RlNAARLIRELAEDDNYVLVVEHDLA 200
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
757-1005 2.51e-10

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 63.30  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  757 LLFLALGIIsFITF------FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIG 830
Cdd:cd18564   53 LLLAAAALV-GIALlrglasYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  831 SRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAgVVEMKMLSGQALKDKKELEGS-GKIATEAIENFRTVVS 909
Cdd:cd18564  130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLA-ARRFSRRIKEASREQRRREGAlASVAQESLSAIRVVQA 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  910 LTQEQKFEHMYAQSLQVPYRNSLRKAHI-------FGITFSFTQAMMYFsyagcfrFGAYLVAHKLMSFEDvLLVFSAVV 982
Cdd:cd18564  209 FGREEHEERRFARENRKSLRAGLRAARLqallspvVDVLVAVGTALVLW-------FGAWLVLAGRLTPGD-LLVFLAYL 280
                        250       260
                 ....*....|....*....|....
gi 42741659  983 FGAMA-VGQVSSFAPDYAKAKISA 1005
Cdd:cd18564  281 KNLYKpVRDLAKLTGRIAKASASA 304
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
119-336 2.80e-10

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 62.89  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  119 SGIGAGVLVAAYIQVSFWCLAAGRQ----IHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 194
Cdd:cd18546   42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  195 QSMATFFTGFIVGFTRGWKLTLVILAISPVLGLsAAVWAKILSSFtdkellAYAKA-GAVAE------EVLAAIRTVIAF 267
Cdd:cd18546  122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  268 GGQKKELERYnKNLEEAKRIGIKKAITAN-ISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGqVLTVFF 336
Cdd:cd18546  195 RRERRNAERF-AELSDDYRDARLRAQRLVaIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
754-1008 3.24e-10

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 62.51  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  754 LFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 833
Cdd:cd18546   40 LAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  834 AVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKmLSGQALKDKKElegsgKIAT------EAIENFRTV 907
Cdd:cd18546  118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-----RIAAvnadlqETLAGIRVV 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  908 VSLTQEQKFEHMYAQsLQVPYRNS-LRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFeDVLLVF---SAVVF 983
Cdd:cd18546  192 QAFRRERRNAERFAE-LSDDYRDArLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTV-GVLVAFllyLRRFF 269
                        250       260
                 ....*....|....*....|....*
gi 42741659  984 GAMavGQVSSFAPDYAKAKISAAHI 1008
Cdd:cd18546  270 API--QQLSQVFDSYQQARAALEKI 292
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
1056-1261 5.54e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 61.49  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1056 LSLEVKKGQTLALVGSSGCGKSTvvqLLERFYD--PLAGKVLLDGKEIKRLNVQWL---RAHLgiVSQEPILF------- 1123
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFampvfqy 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 -DCSIAENIAYGDNSRVVsqEEIVRAAKeanihafiesLPNKYSTKVGdkgtQLSGGQKQRIAIArALVRQ------PH- 1195
Cdd:PRK03695   90 lTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwpdinPAg 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  1196 -ILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1261
Cdd:PRK03695  153 qLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1039-1241 7.79e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 59.96  E-value: 7.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1039 EVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ 1118
Cdd:PRK13540    6 ELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1119 EPILFDCSIAENIAYG--DNSRVVSQEEIVRAAKEANIHAFIESLpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHI 1196
Cdd:PRK13540   83 SGINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKL 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 42741659  1197 LLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1241
Cdd:PRK13540  149 WLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
412-592 1.48e-09

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 60.00  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   412 GLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--------------RTI-NVRFLREIIGV---- 472
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   473 VSQE--------PVLFATTiaeniRYGREnvtmdEIEKAVKEANAYDFIMKLPhkfdtLVGERGAQLSGGQKQRIAIARA 544
Cdd:PRK11300  103 VAQHqqlktglfSGLLKTP-----AFRRA-----ESEALDRAATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 42741659   545 LVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV 592
Cdd:PRK11300  168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLV 217
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1048-1250 1.75e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1048 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-RLNVQWLRAHLGIVSQE-PILFDC 1125
Cdd:PRK10982    9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 SIAENIAYGDNSR---VVSQEEIVRAAKeanihAFIESLPNKYSTKvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1202
Cdd:PRK10982   89 SVMDNMWLGRYPTkgmFVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 42741659  1203 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVFQNGR 1250
Cdd:PRK10982  162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1057-1261 1.84e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.85  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1057 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-RLNVQWLRAhlGIV------SQEPILFDCSIAE 1129
Cdd:PRK11288  273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRA--GIMlcpedrKAEGIIPVHSVAD 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1130 NIAYGDNSRVVSQEEIVRAAKEA-NIHAFIESL----PNKySTKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1204
Cdd:PRK11288  351 NINISARRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  1205 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLL 1261
Cdd:PRK11288  426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
728-870 2.05e-09

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 60.19  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  728 FAIIFSKIIGV----FTR--IDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQ 799
Cdd:cd18550    6 LLILLSALLGLlpplLLReiIDDalPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRM 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  800 DVSWFDDPKntTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 870
Cdd:cd18550   86 SLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1056-1256 2.91e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 60.14  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1056 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLR----AHLGIVSQEPI--LFDC 1125
Cdd:PRK11022   26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1126 -----SIAENIAY--GDNSRVVSQeeivRAakeanihafIESLpnkysTKVG--DKGT-------QLSGGQKQRIAIARA 1189
Cdd:PRK11022  106 ytvgfQIMEAIKVhqGGNKKTRRQ----RA---------IDLL-----NQVGipDPASrldvyphQLSGGMSQRVMIAMA 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1190 LVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGT 1256
Cdd:PRK11022  168 IACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
PLN03211 PLN03211
ABC transporter G-25; Provisional
405-591 2.99e-09

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 61.43  E-value: 2.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   405 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPT-EGMVSVDGqdiRTINVRFLREIiGVVSQEPVLFA- 481
Cdd:PLN03211   79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYPh 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENIRYGRENVTMDEIEKAVKEANAYDFI--MKLPHKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDE 556
Cdd:PLN03211  155 LTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDE 232
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 42741659   557 ATSALD-TESEAVVQVALDKARKGRTTIVIAHRLST 591
Cdd:PLN03211  233 PTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
711-873 3.49e-09

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 59.47  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQpafaIIFSKIIGVFT-RIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLR 789
Cdd:cd18778    1 LILTLLCALLSTLLG----LVPPWLIRELVdLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  790 YMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIgsrLAVITQNIANLGTGIIIS---FIYGWQLTLLLLAIVP 866
Cdd:cd18778   77 SDLYDKLQRLSLRYFDDRQ--TGDLMSRVINDVANVERLI---ADGIPQGITNVLTLVGVAiilFSINPKLALLTLIPIP 151

                 ....*..
gi 42741659  867 IIAIAGV 873
Cdd:cd18778  152 FLALGAW 158
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1053-1237 3.53e-09

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 59.13  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGiVSQE-----PILFDcSI 1127
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-QSEEvdwsfPVLVE-DV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1128 AENIAYGDNSRVVSQEEIVRAAKEANIhAFIESLPNKYStKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK15056  101 VMMGRYGHMGWLRRAKKRDRQIVTAAL-ARVDMVEFRHR-QIG----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
                         170       180       190
                  ....*....|....*....|....*....|.
gi 42741659  1208 TESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1237
Cdd:PRK15056  175 VKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1038-1253 3.83e-09

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 60.57  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1038 GEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPLA-GKVLLDGKEIK-RLNVQWLRA 1111
Cdd:PRK09700  262 HETVFEVRnvTSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKK 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1112 HLGIVSQ---EPILF-DCSIAENIA---------YGDNSRVVSQEEIVRAAKEANihafiESLPNKYSTkVGDKGTQLSG 1178
Cdd:PRK09700  339 GMAYITEsrrDNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSG 412
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1179 GQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGRVKE 1253
Cdd:PRK09700  413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
372-564 4.66e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 60.73  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   372 KPSIDSYSKSGhkpdniKGNLEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMV 451
Cdd:PRK11147  306 KMQVEEASRSG------KIVFEMENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   452 SVDGQdirtINVRFL---REIIgvvsqEPvlfATTIAENIRYGRENVTMDEIEKAVKeanAY--DFIMKlPHKFDTLVge 526
Cdd:PRK11147  377 HCGTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV-- 438
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 42741659   527 rgAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 564
Cdd:PRK11147  439 --KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
1053-1244 5.00e-09

