|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-635 |
1.97e-178 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 537.83 E-value: 1.97e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 45 LFRYSdWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDKFVdTAGNFSFpvnfslsllnpgkileeeMTRYAYYYSGLG 124
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSA------------------LLLLLLLLLGLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 125 AGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFA 204
Cdd:COG1132 72 LLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 205 GFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLE 284
Cdd:COG1132 152 ALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 285 NAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 364
Cdd:COG1132 232 ELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 365 YVIFDIIDNNPKIDSfSERGHKPDSIKGNLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQR 444
Cdd:COG1132 312 ERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 445 LYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDT 524
Cdd:COG1132 389 FYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 525 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFE 604
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570 580 590
....*....|....*....|....*....|.
gi 9961252 605 DGVIVEQGSHSELMKKEGVYFKLVNMQTSGS 635
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-1219 |
1.93e-166 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 533.45 E-value: 1.93e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 18 EGDFELgisskqkRKKTKTVKmIGVLTLFRYSDWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTdKFVDTAGNFSfPVN 97
Cdd:PTZ00265 31 KGTFEL-------YKKIKTQK-IPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIM-KNMNLGENVN-DII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 98 FSLSLLnpgkileeemtryayyysglGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRL 177
Cdd:PTZ00265 101 FSLVLI--------------------GIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 178 TDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAE 257
Cdd:PTZ00265 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 258 EALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVIS--------KEYT 329
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 330 IGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSfSERGHKPDSIKgNLEFNDVHFSYPSRANV 409
Cdd:PTZ00265 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINI-DGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAE 488
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 489 NI-------------------------------------CYGRGNVTM-----DEIKKAVKEANA--------------- 511
Cdd:PTZ00265 479 NIkyslyslkdlealsnyynedgndsqenknkrnscrakCAGDLNDMSnttdsNELIEMRKNYQTikdsevvdvskkvli 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 512 YEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAH 589
Cdd:PTZ00265 559 HDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAH 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 590 RLSTVRNADVI-----------------------------------------------AGFEDGVIVEQGSHSELMK-KE 621
Cdd:PTZ00265 639 RLSTIRYANTIfvlsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKnKN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 622 GVYFKLVNMQTSGSQIQSEefelNDEKAATRMapngwKSRLFRHSTQ---------------KNLKNSQMCQKSlDVETD 686
Cdd:PTZ00265 719 GIYYTMINNQKVSSKKSSN----NDNDKDSDM-----KSSAYKDSERgydpdemngnskhenESASNKKSCKMS-DENAS 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 687 GLEANvPPVSFLKVLKLNKTEWPY---------------FVVGTVCAIANGGLQPAFSVIFSEIIA-IFgpgDDAVKQQK 750
Cdd:PTZ00265 789 ENNAG-GKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVStLF---DFANLEAN 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 751 CNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGT 830
Cdd:PTZ00265 865 SNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVN 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 831 RLALIAQNIANLGTGIIISFIYgwqltllllavVPIIA--VSGI--VEMKL------LAGNAKRDKKELEAAGKI----- 895
Cdd:PTZ00265 945 NIVIFTHFIVLFLVSMVMSFYF-----------CPIVAavLTGTyfIFMRVfairarLTANKDVEKKEINQPGTVfayns 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 896 -----------ATEAIENIRTVVSLTQERKFESMyVEKL-----------------------------------YGPYRV 929
Cdd:PTZ00265 1014 ddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNL-IEKAidysnkgqkrktlvnsmlwgfsqsaqlfinsfaywFGSFLI 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 930 --------------FSAIVFGAVAlGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLK---PDKFEGNITFNEV 992
Cdd:PTZ00265 1093 rrgtilvddfmkslFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDV 1171
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 993 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-------------------------------- 1040
Cdd:PTZ00265 1172 NFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvg 1251
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1041 ----------------------PLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIV 1098
Cdd:PTZ00265 1252 mknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVK 1329
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1099 SAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL----DKAr 1174
Cdd:PTZ00265 1330 RACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA- 1408
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1175 eGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1219
Cdd:PTZ00265 1409 -DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
696-1230 |
6.30e-158 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 484.28 E-value: 6.30e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 696 SFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDdavkQQKCNIFSLIFLFLGIISFFTFFLQGF 774
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD----LSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 775 TFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGW 854
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 855 QLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFE-------------SMYVE 921
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELerfreaneelrraNLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 922 KLYGPY----RVFSAIVFGAVA------------------------------LGHASSFAPDYAKAKLSAAHLFMLFERQ 967
Cdd:COG1132 242 RLSALFfplmELLGNLGLALVLlvggllvlsgsltvgdlvafilyllrlfgpLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 968 PLIDSySEEGLKPDKFEGNITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVL 1047
Cdd:COG1132 322 PEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1048 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQ 1127
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1128 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1207