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 58.78  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG---IVSQEPI-------- 1121
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1122 -----LFD------CSIAENIAYgdNSRVVSqeeiVRAaKEANIH-----------AFIESLP---NKYST--------- 1167
Cdd:cd03271   89 atytgVFDeirelfCEVCKGKRY--NRETLE----VRY-KGKSIAdvldmtveealEFFENIPkiaRKLQTlcdvglgyi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1168 KVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1243
Cdd:cd03271  162 KLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241

                 .
gi 42741659 1244 V 1244
Cdd:cd03271  242 I 242
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
751-964 5.33e-09

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 59.13  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  751 NSNLFSLLFLALGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQV 825
Cdd:cd18566   35 NESIPTLQVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQI 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  826 KGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgQALKDKKELEGS-GKIATEAIENF 904
Cdd:cd18566  112 REFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERSRADERrQNFLIETLTGI 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659  905 RTVVSLTQEQ----KFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMyfsyAGCFRFGAYLV 964
Cdd:cd18566  191 HTIKAMAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLV 250
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
401-565 7.75e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 59.75  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   401 YPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGmvsvdgqdirtiNVRFLREI-IGVVSQEPVL 479
Cdd:PRK11819   16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------EARPAPGIkVGYLPQEPQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   480 FAT-TIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPH-KFDTLVGERG----------------------------- 528
Cdd:PRK11819   82 DPEkTVRENVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcpp 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 42741659   529 -----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 565
Cdd:PRK11819  157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
121-341 7.81e-09

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 58.37  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  121 IGAGVLVAAYIQVSFWCL-------AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGI-GDKIGM 192
Cdd:cd18782   44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLtGTALTT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  193 FFQSMATFFTgFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAfggQKK 272
Cdd:cd18782  123 LLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNA 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659  273 EL-------ERYNKNLEEAKRIGIKKAITANISigaaFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIG 341
Cdd:cd18782  199 ELkarwrwqNRYARSLGEGFKLTVLGTTSGSLS----QFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
410-598 9.78e-09

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 57.62  E-value: 9.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPTEGMVSVDgqdiRTINV------RFLRE 468
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLhlkkeqpgnHDRIEGLEHID----KVIVIdqspigRTPRS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  469 I----IGVVSQEPVLFATtIAENIRYGRE-------NVTMDEI-EKAVKEAnaYDF---IMKLPHKFDTLV--------- 524
Cdd:cd03271   87 NpatyTGVFDEIRELFCE-VCKGKRYNREtlevrykGKSIADVlDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  525 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRNADVI 598
Cdd:cd03271  164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWI 241
PLN03140 PLN03140
ABC transporter G family member; Provisional
407-612 9.79e-09

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 60.24  E-value: 9.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   407 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM--QRLYDPTEGMVSVDG-----------------QDIRT--INVR- 464
Cdd:PLN03140  893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSpqVTVRe 972
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   465 ------FLREIIGVVSQEPVLFattiaenirygrenvtMDEIEKAVKEANAYDFIMKLPhkfdtlvGERGaqLSGGQKQR 538
Cdd:PLN03140  973 sliysaFLRLPKEVSKEEKMMF----------------VDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKR 1027
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659   539 IAIARALVRNPKILLLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTvrnaDVIAGFDDGVIVEKGNH 612
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
408-590 1.04e-08

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 59.76  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    408 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirtinvrflREIIGVVSQEPVLFATTIAEN 487
Cdd:TIGR00954  466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQ 534
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    488 IRYgrENVTMDEIEKAVKEAN--AYDFIMKLPHKFDTLVGERGAQ-----LSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:TIGR00954  535 IIY--PDSSEDMKRRGLSDKDleQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
                          170       180       190
                   ....*....|....*....|....*....|.
gi 42741659    561 LDTESE-AVVQVAldkARKGRTTIVIAHRLS 590
Cdd:TIGR00954  613 VSVDVEgYMYRLC---REFGITLFSVSHRKS 640
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
392-558 1.61e-08

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 58.88  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  392 LEFRNVhfsypSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF-LREII 470
Cdd:COG1129  257 LEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGI 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  471 GVVS----QEPVLFATTIAENI------RYGReNVTMDEiEKAVKEANAY--DFIMKLPHKfDTLVGergaQLSGGQKQR 538
Cdd:COG1129  330 AYVPedrkGEGLVLDLSIRENItlasldRLSR-GGLLDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLSGGNQQK 402
                        170       180
                 ....*....|....*....|
gi 42741659  539 IAIARALVRNPKILLLDEAT 558
Cdd:COG1129  403 VVLAKWLATDPKVLILDEPT 422
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
120-343 1.66e-08

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 57.52  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  120 GIGAGVLVAAYIQVSF---WCLAagrQIHK-----IRKQFFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGIGDKIG 191
Cdd:cd18555   45 GIGILILFLLYGLFSFlrgYIII---KLQTkldksLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  192 MFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQK 271
Cdd:cd18555  121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42741659  272 KELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF 343
Cdd:cd18555  201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
150-341 1.80e-08

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 57.57  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  150 QFFHAIMRQEIGWFDVHDVGELNTRltddvskINEGigDKIGMFF--QSMATF---FTGFIVG---FTRGWKLTLVILAI 221
Cdd:cd18568   80 DFYKHLLSLPLSFFASRKVGDIITR-------FQEN--QKIRRFLtrSALTTIldlLMVFIYLglmFYYNLQLTLIVLAF 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  222 SPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ----KKELERYNKNLEEAKRiGIKKAITANI 297
Cdd:cd18568  151 IPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErpirWRWENKFAKALNTRFR-GQKLSIVLQL 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42741659  298 SIGAAFLLiyaSYALAFWYGTTLVLSGEYSIGQVltVFFSVLIG 341
Cdd:cd18568  230 ISSLINHL---GTIAVLWYGAYLVISGQLTIGQL--VAFNMLFG 268
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
1046-1209 2.14e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.01  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlRA-HLGIVSQEPIL-F 1123
Cdd:PRK13543   20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSrFMAYLGHLPGLkA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1124 DCSIAENIAY--GDNSRVVSQeeivraakeanihafiesLPNKYSTKVGDKG------TQLSGGQKQRIAIARALVRQPH 1195
Cdd:PRK13543   96 DLSTLENLHFlcGLHGRRAKQ------------------MPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAP 157
                         170
                  ....*....|....
gi 42741659  1196 ILLLDEATSALDTE 1209
Cdd:PRK13543  158 LWLLDEPYANLDLE 171
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
529-685 2.78e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.04  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   529 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALdKARKGrTTIVIAHRLSTVRN-ADVIAGFDDGVIV 607
Cdd:PRK11147  155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   608 E-KGNHDELMKEKGIYFKLVTMQTAGNEVELenaADES---KSEIDAlEMSSNDSR----SSLIRKRSTRRSVRGS---Q 676
Cdd:PRK11147  233 SyPGNYDQYLLEKEEALRVEELQNAEFDRKL---AQEEvwiRQGIKA-RRTRNEGRvralKALRRERSERREVMGTakmQ 308

                  ....*....
gi 42741659   677 AQDRKLSTK 685
Cdd:PRK11147  309 VEEASRSGK 317
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
759-983 2.95e-08

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 56.81  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  759 FLALGIISFITF-------FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDpkNTTGALTTRLANDAAQVKGAIGS 831
Cdd:cd18565   53 LWLLGGLTVAAFlleslfqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  832 RLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIAT---EAIENFRTVV 908
Cdd:cd18565  131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAV---GDLNArleNNLSGIAVIK 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  909 SLTQEQK-FEHMYAQSLQvpYRNSLRKAHIFGITFSFT-QAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVF 983
Cdd:cd18565  208 AFTAEDFeRERVADASEE--YRDANWRAIRLRAAFFPViRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVGTLVTF 282
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1036-1246 3.19e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.90  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1036 TFGEVVFNYPtrpDIPV-LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDgkeikrLNV--- 1106
Cdd:PRK13409  335 SERETLVEYP---DLTKkLGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsyk 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1107 -QWLRA-HLGIVSQepilFDCSIAENIaygDNSRVvsQEEIVraaKEANIHAFIESlpnkystKVGDkgtqLSGGQKQRI 1184
Cdd:PRK13409  406 pQYIKPdYDGTVED----LLRSITDDL---GSSYY--KSEII---KPLQLERLLDK-------NVKD----LSGGELQRV 462
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659  1185 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVF 1246
Cdd:PRK13409  463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVF 527
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
405-592 3.44e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.20  E-value: 3.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    405 KEVKILKGLNLKVQSGQTVALVGNSGCGKST-----TVQLMQRLYDpTEGMVSVDGQDIRTInVRFLREIIGVVSQEPVL 479
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEI-KKHYRGDVVYNAETDVH 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    480 FAT-TIAE-----------NIRYgrENVtmDEIEKAVKEANAYDFIMKLPHKFDTLVGE---RGaqLSGGQKQRIAIARA 544
Cdd:TIGR00956  150 FPHlTVGEtldfaarcktpQNRP--DGV--SREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEA 223
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 42741659    545 LVRNPKILLLDEATSALDTESeavvqvALDKARKGRTTIVIAHRLSTV 592
Cdd:TIGR00956  224 SLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
204-344 3.58e-08

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 56.35  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  204 FIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEE 283
Cdd:cd18588  133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42741659  284 AKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVltVFFSVLIGAFS 344
Cdd:cd18588  213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
111-337 3.86e-08

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 56.33  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  111 MTRYA-------------YYYSGIGAGVLVAAYIQVSFWCLAAGRQ----IHKIRKQFFHAIMRQEIGWFDVHDVGELNT 173
Cdd:cd18540   24 LTKYAidhfitpgtldglTGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  174 RLTDDVSKINE----GIGDkigMFFQSMATFFTgFIVGFTRGWKLTLVILAISPVLglsaaVWAKILssFTDKELLAYAK 249
Cdd:cd18540  104 RVTSDTQRLGEiiswGLVD---LVWGITYMIGI-LIVMLILNWKLALIVLAVVPVL-----AVVSIY--FQKKILKAYRK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  250 AGAVAEEVLAA-------IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVL 322
Cdd:cd18540  173 VRKINSRITGAfnegitgAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVL 252
                        250
                 ....*....|....*
gi 42741659  323 SGEYSIGQvLTVFFS 337
Cdd:cd18540  253 AGAITIGT-LVAFIS 266
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
413-589 4.22e-08

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 58.10  E-value: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    413 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIGVVSQEPVLfattiaENIRYGR 492
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGR 2030
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    493 EN---------VTMDEIEKAvkeANAYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 563
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
                          170       180
                   ....*....|....*....|....*..
gi 42741659    564 ESEAVV-QVALDKARKGRTTIVIAHRL 589
Cdd:TIGR01257 2104 QARRMLwNTIVSIIREGRAVVLTSHSM 2130
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1051-1265 4.44e-08

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 58.10  E-value: 4.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIkRLNVQWLRAHLGIVSQEPILFDCSIA-E 1129
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAIDDLLTGrE 2031
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1130 NIAYGDNSRVVSQEEIVRAAKEAnihafIESLP-NKYSTKVGdkGTqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1208
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWS-----IQSLGlSLYADRLA--GT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659   1209 ESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1265
Cdd:TIGR01257 2104 QARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
108-349 4.63e-08

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 55.97  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  108 EEDMTRYAYYYSGIGAGVLVAAYIQVSFW----CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKIN 183
Cdd:cd18580   34 NSSSGYYLGVYAALLVLASVLLVLLRWLLfvlaGLRASRRLHD---KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLID 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  184 EGIGDKIGMFFQSMATFFTGFIV-GFTRGWkltlvILAISPVLGLSAAVWAK-------------------ILSSFTdke 243
Cdd:cd18580  111 EELPLALLDFLQSLFSVLGSLIViAIVSPY-----FLIVLPPLLVVYYLLQRyylrtsrqlrrlesesrspLYSHFS--- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  244 llayakagavaeEVLAAIRTVIAFGGQKKELERYNKNLeeakrigikkaitaNISIGAAFLLIYASYALAFWYgttlvls 323
Cdd:cd18580  183 ------------ETLSGLSTIRAFGWQERFIEENLRLL--------------DASQRAFYLLLAVQRWLGLRL------- 229
                        250       260
                 ....*....|....*....|....*.
gi 42741659  324 geysigQVLTVFFSVLIGAFSVGQAS 349
Cdd:cd18580  230 ------DLLGALLALVVALLAVLLRS 249
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
402-614 4.95e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 57.23  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   402 PSRKEVKILKG------LNLKVQSGQTVALVGNSGCGKSttvQLMQRLY---DPTEGMVSVDGQdirTINVRFLREII-- 470
Cdd:PRK11288  255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRS---ELMKLLYgatRRTAGQVYLDGK---PIDIRSPRDAIra 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   471 GVV------SQEPVLFATTIAENIRYG--RENVTMDEIEKAVKEA-NAYDFIMKL----PHKfDTLVGergaQLSGGQKQ 537
Cdd:PRK11288  329 GIMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQ 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   538 RIAIARALVRNPKILLLDEATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 614
Cdd:PRK11288  404 KAILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1052-1235 4.99e-08

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 55.45  E-value: 4.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1052 VLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPLAGKVLLD---GKEIKRLNVQWLRAHLGI----- 1115
Cdd:cd03236   16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpq 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1116 -VSQEPILFDCSIAENIAYGDNSRVvsQEEIVRAAKEANIhafiesLPNKYStkvgdkgtQLSGGQKQRIAIARALVRQP 1194
Cdd:cd03236   95 yVDLIPKAVKGKVGELLKKKDERGK--LDELVDQLELRHV------LDRNID--------QLSGGELQRVAIAAALARDA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 42741659 1195 HILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLS 1235
Cdd:cd03236  159 DFYFFDEPSSYLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1049-1263 5.28e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.95  E-value: 5.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAhlgIVSQE------PIL 1122
Cdd:PRK10938   15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDEwqrnntDML 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1123 fdcSIAENiAYGDNSRVVSQEEIVRAAKEANIHAF--IESL---PNKYstkvgdkgtqLSGGQKQRIAIARALVRQPHIL 1197
Cdd:PRK10938   92 ---SPGED-DTGRTTAEIIQDEVKDPARCEQLAQQfgITALldrRFKY----------LSTGETRKTLLCQALMSEPDLL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1198 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK10938  158 ILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
403-564 7.64e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.47  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   403 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN-VRFlreiIGVVSQEPVLFA 481
Cdd:PRK13543   20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRF----MAYLGHLPGLKA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIA-ENIRY-----GRENVTMdeiekavkEANAYDfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLD 555
Cdd:PRK13543   96 DLSTlENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162