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 9961252 1208 THQQLLAQKGIYFSMVSVQAGTQ 1230
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
395-631 |
4.23e-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: 458.16 E-value: 4.23e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
987-1226 |
7.34e-152 |
|
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: 455.08 E-value: 7.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIAYGDNSRvvSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1146
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1226
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
123-632 |
1.70e-141 |
|
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: 445.82 E-value: 1.70e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 123 LGAGVLVAAYIQV------SFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDdISKISEGIGDKVGMF 195
Cdd:COG2274 198 LAIGLLLALLFEGllrllrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 196 FQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 275
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 276 LERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF--SVGQAAPC 353
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLG--QLIAFNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 354 IDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDsIKGNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGC 433
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 434 GKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYE 513
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 514 FIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 593
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 9961252 594 VRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQT 632
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-367 |
2.38e-138 |
|
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: 422.84 E-value: 2.38e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 57 MSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFSL-SLLNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQV 135
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLnSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 136 SFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWK 215
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 216 LTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAI 295
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 296 SANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 367
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
42-628 |
1.73e-135 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 429.91 E-value: 1.73e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 42 VLTLFRYSDWQDKLFMSLGTIMAIahgSGLPLMMIVF--GEMTDKFVDTAGNFSFPVN-FSLSLLNPGkileeemtryay 118
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTL---SSLGEMFIPFytGRVIDTLGGDKGPPALASAiFFMCLLSIA------------ 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 119 yySGLGAGVLVAAYiqvsfwTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQA 198
Cdd:TIGR00958 214 --SSVSAGLRGGSF------NYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 199 VATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 278
Cdd:TIGR00958 286 LVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASR 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQAAPCIDAFA 358
Cdd:TIGR00958 366 FKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVY 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 359 N----ARGAAYVIFDIIDNNPKIDSfsERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCG 434
Cdd:TIGR00958 442 SgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 435 KSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEF 514
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDF 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 515 IMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAalDKAREGRTTIVIAHRLSTV 594
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTV 677
|
570 580 590
....*....|....*....|....*....|....
gi 9961252 595 RNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLV 628
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
111-631 |
1.03e-125 |
|
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: 399.46 E-value: 1.03e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:TIGR02204 55 GLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:TIGR02204 135 SLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIGAfSVGQ 349
Cdd:TIGR02204 215 HEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTlGQFVFYAVMVAG-SIGT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 350 AAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVG 429
Cdd:TIGR02204 294 LSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 430 SSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEA 509
Cdd:TIGR02204 374 PSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 510 NAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH 589
Cdd:TIGR02204 454 HAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 9961252 590 RLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:TIGR02204 534 RLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
689-1227 |
2.72e-121 |
|
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: 391.89 E-value: 2.72e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 689 EANVPPVSFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQkcNIFSLIFLFLGIISFFT 768
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVI------DRVLPNQ--DLSTLWVLAIGLLLALL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 769 F-----FLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLaTDAAQVQGATGTRLALIAQNIANLG 843
Cdd:COG2274 208 FegllrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 844 TGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAgnaKRDKKELEAAGKIAT---EAIENIRTVVSLTQE----RKFE 916
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAEsrfrRRWE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 917 SMYVEKL------------------------------YGPYRV------------FSAIVFGAVA-LGHASSFAPDYAKA 953
Cdd:COG2274 362 NLLAKYLnarfklrrlsnllstlsgllqqlatvallwLGAYLVidgqltlgqliaFNILSGRFLApVAQLIGLLQRFQDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 954 KLSAAHLFMLFERQPLIDSySEEGLKPDKFEGNITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ 1033
Cdd:COG2274 442 KIALERLDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLK 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1034 LLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETL 1113
Cdd:COG2274 520 LLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEAL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1114 PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNAD 1193
Cdd:COG2274 598 PMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLAD 677
|
570 580 590
....*....|....*....|....*....|....