                  ....*....
gi 42741659   556 EATSALDTE 564
Cdd:PRK13543  163 EPYANLDLE 171
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1049-1241 7.92e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.56  E-value: 7.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE----RFYdplAGKVLLDGK---------EIKRlnvqwlraHLGI 1115
Cdd:PRK10938  272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGRrrgsgetiwDIKK--------HIGY 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1116 VS-------------QEPIL---FDcSIAENIAYGDNSRVVSQEEIVRAAkeanihafieslpnkYSTKVGDKGTQ-LSG 1178
Cdd:PRK10938  341 VSsslhldyrvstsvRNVILsgfFD-SIGIYQAVSDRQQKLAQQWLDILG---------------IDKRTADAPFHsLSW 404
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659  1179 GQkQRIA-IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLSTIQNAD 1241
Cdd:PRK10938  405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGD 480
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1046-1207 8.27e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.60  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1046 TRPDIPVLQ----------GLSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPLAGKVLLDGKEIKRLNVQwLRAH 1112
Cdd:PRK15439  262 QAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLA 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1113 LGIV-----SQEPILF-DCSIAENI---AYGDNSRvvsqeeIVRAAKEANI-HAFIESLPNKYSTKVGDKGTqLSGGQKQ 1182
Cdd:PRK15439  338 RGLVylpedRQSSGLYlDAPLAWNVcalTHNRRGF------WIKPARENAVlERYRRALNIKFNHAEQAART-LSGGNQQ 410
                         170       180
                  ....*....|....*....|....*
gi 42741659  1183 RIAIARALVRQPHILLLDEATSALD 1207
Cdd:PRK15439  411 KVLIAKCLEASPQLLIVDEPTRGVD 435
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
392-621 8.66e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.44  E-value: 8.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSvdgqdiRTINVRflreiIG 471
Cdd:PRK15064  320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------WSENAN-----IG 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 VVSQEPVL-FATTIA---------------ENIR--YGRENVTMDEIEKAVKeanaydfimklphkfdtlvgergaQLSG 533
Cdd:PRK15064  386 YYAQDHAYdFENDLTlfdwmsqwrqegddeQAVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   534 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKArKGrTTIVIAH------RLSTvrnaDVIAGFDDGVIV 607
Cdd:PRK15064  442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
                         250
                  ....*....|....
gi 42741659   608 EKGNHDELMKEKGI 621
Cdd:PRK15064  516 FSGTYEEYLRSQGI 529
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
383-607 9.43e-08

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 56.37  E-value: 9.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    383 HKPDNIKGN-LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT-EGMVSVDGQ--DI 458
Cdd:TIGR02633  248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    459 RT---------INVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLvgergA 529
Cdd:TIGR02633  328 RNpaqairagiAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----G 402
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42741659    530 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVrnadviAGFDDGVIV 607
Cdd:TIGR02633  403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYeIYKLINQLAQEGVAIIVVSSELAEV------LGLSDRVLV 475
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1038-1219 1.12e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 56.11  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1038 GEVVF-----NYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrLNVQWL--- 1109
Cdd:PRK11147  316 GKIVFemenvNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqh 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1110 RAHLgivsqEPilfDCSIAENIAYGdnsrvvSQEEIVRAAKEaniHA------FIESlPNKYSTKVgdkgTQLSGGQKQR 1183
Cdd:PRK11147  391 RAEL-----DP---EKTVMDNLAEG------KQEVMVNGRPR---HVlgylqdFLFH-PKRAMTPV----KALSGGERNR 448
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 42741659  1184 IAIARALVRQPHILLLDEATSALDTESEKVVQEALD 1219
Cdd:PRK11147  449 LLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1053-1256 1.30e-07

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 54.34  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1053 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKrLNVQWLRAHL-GIVSQepILFDCS 1126
Cdd:cd03237   10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYeGTVRD--LLSSIT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1127 iaeNIAYGDNSrvvSQEEIVRAAKeanihafIESLpnkYSTKVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1206
Cdd:cd03237   87 ---KDFYTHPY---FKTEIAKPLQ-------IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1207 DTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVFQnGRVKEHGT 1256
Cdd:cd03237  147 DVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1035-1256 1.32e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 55.95  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1035 VTFGEVVFNYPtrpDIPV-LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEI-KRLNV- 1106
Cdd:COG1245  335 EKEEETLVEYP---DLTKsYGGFSLEVeggeiREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIs 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1107 ---QWLRAHLGIVSQEpILFDcSIAENIaygDNSRVvsQEEIVRAAKeanihafIESLPNKYstkVGDkgtqLSGGQKQR 1183
Cdd:COG1245  405 ykpQYISPDYDGTVEE-FLRS-ANTDDF---GSSYY--KTEIIKPLG-------LEKLLDKN---VKD----LSGGELQR 463
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1184 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFqNGRVKEHGT 1256
Cdd:COG1245  464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVF-EGEPGVHGH 538
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
488-615 1.51e-07

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 56.17  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    488 IRYGRENVTmDEIEKAVKEAnaYDFIMKLP---HKFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKIL 552
Cdd:TIGR00630  778 VKYKGKNIA-DVLDMTVEEA--YEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659    553 LLDEATSALDTESEA----VVQVALDKarkGRTTIVIAHRLSTVRNADVI------AGFDDGVIVEKGNHDEL 615
Cdd:TIGR00630  855 ILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
PLN03073 PLN03073
ABC transporter F family; Provisional
1035-1258 2.11e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 55.25  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1035 VTFGEVVFNYPTRPDIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeiKRLNVqWLRAHL- 1113
Cdd:PLN03073  509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--VRMAV-FSQHHVd 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1114 GI-VSQEPILFdcsiaeniaygdnsrvvsQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTqLSGGQKQRIAIARALVR 1192
Cdd:PLN03073  584 GLdLSSNPLLY------------------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKITFK 644
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1193 QPHILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVFQNGRVKE-HGTHQ 1258
Cdd:PLN03073  645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
1051-1266 2.45e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 54.90  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEIKrlnvqWL-RAHLGIVSQEP--------I 1121
Cdd:PRK15064  333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVK-----WSeNANIGYYAQDHaydfendlT 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1122 LFDCsIAENIAYGDNSRVV---------SQEEIvraakeanihafieslpnKYSTKVgdkgtqLSGGQKQRIAIARALVR 1192
Cdd:PRK15064  401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDI------------------KKSVKV------LSGGEKGRMLFGKLMMQ 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1193 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVFQNGRVKEHGTHQQLLAQKGI 1266
Cdd:PRK15064  456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
708-870 2.58e-07

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 54.02  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  708 WPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKrqnsNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKR 787
Cdd:cd18540    1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGL----TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  788 LRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPI 867
Cdd:cd18540   77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154

                 ...
gi 42741659  868 IAI 870
Cdd:cd18540  155 LAV 157
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
753-870 2.66e-07

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 53.63  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  753 NLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSR 832
Cdd:cd18545   40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNG 117
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 42741659  833 LAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 870
Cdd:cd18545  118 LINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1051-1262 2.81e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 54.62  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1051 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHlGIV------SQEPILFD 1124
Cdd:PRK10762  266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1125 CSIAENI---AYGDNSRVVSQeeIVRAAKEANIHAFIESLPNKYSTKVGDKGtQLSGGQKQRIAIARALVRQPHILLLDE 1201
Cdd:PRK10762  345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDE 421
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1202 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLLA 1262
Cdd:PRK10762  422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1174-1210 3.24e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 54.74  E-value: 3.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 42741659  1174 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:PRK11819  162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1052-1218 3.62e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.41  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1052 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdGKEIKrlnvqwlrahLGIVSQEPILF---DCSIA 1128
Cdd:PRK10636  327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK----------LGYFAQHQLEFlraDESPL 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1129 ENIAygdnsRVVSQEeivraaKEANIHAFIESLPNKySTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1208
Cdd:PRK10636  396 QHLA-----RLAPQE------LEQKLRDYLGGFGFQ-GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
                         170
                  ....*....|
gi 42741659  1209 ESEKVVQEAL 1218
Cdd:PRK10636  464 DMRQALTEAL 473
PLN03073 PLN03073
ABC transporter F family; Provisional
385-570 5.16e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.10  E-value: 5.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   385 PDNIKGN--LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVsvdgqdIRTIN 462
Cdd:PLN03073  500 PDDRPGPpiISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK 571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   463 VRflreiIGVVSQEPVLFATTIAENIRYgrenvtMDEIEKAVKEanaydfiMKLPHKFDT--LVGERGAQ----LSGGQK 536
Cdd:PLN03073  572 VR-----MAVFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQK 633
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 42741659   537 QRIAIARALVRNPKILLLDEATSALDTES-EAVVQ 570
Cdd:PLN03073  634 SRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1045-1263 5.43e-07

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 53.17  E-value: 5.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1045 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRaHLGIV----SQep 1120
Cdd:COG4586   30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1121 ILFDCSIAENIA-----YGdnsrvVSQEEIvraakEANIHAFIESLpnkystKVGDKGT----QLSGGQKQRIAIARALV 1191
Cdd:COG4586  107 LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELL------DLGELLDtpvrQLSLGQRMRCELAAALL 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1192 RQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:COG4586  171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
427-562 6.03e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.98  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   427 GNSGCGKSTTVQLMQRLYDPTEGMV-----SVDGQDIRTinvrflREIIGVVSQEPVLfattiaenirYG----REN--- 494
Cdd:NF033858  299 GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT------RRRVGYMSQAFSL----------YGeltvRQNlel 362
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659   495 ------VTMDEIEKAVKEanaydfimkLPHKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:NF033858  363 harlfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1168-1244 6.37e-07