gi 9961252 1194 LIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQA 1227
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-367 |
3.42e-120 |
|
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: 374.12 E-value: 3.42e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 57 MSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFslsllnpgkilEEEMTRYAYYYSGLGAGVLVAAYIQVS 136
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEF-----------LDDVNKYALYFVYLGIGSFVLSYIQTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 137 FWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKL 216
Cdd:cd18577 70 CWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 217 TLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAIS 296
Cdd:cd18577 150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 297 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 367
Cdd:cd18577 230 SGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
684-1223 |
2.15e-115 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 376.37 E-value: 2.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 684 ETDGLEANVPPVSFlKVLKLNKTEWPYFVVGTV---CAIANGGLQPAFSvifSEIIAIFGpGDDAVKQQKCNIFSLIFLF 760
Cdd:TIGR00958 137 EAEQGQSETADLLF-RLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLG-GDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 761 LGiiSFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIA 840
Cdd:TIGR00958 212 IA--SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 841 NLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYV 920
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 921 EKL----------------------------------YGPYRVFSAIVFGA---------VALGHA----SSFAPDYAKA 953
Cdd:TIGR00958 368 EALeetlqlnkrkalayagylwttsvlgmliqvlvlyYGGQLVLTGKVSSGnlvsfllyqEQLGEAvrvlSYVYSGMMQA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 954 KLSAAHLFMLFERQPLIDSysEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ 1033
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAA 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1034 LLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETL 1113
Cdd:TIGR00958 526 LLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDFIMEF 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1114 PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLSTIQNAD 1193
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERAD 681
|
570 580 590
....*....|....*....|....*....|
gi 9961252 1194 LIVVFQNGRVKEHGTHQQLLAQKGIYFSMV 1223
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
129-631 |
4.56e-114 |
|
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: 367.89 E-value: 4.56e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNaMTVFFSiligafSVGQAAPCIDAFANARG------ 362
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 363 -AAYVIFDIIDNNPKIDsfsERGHKPDSIKGNLEFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQL 441
Cdd:TIGR02203 302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 442 IQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGR-GNVTMDEIKKAVKEANAYEFIMKLPQ 520
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 521 KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVI 600
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|.
gi 9961252 601 AGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
701-970 |
6.49e-113 |
|
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: 355.22 E-value: 6.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 701 LKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAG 780
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 781 EILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLL 860
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 861 LAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYR------------ 928
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKkglrralisglg 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 929 -----------------------------------VFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLI 970
Cdd:cd18578 241 fglsqsltffayalafwyggrlvangeytfeqffiVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-636 |
1.38e-112 |
|
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: 365.30 E-value: 1.38e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 265 TVIAFGGQNKELERYQKHLENAKEIGIKKAISAN---------ISMGIAFLLIYASYAlafwygstlVISKEYTIGNamt 335
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGD--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 336 vfFsILIGAFSVGQAAPCidafaNARGAAY-----------VIFDIIDNNPKIDSfserghKPDSI-----KGNLEFNDV 399
Cdd:COG5265 298 --F-VLVNAYLIQLYIPL-----NFLGFVYreirqaladmeRMFDLLDQPPEVAD------APDAPplvvgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 400 HFSY-PSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQE 478
Cdd:COG5265 364 SFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 479 PVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 559 ATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQTSGSQ 636
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
394-627 |
7.05e-112 |
|
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: 349.22 E-value: 7.05e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
142-631 |
4.57e-109 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 354.71 E-value: 4.57e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 142 AGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDD------------ISKISEGigdkvgmffqavATFFAGFIVG 209
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------ASIIGLFIMM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 210 FIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEI 289
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 290 GIKKAISANISMGIAFLLiyASYALAF--WYGSTLVISKEYTIGnAMTVFFSILIGAFSVGQAAPCIDA-FANARGAAYV 366
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 367 IFDIIDNNPKIDsfsERGHKPDSIKGNLEFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLY 446
Cdd:PRK11176 318 LFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 447 DPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNV-TMDEIKKAVKEANAYEFIMKLPQKFDTL 525
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 526 VGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFED 605
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|....*.
gi 9961252 606 GVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
752-1226 |
2.16e-108 |
|
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: 352.85 E-value: 2.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 752 NIFSLIF---LFLGIISFFTFFLqgftFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGAT 828
Cdd:TIGR02204 59 RYFAFLLvvaLVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 829 GTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVS 908
Cdd:TIGR02204 133 GSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 909 LTQERKFESMY---VEKLYGPYR----------------VFSAIV----------------------------FGAVALG 941
Cdd:TIGR02204 213 FGHEDAERSRFggaVEKAYEAARqrirtralltaivivlVFGAIVgvlwvgahdviagkmsagtlgqfvfyavMVAGSIG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 942 HASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALV 1021
Cdd:TIGR02204 293 TLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1022 GSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdnsRV-VSQDEIVSA 1100
Cdd:TIGR02204 373 GPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG---RPdATDEEVEAA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1101 AKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCI 1180
Cdd:TIGR02204 450 ARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTL 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 9961252 1181 VIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1226
Cdd:TIGR02204 530 IIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
394-631 |
4.14e-108 |
|
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: 339.21 E-value: 4.14e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
987-1219 |
1.84e-105 |
|
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: 331.89 E-value: 1.84e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIAYGDnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1146
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1219
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
959-1227 |
2.89e-104 |
|
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: 342.57 E-value: 2.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 959 HLFMLFERQPLI-DSYSEEGLKPDkfEGNITFNEVVFNY-PTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1036
Cdd:COG5265 331 RMFDLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1037 RFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHK 1116
Cdd:COG5265 406 RFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1117 YETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1196
Cdd:COG5265 484 YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
250 260 270
....*....|....*....|....*....|.
gi 9961252 1197 VFQNGRVKEHGTHQQLLAQKGIYFSMVSVQA 1227
Cdd:COG5265 564 VLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
987-1226 |
3.05e-101 |
|
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: 320.72 E-value: 3.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1146
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1226
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
696-1229 |
2.01e-100 |
|
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: 330.91 E-value: 2.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 696 SFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGF 774
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 775 TFGKageiLTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTRLALIAQNIANLGTgIIISFIYG 853
Cdd:TIGR02203 81 VSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASaATDAFIVLVRETLTVIGL-FIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 854 WQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQE----RKFE---------SMYV 920
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDavsnrnrrlAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 921 EK---LYGP------YRVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFM----------------------LFErqpL 969
Cdd:TIGR02203 234 TSagsISSPitqliaSLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIrplksltnvnapmqrglaaaesLFT---L 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 970 IDSYSEE---GLKPDKFEGNITFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV 1046
Cdd:TIGR02203 311 LDSPPEKdtgTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1047 LLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQdEIVSAAKAANIHPFIETLPHKYETRVGDKGT 1126
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRA-EIERALAAAYAQDFVDKLPLGLDTPIGENGV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1127 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEH 1206
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVER 548
|
570 580
....*....|....*....|...