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 53.86  E-value: 6.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1168 KVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEALDKareGRTCIVIAHRLSTIQNA 1240
Cdd:TIGR00630  822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTA 898

                   ....
gi 42741659   1241 DLIV 1244
Cdd:TIGR00630  899 DYII 902
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1174-1210 7.32e-07

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 53.40  E-value: 7.32e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 42741659   1174 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1210
Cdd:TIGR03719  160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1175-1246 1.42e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.48  E-value: 1.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659 1175 QLSGGQKQRIAIARALVRQPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVF 1246
Cdd:COG1245  212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1060-1232 1.71e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.48  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1060 VKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlnvQWlraHLGIVSQEPILFDCSIAENIAYGDnsRV 1139
Cdd:PRK10636   24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGD--RE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1140 VSQ-EEIVRAAKEAN--------------IHAF-IESLPNKYSTKVGDKGTQL-------SGGQKQRIAIARALVRQPHI 1196
Cdd:PRK10636   91 YRQlEAQLHDANERNdghaiatihgkldaIDAWtIRSRAASLLHGLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDL 170
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 42741659  1197 LLLDEATSALDTESEKVVQEALdKAREGrTCIVIAH 1232
Cdd:PRK10636  171 LLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
530-591 1.88e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.09  E-value: 1.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  530 QLSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLST 591
Cdd:COG1245  212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
217-343 2.11e-06

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 350052 [Multi-domain]  Cd Length: 294  Bit Score: 51.01  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  217 VILAISP-----VLGLSAAVWAKILSSF------TDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAK 285
Cdd:cd18779  135 LLFAQSPllglvVLGLAALQVALLLATRrrvrelMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQL 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  286 RIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF 343
Cdd:cd18779  215 NASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA--LNALAGAF 270
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
1060-1250 2.60e-06

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 52.03  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1060 VKKGQTLALVGSSGCGKSTVVQLL----ERFYDPLAGKVLLDG---KEIKRlnvqWLRAHLGIVSQEPILF-DCSIAENI 1131
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKK----HYRGDVVYNAETDVHFpHLTVGETL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1132 AY-----GDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGD---KGtqLSGGQKQRIAIARALVRQPHILLLDEAT 1203
Cdd:TIGR00956  160 DFaarckTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNAT 237
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   1204 SALDTESekvvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVFQNGR 1250
Cdd:TIGR00956  238 RGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
108-231 3.36e-06

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 50.54  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  108 EEDMTRYAYYYSGIGAGVLVAAYIQVSFWC---LAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE 184
Cdd:cd18604   39 EVSVLYYLGIYALISLLSVLLGTLRYLLFFfgsLRASRKLHE---RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDS 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659  185 GIGDKIGMFFQSMATFFTGFIvgftrgwkltlVILAISPVLGLSAAV 231
Cdd:cd18604  116 ELADSLSSLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
PLN03073 PLN03073
ABC transporter F family; Provisional
420-666 3.56e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.40  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   420 GQTVALVGNSGCGKSTTVQLM------------QRLY-------DPTEGMVSVDGQDIRtiNVRFLREIIGVVSQEPVLF 480
Cdd:PLN03073  203 GRHYGLVGRNGTGKTTFLRYMamhaidgipkncQILHveqevvgDDTTALQCVLNTDIE--RTQLLEEEAQLVAQQRELE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   481 ATTIAENIRyGRENVTMD---------EIEKAVKEANAY-------------DFIMKLPHKfdtlvgeRGAQLSGGQKQR 538
Cdd:PLN03073  281 FETETGKGK-GANKDGVDkdavsqrleEIYKRLELIDAYtaearaasilaglSFTPEMQVK-------ATKTFSGGWRMR 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   539 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKgrTTIVIAHR---LSTVRnADVIAGFDDGVIVEKGNHDEl 615
Cdd:PLN03073  353 IALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHArefLNTVV-TDILHLHGQKLVTYKGDYDT- 428
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42741659   616 mkekgiyFKLVTMQTAGNEVELENAADESKSEIDAL--EMSSNDSRSSLIRKR 666
Cdd:PLN03073  429 -------FERTREEQLKNQQKAFESNERSRSHMQAFidKFRYNAKRASLVQSR 474
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
1045-1207 3.57e-06

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 49.18  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1045 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPlAGKVLLDGKEIKRLNVQWlRAHLGIVSQEp 1120
Cdd:cd03233   15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659 1121 ilfDCSIAEniaygdnsrvVSQEEIVRAAKEANIHAFIeslpnkystkvgdKGtqLSGGQKQRIAIARALVRQPHILLLD 1200
Cdd:cd03233   92 ---DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWD 143

                 ....*..
gi 42741659 1201 EATSALD 1207
Cdd:cd03233  144 NSTRGLD 150
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
488-598 4.00e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 51.75  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   488 IRYGRENVTmDEIEKAVKEANayDFIMKLPH---KFDTL---------VGERGAQLSGGQKQRIAIARAL---VRNPKIL 552
Cdd:PRK00635  758 VRYKGKNIA-DILEMTAYEAE--KFFLDEPSiheKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLY 834
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 42741659   553 LLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVI 598
Cdd:PRK00635  835 VLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
410-645 4.71e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 49.81  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ-DIRTINVRFLREIIGVvsqepvlfattiaENI 488
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI-------------ENI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   489 RYGR--ENVTMDEIEKAVKEANAY----DFIMKLPHKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:PRK13546  107 EFKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   563 tesEAVVQVALDK----ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVEL 637
Cdd:PRK13546  176 ---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKEF 252

                  ....*...
gi 42741659   638 ENAADESK 645
Cdd:PRK13546  253 RNKLDESR 260
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
1176-1246 5.04e-06

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 48.09  E-value: 5.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659 1176 LSGGQKQRIAIARALVRQPH--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVF 1246
Cdd:cd03238   88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDF 161
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
417-587 5.10e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 50.94  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   417 VQSGQTVALVGNSGCGKSTTVQLMQrlydpteGMVSVDGQDIRTINVRFLreiiGVVSQE-PVLFATTIAENIRYGREnv 495
Cdd:PRK10636   24 INPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPGNWQL----AWVNQEtPALPQPALEYVIDGDRE-- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   496 tMDEIEKAVKEANAYD---FIMKLPHKFDTL----VGERGAQL------------------SGGQKQRIAIARALVRNPK 550
Cdd:PRK10636   91 -YRQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSD 169
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 42741659   551 ILLLDEATSALDTesEAVVQvaLDKARKGR--TTIVIAH 587
Cdd:PRK10636  170 LLLLDEPTNHLDL--DAVIW--LEKWLKSYqgTLILISH 204
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
392-562 5.99e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 50.31  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-PTEGMVSVDGQDIRTINVR-FLREI 469
Cdd:PRK13549  260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQG 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   470 IGVVSQE-------PVLfatTIAENI------RYGRENVtmdeIEKAVKEANAYDFIMKLPHKFDTLVgERGAQLSGGQK 536
Cdd:PRK13549  340 IAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQ 411
                         170       180
                  ....*....|....*....|....*.
gi 42741659   537 QRIAIARALVRNPKILLLDEATSALD 562
Cdd:PRK13549  412 QKAVLAKCLLLNPKILILDEPTRGID 437
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
407-587 6.21e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.58  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   407 VKILKGLNLKVQSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDgqdirtINVRFLREIIGVVSQEPV-LF 480
Cdd:PRK13409  347 TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKPDYDGTVeDL 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   481 ATTIAENIRygrENVTMDEIEKAvkeanaydfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK13409  421 LRSITDDLG---SSYYKSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 483
                         170       180
                  ....*....|....*....|....*....
gi 42741659   561 LDTESEAVVQVALDK--ARKGRTTIVIAH 587
Cdd:PRK13409  484 LDVEQRLAVAKAIRRiaEEREATALVVDH 512
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1060-1245 6.26e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.58  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1060 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydplAGKVLLDgkEIKRLNVQWLRAHLGI--V 1116
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1117 SQEPILFDCSIAENIAYGDNSRVVsqEEIVraaKEANIhafieslpnkysTKVGDKG-TQLSGGQKQRIAIARALVRQPH 1195
Cdd:PRK13409  170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGL------------ENILDRDiSELSGGELQRVAIAAALLRDAD 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  1196 ILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVV 1245
Cdd:PRK13409  233 FYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHI 283
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
145-330 8.13e-06