gi 9961252 1207 GTHQQLLAQKGIYFSMVSVQAGT 1229
Cdd:TIGR02203 549 GTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
392-622 |
2.12e-98 |
|
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: 312.62 E-value: 2.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEG 622
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
985-1217 |
1.78e-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: 307.61 E-value: 1.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQ 1064
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 LGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIR 1144
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1217
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
358-622 |
3.85e-95 |
|
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: 316.31 E-value: 3.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 358 ANARGAAYVIFDIIDNNPKIdsfSERGHKPDSIKGN--LEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGK 435
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 436 STTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFI 515
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 516 MKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVR 595
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 9961252 596 NADVIAGFEDGVIVEQGSHSELMKKEG 622
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
295-657 |
5.87e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 313.82 E-value: 5.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 295 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGN--AMTVFFSILIG------AF--SVGQAAPCIDAFanargaa 364
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEvvAFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 365 yviFDIIDNNPKIDsfsERGHKPD--SIKGNLEFNDVHFSYPSRAnvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI 442
Cdd:PRK13657 310 ---FEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 443 QRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKF 522
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 523 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 602
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 603 FEDGVIVEQGSHSELMKKEGVYFKLVNMQtsgsqiqseeFELNDEKAATRMAPNG 657
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQ----------GMLQEDERRKQPAAEG 586
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
753-1228 |
3.13e-92 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 308.87 E-value: 3.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 753 IFSLIFLfLGIISFFTFFLQGFTFGKAGEILTRRLrsmaFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 832
Cdd:PRK11176 71 VIGLMIL-RGITSFISSYCISWVSGKVVMTMRRRL----FGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 833 ALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS-GIVemkllagnAKR----DKKELEAAGKIATEA-------- 899
Cdd:PRK11176 144 ITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVV--------SKRfrniSKNMQNTMGQVTTSAeqmlkghk 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 900 ---------IENIR-TVVSLTQERKfeSMyveKLYGPYRVFSAIV-----FGAVALGHASSFapDYAKAKLSAAHLFMLF 964
Cdd:PRK11176 216 evlifggqeVETKRfDKVSNRMRQQ--GM---KMVSASSISDPIIqliasLALAFVLYAASF--PSVMDTLTAGTITVVF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 965 ER-----QPL-----------------------IDSYSE--EG-LKPDKFEGNITFNEVVFNYPTRaNVPVLQGLSLEVK 1013
Cdd:PRK11176 289 SSmialmRPLksltnvnaqfqrgmaacqtlfaiLDLEQEkdEGkRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1014 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVvS 1093
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQY-S 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1094 QDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA 1173
Cdd:PRK11176 447 REQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1174 REGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1228
Cdd:PRK11176 527 QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
138-627 |
4.10e-91 |
|
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: 305.15 E-value: 4.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 138 WTLaagRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDIskisegigDKVGMFF-QAVATFFAGFIVGFIrgwkL 216
Cdd:COG4987 82 ATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----A 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 217 TLVIMAISPILGLS-------AAVWAKILSAFSDKELAAYAKAG-----AVAEEALGAIRTVIAFGGQNKELERYQKHLE 284
Cdd:COG4987 147 VAFLAFFSPALALVlalglllAGLLLPLLAARLGRRAGRRLAAAraalrARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 285 NAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVgqAAPCIDAFAN---AR 361
Cdd:COG4987 227 RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 362 GAAYVIFDIIDNNPKIDSFSERGHKPDSikGNLEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQL 441
Cdd:COG4987 304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 442 IQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQK 521
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 522 FDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIA 601
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*.
gi 9961252 602 GFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
700-1217 |
3.11e-88 |
|
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: 297.05 E-value: 3.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 700 VLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIA--IFGPGDDAvkqqkcNIFSLIFLFLGII---SFFTFFLQGF 774
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLS------ALLPLLGLLLAVLllrALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 775 TFgKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTrLATDaaQVQGATG------TRLALIAqnIANLGTGIII 848
Cdd:COG4988 82 AF-RAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELAT-LLTE--GVEALDGyfarylPQLFLAA--LVPLLILVAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 849 SFIYgWQLTLLLLAVVPIIAVSGIVEMKllaGNAKRDKKELEAAGKIATEAIENIR---TVVSLTQERKfesmYVEKLYG 925
Cdd:COG4988 154 FPLD-WLSGLILLVTAPLIPLFMILVGK---GAAKASRRQWRALARLSGHFLDRLRgltTLKLFGRAKA----EAERIAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 926 ---PYR------------------VFSA--IVFGAVALGH---------ASSF-----APDY--------------AKAK 954
Cdd:COG4988 226 aseDFRkrtmkvlrvaflssavleFFASlsIALVAVYIGFrllggsltlFAALfvlllAPEFflplrdlgsfyharANGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 955 LSAAHLFMLFERQPLIDSYSEEGLKPDKfEGNITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL 1034
Cdd:COG4988 306 AAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1035 LERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVSAAKAANIHPFIETLP 1114
Cdd:COG4988 383 LLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1115 HKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADL 1194
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|...