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 49.12  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  145 HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEgigdkigmFF--QSMATF------FTGFIVGFTRGWKLTL 216
Cdd:cd18566   75 HRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpfvLIFLGLIWYLGGKLVL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  217 VILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITAN 296
Cdd:cd18566  146 VPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINA 225
                        170       180       190
                 ....*....|....*....|....*....|....
gi 42741659  297 ISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQ 330
Cdd:cd18566  226 VAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGA 259
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
404-562 8.39e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 50.00  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   404 RKEVKILKG-----LNLKVQSGQTVALVGNSGCGKSttvQLMQRLYDP---TEGMVSVDGQDIRTINVR-FLREIIGVVS 474
Cdd:PRK10762  257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRT---ELMKVLYGAlprTSGYVTLDGHEVVTRSPQdGLANGIVYIS 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   475 QEP----VLFATTIAEN---------------IRYGRENVTMDeiekavkeanayDFIM----KLPHKfDTLVGErgaqL 531
Cdd:PRK10762  334 EDRkrdgLVLGMSVKENmsltalryfsraggsLKHADEQQAVS------------DFIRlfniKTPSM-EQAIGL----L 396
                         170       180       190
                  ....*....|....*....|....*....|.
gi 42741659   532 SGGQKQRIAIARALVRNPKILLLDEATSALD 562
Cdd:PRK10762  397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
711-978 9.81e-06

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 48.99  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  711 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTriddPEtkrQNSNLFSLLFLALGIISFITFFLQgFTFGKAGEILTKR--- 787
Cdd:cd18549    4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLL----PS---KNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARiet 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  788 -LRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVkgaigSRLA-------VITqnIANLGTGIIISFIYGWQLTL 859
Cdd:cd18549   76 dMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  860 LLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTQE----QKFEhmyaqSLQVPYRNSL 932
Cdd:cd18549  147 IVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEINAQLEDSLsgiRVVKAFANEeyeiEKFD-----EGNDRFLESK 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659  933 RKAH-IFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDvLLVF 978
Cdd:cd18549  219 KKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGD-LVAF 264
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
1070-1243 9.83e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.94  E-value: 9.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1070 GSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAhlgIVSQEPILFDCSIAENIAYGdnSRVVSQEEIVRAA 1149
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1150 keanIHAFieslpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREGRTCI 1228
Cdd:PRK13541  108 ----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
                         170
                  ....*....|....*
gi 42741659  1229 VIAHRLSTIQNADLI 1243
Cdd:PRK13541  178 LSSHLESSIKSAQIL 192
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
406-620 1.00e-05

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   406 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVqLMQRLYDPTEGMvsvdgQDIR----TINVRFLREIIGVvsQEPVLFA 481
Cdd:NF000106   25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRf*twCANRRALRRTIG*--HRPVR*G 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   482 TTIAENiryGRENVTM--DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 559
Cdd:NF000106   97 RRESFS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42741659   560 ALD--TESEAVVQVAlDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 620
Cdd:NF000106  174 GLDprTRNEVWDEVR-SMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1049-1236 1.21e-05

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 49.55  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1049 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdGKEIKRLNVQWLRAHLgivsqEPilfDCSIA 1128
Cdd:TIGR03719  334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL-----DP---NKTVW 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   1129 ENIAYGdnsrvvsQEEIVRAAKEANIHAFIESLPNKYS---TKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1205
Cdd:TIGR03719  405 EEISGG-------LDIIKLGKREIPSRAYVGRFNFKGSdqqKKVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 42741659   1206 LDTESEKVVQEALDKAreGRTCIVIAH------RLST 1236
Cdd:TIGR03719  474 LDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
GguA NF040905
sugar ABC transporter ATP-binding protein;
1034-1230 1.61e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1034 NVTFGEVVF-------NYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-LAGKVLLDGKEIKRL 1104
Cdd:NF040905  250 TPKIGEVVFevknwtvYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVS 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1105 NVQWL-----------RAHLGIVSQEPILFDCSIA--ENIAygdNSRVVSQEEIVRAAKEanihaFIESLPNKYSTkVGD 1171
Cdd:NF040905  330 TVSDAidaglayvtedRKGYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKMNIKTPS-VFQ 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42741659  1172 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1230
Cdd:NF040905  401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
392-598 1.77e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.17  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   392 LEFRNVHFSYpsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTInvrflreiig 471
Cdd:PRK13541    2 LSLHQLQFNI----EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   472 vvsQEPvlFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPH--KFDTLVGERGAQLSGGQKQRIAIARALVRNP 549
Cdd:PRK13541   68 ---AKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 42741659   550 KILLLDEATSALDTESEAVV-QVALDKARKGRTTIVIAHRLSTVRNADVI 598
Cdd:PRK13541  143 DLWLLDEVETNLSKENRDLLnNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
395-587 1.87e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.01  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  395 RNVHFSYPSRkeVKILKGLNLKVQSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPTEGmvSVDG--------QDIRT- 460
Cdd:COG1245  338 EETLVEYPDL--TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEdlkisykpQYISPd 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  461 --INVR-FLREIIGVVsqepvlFATTIAENirygrenvtmdEIEKAvkeanaydfiMKLPHKFDTLVGErgaqLSGGQKQ 537
Cdd:COG1245  414 ydGTVEeFLRSANTDD------FGSSYYKT-----------EIIKP----------LGLEKLLDKNVKD----LSGGELQ 462
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 42741659  538 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-AR-KGRTTIVIAH 587
Cdd:COG1245  463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfAEnRGKTAMVVDH 514
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
1176-1247 2.02e-05

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.41  E-value: 2.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1176 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQ 1247
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
758-870 2.20e-05

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 47.85  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  758 LFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpknTT--GALTTRLANDAAQVKGAIGSRLAV 835
Cdd:cd18606   40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD----TTplGRILNRFSKDTDVLDNELPDSLRM 115
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 42741659  836 ITQNIANLGTGIIISFIYgwqLTLLLLAIVPIIAI 870
Cdd:cd18606  116 FLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
417-589 3.31e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.27  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   417 VQSGQTVALVGNSGCGKSTTV-----QLMQRLYDPTEGmVSVDgqdirtinvRFLREIIGVVSQEpvLFATTIAENIRYG 491
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVkilsgELIPNLGDYEEE-PSWD---------EVLKRFRGTELQN--YFKKLYNGEIKVV 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   492 RENVTMDEIEKAVKeANAYDFIMKLPH--KFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK13409  164 HKPQYVDLIPKVFK-GKVRELLKKVDErgKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
                         170       180
                  ....*....|....*....|....*....
gi 42741659   561 LDTESEAVVQVALDKARKGRTTIVIAHRL 589
Cdd:PRK13409  243 LDIRQRLNVARLIRELAEGKYVLVVEHDL 271
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
169-336 3.96e-05

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350005 [Multi-domain]  Cd Length: 289  Bit Score: 46.89  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  169 GELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYA 248
Cdd:cd18561   93 GELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYG 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  249 KAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSI 328
Cdd:cd18561  173 RLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTL 252

                 ....*...
gi 42741659  329 GQVLTVFF 336
Cdd:cd18561  253 SSLLLILF 260
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
530-601 4.25e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 45.43  E-value: 4.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  530 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGF 601
Cdd:cd03227   77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
715-971 6.49e-05

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 46.43  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  715 VFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETkrqnsnLFSLLFLALGIISFITFF--LQGFTFGKAGEILTKRLRYMV 792
Cdd:cd18782    8 LALSFVVQLLGLANPLLFQVIIDKVLVQQDLAT------LYVIGVVMLVAALLEAVLtaLRTYLFTDTANRIDLELGGTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  793 FRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKG-AIGSRLAVITQNIANLGTgIIISFIYGWQLTLLLLAIVPIIAIA 871
Cdd:cd18782   82 IDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  872 GVVEMKMLSGQaLKDKKELEGSGKIA-TEAIENFRTVVSLTQE----QKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQ 946
Cdd:cd18782  158 TFLFGPILRRQ-IRRRAEASAKTQSYlVESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
                        250       260
                 ....*....|....*....|....*
gi 42741659  947 ammyFSYAGCFRFGAYLVAHKLMSF 971
Cdd:cd18782  237 ----LSSLLVLWVGAYLVLRGELTL 257
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
731-971 7.31e-05

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 46.35  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  731 IFSKIIGVFTR--IDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDd 806
Cdd:cd18555   16 LLTLLIPILTQyvIDNviVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  807 pKNTTGALTTRlANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKD 886
Cdd:cd18555   95 -NRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKK---LN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  887 KKELEGSGK---IATEAIENFRTVVSLTQEQKF----EHMYAQSLQVpyrnSLRKAHIFGITFSFTQAMMYFSYAGCFRF 959
Cdd:cd18555  170 QEEIVAQTKvqsYLTETLYGIETIKSLGSEKNIykkwENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLILWI 245
                        250
                 ....*....|..
gi 42741659  960 GAYLVAHKLMSF 971
Cdd:cd18555  246 GAYLVINGELTL 257
uvrA PRK00349
excinuclease ABC subunit UvrA;
1168-1244 7.55e-05

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 47.37  E-value: 7.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1168 KVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1240
Cdd:PRK00349  823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899

                  ....
gi 42741659  1241 DLIV 1244
Cdd:PRK00349  900 DWII 903
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
376-619 7.80e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 46.70  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   376 DSYSKSGHKPDNIKGN--LEFRNVhfsypSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSttvQLMQRLY--DP-TEGM 450
Cdd:PRK09700  248 NRFNAMKENVSNLAHEtvFEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKrAGGE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   451 VSVDGQDIRTIN-VRFLREIIGVVSQ---EPVLFAT-TIAENI------RYGRENVTM----DEIEKAVKEANAYDFIMK 515
Cdd:PRK09700  320 IRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLALK 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   516 LpHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN 594
Cdd:PRK09700  400 C-HSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIIT 474
                         250       260
                  ....*....|....*....|....*..
gi 42741659   595 A-DVIAGFDDGVIVEK-GNHDELMKEK 619
Cdd:PRK09700  475 VcDRIAVFCEGRLTQIlTNRDDMSEEE 501
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
750-970 8.36e-05

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 46.01  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  750 QNSNLFSLLFLALGIISF-------ITFFLQGFTFGKAGEILTKRLrymvFRSMLRQDVSWFDdpKNTTGALTTRLA-ND 821
Cdd:cd18568   36 KNISLLNLILIGLLIVGIfqillsaVRQYLLDYFANRIDLSLLSDF----YKHLLSLPLSFFA--SRKVGDIITRFQeNQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  822 AAQ---VKGAIGSRLAVITQNIAnlgtgIIISFIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGSgk 895
Cdd:cd18568  110 KIRrflTRSALTTILDLLMVFIY-----LGLMFYYNLQLTLIVLAFIPLYVLLTLLsspKLKRNSREIFQANAEQQSF-- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  896 iATEAIENFRTVVSLTQEQKF----EHMYAQSLQVPYRNSlrkahIFGITFSFT-QAMMYFSYAGCFRFGAYLVAHKLMS 970
Cdd:cd18568  183 -LVEALTGIATIKALAAERPIrwrwENKFAKALNTRFRGQ-----KLSIVLQLIsSLINHLGTIAVLWYGAYLVISGQLT 256
PLN03073 PLN03073
ABC transporter F family; Provisional
1175-1232 1.03e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.78  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42741659  1175 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH 1232
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
531-586 1.03e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.26  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659   531 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIA 586
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
151-337 1.29e-04

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 45.53  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  151 FFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGIGDK-IGMFFQSMATFFTgFIVGFTRGWKLTLVILAISPVLGLSA 229
Cdd:cd18567   81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGfVEALLDGLMAILT-LVMMFLYSPKLALIVLAAVALYALLR 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  230 AVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAItANISIGAAF-LLIYA 308
Cdd:cd18567  159 LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQR-LQILFSAANgLLFGL 237
                        170       180
                 ....*....|....*....|....*....
gi 42741659  309 SYALAFWYGTTLVLSGEYSIGqVLTVFFS 337
Cdd:cd18567  238 ENILVIYLGALLVLDGEFTVG-MLFAFLA 265
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
410-610 1.55e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.85  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  410 LKGLNLKVQSGQTVALVGNSGCGKSTTVQlmQRLYDPTEGMVSVDGQdirtinvRFLREIIGVVSQepvlFATTIAENIR 489
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLP-------KFSRNKLIFIDQ----LQFLIDVGLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  490 YgrenvtmdeiekavkeanaydfiMKLPHKFDTLvgergaqlSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEA 567
Cdd:cd03238   78 Y-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42741659  568 VVQVALDKAR-KGRTTIVIAHRLSTVRNADVI------AGFDDGVIVEKG 610
Cdd:cd03238  127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
417-589 1.65e-04

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 43.71  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  417 VQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEgmvsvdgqdirtinvrflreiigvvsqepvlfattiaenirygrENVT 496
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG--------------------------------------------DNDE 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  497 MDEIEKAVKeanaydfimklPHKFDtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK- 575
Cdd:cd03222   58 WDGITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRl 117
                        170
                 ....*....|....*
gi 42741659  576 -ARKGRTTIVIAHRL 589
Cdd:cd03222  118 sEEGKKTALVVEHDL 132
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1170-1265 2.92e-04

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 44.73  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1170 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQ 1247
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
                          90
                  ....*....|....*...
gi 42741659  1248 NGRVKEHGTHQQLLAQKG 1265
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1175-1262 4.23e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 44.02  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1175 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1251
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
                          90
                  ....*....|.
gi 42741659  1252 KEHGTHQQLLA 1262
Cdd:PRK15093  238 VETAPSKELVT 248
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
392-591 6.66e-04

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 43.77  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    392 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdGQDIRTINVRFLREIIg 471
Cdd:TIGR03719  323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659    472 vvsqEPvlfATTIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPHKF---DTLVGergaQLSGGQKQRIAIARALVRN 548
Cdd:TIGR03719  398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPSRAYVGRFNFKGsdqQKKVG----QLSGGERNRVHLAKTLKSG 461
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 42741659    549 PKILLLDEATSALDTESEAVVQVALDKArkGRTTIVIAH------RLST 591
Cdd:TIGR03719  462 GNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
PLN03140 PLN03140
ABC transporter G family member; Provisional
1140-1235 6.80e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.07  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1140 VSQEEIVRAAKEANIHAFIESLPNKYstkVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL 1218
Cdd:PLN03140  986 VSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
                          90
                  ....*....|....*...
gi 42741659  1219 -DKAREGRTCIVIAHRLS 1235
Cdd:PLN03140 1063 rNTVDTGRTVVCTIHQPS 1080
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
414-618 8.68e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.46  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   414 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIigvVSQEpvlfattiaenirYGRE 493
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDE-------------WQRN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   494 NVTM---DE----------IEKAVKEANAYDFIMKLPHkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 560
Cdd:PRK10938   87 NTDMlspGEddtgrttaeiIQDEVKDPARCEQLAQQFG-ITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   561 LDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKE 618
Cdd:PRK10938  166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
373-596 9.06e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.46  E-value: 9.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   373 PSIDSYSKSGHKPDNIKgNLEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRlyDPTEGMvS 452
Cdd:PRK10938  243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGY-S 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   453 VD----------GQDIRTInvrflREIIGVVSQEPVL---FATTIAENIRYGrenvTMDEI--EKAVKEANaydfiMKLP 517
Cdd:PRK10938  316 NDltlfgrrrgsGETIWDI-----KKHIGYVSSSLHLdyrVSTSVRNVILSG----FFDSIgiYQAVSDRQ-----QKLA 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   518 HKFDTLVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIV---- 584
Cdd:PRK10938  382 QQWLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvsh 460
                         250       260
                  ....*....|....*....|
gi 42741659   585 --------IAHRLSTVRNAD 596
Cdd:PRK10938  461 haedapacITHRLEFVPDGD 480
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
413-606 9.09e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.50  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   413 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRfLREIIGVV-----SQEPVLF------- 480
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYldaplaw 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   481 -ATTIAEN-----IRYGRENVTMDEIEKAVKeanaydfiMKLPHKfDTLVGergaQLSGGQKQRIAIARALVRNPKILLL 554
Cdd:PRK15439  361 nVCALTHNrrgfwIKPARENAVLERYRRALN--------IKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLLIV 427
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 42741659   555 DEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 606
Cdd:PRK15439  428 DEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1174-1244 1.08e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 43.48  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1174 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1244
Cdd:COG0178  825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1175-1244 1.30e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 40.81  E-value: 1.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42741659 1175 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1244
Cdd:cd03227   77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
99-345 1.52e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 42.13  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   99 NDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQ-VSFW--CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRL 175
Cdd:cd18605   29 SNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRaFLFAygGLRAARRLHN---KLLSSILFAKMSFFDKTPVGRILNRF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  176 TDDVSKINEGIGDKIGMFFQSMATFFtGFIVGFTRGWKLTLVILAISPVLG----------------LSAAVWAKILSSF 239
Cdd:cd18605  106 SSDVYTIDDSLPFILNILLAQLFGLL-GYLVVICYQLPWLLLLLLPLAFIYyriqryyratsrelkrLNSVNLSPLYTHF 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  240 TdkellayakagavaeEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGikkaitanisigaaflliYASYALAFWYGTT 319
Cdd:cd18605  185 S---------------ETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQ------------------LASQAASQWLSIR 231
                        250       260
                 ....*....|....*....|....*.
gi 42741659  320 LVLSGeysigqVLTVFFSVLIGAFSV 345
Cdd:cd18605  232 LQLLG------VLIVTFVALTAVVQH 251
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1089-1273 1.58e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1089 PLAGKVLLDGKeikrlnvqwlraHLGIVSQEPIlfdcsiaENIAygdnsRVVSQEEIVRAAKEANIHAFIESLPnkystk 1168
Cdd:PRK00635 1643 PLAQEVVYEGK------------HFGQLLQTPI-------EEVA-----ETFPFLKKIQKPLQALIDNGLGYLP------ 1692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1169 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1244
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
                         170       180       190
                  ....*....|....*....|....*....|..
gi 42741659  1245 VFQNGRVKEHGthqQLL---AQKGIYFSMVSV 1273
Cdd:PRK00635 1773 EMGPGSGKTGG---KILfsgPPKDISASKDSL 1801
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
847-964 1.65e-03

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 42.10  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  847 IIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLsgQALKDKKELEGSGKIA--TEAIENFRTVVSLTQEQKFEHMYAQSL 924
Cdd:cd18588  133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL--RRRLEEKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELL 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 42741659  925 QVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLV 964
Cdd:cd18588  211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
754-874 2.20e-03

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 41.68  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  754 LFSLLFLALGIISFITFFLQGFtfgKAGEILTKRLRYMVFRSMLRqdvsWFDdpKNTTGALTTRLANDAaqvkGAIGSRL 833
Cdd:cd18604   51 LISLLSVLLGTLRYLLFFFGSL---RASRKLHERLLHSVLRAPLR----WLD--TTPVGRILNRFSKDI----ETIDSEL 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 42741659  834 AVITQNIANLGTGIIISFIygwqltlLLLAIVPIIAIAGVV 874
Cdd:cd18604  118 ADSLSSLLESTLSLLVILI-------AIVVVSPAFLLPAVV 151
PRK01889 PRK01889
GTPase RsgA; Reviewed
1048-1083 2.83e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.46  E-value: 2.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 42741659  1048 PDIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1083
Cdd:PRK01889  170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
530-616 3.07e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 41.33  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   530 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVI 606
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
                          90
                  ....*....|
gi 42741659   607 VEKGNHDELM 616
Cdd:PRK15093  238 VETAPSKELV 247
uvrA PRK00349
excinuclease ABC subunit UvrA;
509-598 3.09e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   509 AYDF---IMKLPHKFDTLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA----VV 569
Cdd:PRK00349  797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRklleVL 876
                          90       100
                  ....*....|....*....|....*....
gi 42741659   570 QVALDKarkGRTTIVIAHRLSTVRNADVI 598
Cdd:PRK00349  877 HRLVDK---GNTVVVIEHNLDVIKTADWI 902
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
130-336 3.45e-03

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 40.87  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  130 YIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFT 209
Cdd:cd18554   64 YYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  210 RGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGI 289
Cdd:cd18554  144 LNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRAL 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42741659  290 KKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFF 336
Cdd:cd18554  224 KHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGT-LVAFV 269
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
847-970 3.46e-03

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.


Pssm-ID: 350031  Cd Length: 293  Bit Score: 40.88  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  847 IIISFIyGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKdkkelEGSGKIAT--EAIENFRTVVSLTQEQKFEHMYA 921
Cdd:cd18587  133 AVIALI-GGPLALVPLVAIPLVLLYGLLlqkPLRRLVEESMR-----ESAQKNALlvESLSGLETIKALGAEGRMQRRWE 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 42741659  922 QSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMS 970
Cdd:cd18587  207 EAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELT 255
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
1053-1263 3.56e-03

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 40.95  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1053 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlNVQWLRAHLGIVSQepilfdCSIAENIA 1132
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQ------LTGIENIE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1133 YGDNSRVVSQEEIVRAAKE----ANIHAFIESLPNKYSTkvgdkgtqlsgGQKQRIAIARALVRQPHILLLDEATSALDt 1208
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKYSS-----------GMRAKLGFSINITVNPDILVIDEALSVGD- 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  1209 esEKVVQEALDKARE----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1263
Cdd:PRK13546  176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
534-616 4.03e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.42  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659   534 GQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqvaldKARKGrTTIVIAH-R--LSTV--RNADViagfDDG 604
Cdd:PRK15064  159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTirwlEDVL-----NERNS-TMIIISHdRhfLNSVctHMADL----DYG 228
                          90
                  ....*....|...
gi 42741659   605 VI-VEKGNHDELM 616
Cdd:PRK15064  229 ELrVYPGNYDEYM 241
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
523-598 4.37e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 39.90  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  523 LVGERGaQLSGGQKQ------RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG---RTTIVIAHRLSTVR 593
Cdd:cd03240  109 LLDMRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVD 187

                 ....*
gi 42741659  594 NADVI 598
Cdd:cd03240  188 AADHI 192
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
751-889 5.17e-03

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 40.48  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  751 NSNLFSLLFLALGIISFITFFL--------QGFTFGKAGEILtKRLRYMVFRSMLRQDVSWFDDpkNTTGALTTRLANDA 822
Cdd:cd18554   37 LDEKVYKLFTIIGIMFFIFLILrppveyyrQYFAQWIANKIL-YDIRKDLFDHLQKLSLRYYAN--NRSGEIISRVINDV 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42741659  823 AQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKE 889
Cdd:cd18554  114 EQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILA----VKYFFGRLRKLTKE 176
COG4639 COG4639
Predicted kinase [General function prediction only];
423-511 7.23e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 38.27  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42741659  423 VALVGNSGCGKSTTVqlmQRLYDPTEgMVSVDgqDIRTInvRFLREIIGVVSQEPV-LFATTIAENIRYGRE------NV 495
Cdd:COG4639    5 VVLIGLPGSGKSTFA---RRLFAPTE-VVSSD--DIRAL--LGGDENDQSAWGDVFqLAHEIARARLRAGRLtvvdatNL 76
                         90
                 ....*....|....*.
gi 42741659  496 TMDEIEKAVKEANAYD 511
Cdd:COG4639   77 QREARRRLLALARAYG 92
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
1176-1244 7.66e-03

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 39.55  E-value: 7.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42741659 1176 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1244
Cdd:cd03270  138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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