gi 9961252 1195 IVVFQNGRVKEHGTHQQLLAQKG 1217
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
978-1203 |
1.81e-87 |
|
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: 282.82 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 978 LKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN 1057
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1058 VQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIA 1137
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
199-632 |
7.75e-86 |
|
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: 294.34 E-value: 7.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 199 VATFFAgfiVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 278
Cdd:TIGR01846 266 VVVFLA---VMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAFS--VGQAAPCIDA 356
Cdd:TIGR01846 343 WDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVTqpVLRLAQLWQD 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 357 FANARGAAYVIFDIIdNNPKIDSFSERGHKPDsIKGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKS 436
Cdd:TIGR01846 421 FQQTGIALERLGDIL-NSPTEPRSAGLAALPE-LRGAITFENIRFRYAPDSPE-VLSNLNLDIKPGEFIGIVGPSGSGKS 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 437 TTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIM 516
Cdd:TIGR01846 498 TLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFIS 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 517 KLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN 596
Cdd:TIGR01846 578 ELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRA 657
|
410 420 430
....*....|....*....|....*....|....*.
gi 9961252 597 ADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQT 632
Cdd:TIGR01846 658 CDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
394-631 |
1.65e-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: 275.13 E-value: 1.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
394-606 |
2.68e-83 |
|
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: 268.87 E-value: 2.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 606
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
387-608 |
6.16e-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: 270.11 E-value: 6.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 387 PDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN 466
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 YLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVI 608
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-960 |
1.30e-81 |
|
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: 269.92 E-value: 1.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVK-----------------QQKCNIFSLIFLFLGIISFFTFFLQG 773
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 774 FTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYG 853
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 854 WQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYR----- 928
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRngikk 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 929 -------------------------------------------VFSAIVFGAVALGHASSFAPdYAKAKLSAAHL 960
Cdd:cd18558 239 aitfnismgaaflliyasyalafwygtylvtqqeysigevltvFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
987-1226 |
1.36e-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: 263.96 E-value: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQL 1065
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1145
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSV 1225
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 9961252 1226 Q 1226
Cdd:cd03252 237 Q 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
980-1217 |
1.04e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 274.15 E-value: 1.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 980 PDKFEGNITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQ 1059
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1060 WLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIA 1139
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1140 RALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1217
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
932-1224 |
1.85e-79 |
|
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: 272.80 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 932 AIVFGAVALGHAssFAP------DYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDkfEGNITFNEVVFNYPTrANVPVL 1005
Cdd:COG4987 277 LLVLAALALFEA--LAPlpaaaqHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPG-AGRPVL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1006 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAY 1085
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1086 GDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKV 1165
Cdd:COG4987 432 ARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1166 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVS 1224
Cdd:COG4987 510 LLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
987-1202 |
2.93e-79 |
|
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: 257.70 E-value: 2.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIRQP 1146
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGR 1202
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
57-345 |
3.53e-76 |
|
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: 253.33 E-value: 3.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 57 MSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFslsllnpgkileeemtrYAYYYSGLGAGVLVAAYIQVS 136
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV-----------------YSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 137 FWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKL 216
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 217 TLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAIS 296
Cdd:pfam00664 144 TLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 297 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 345
Cdd:pfam00664 224 NGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
51-377 |
7.71e-76 |
|
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: 253.91 E-value: 7.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 51 WQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDkfvdtagnfsfpvnfSLSLLNPGKILEEeMTRYAYYYSGLGAGVLVA 130
Cdd:cd18578 5 KPEWPLLLLGLIGAIIAGAVFPVFAILFSKLIS---------------VFSLPDDDELRSE-ANFWALMFLVLAIVAGIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 131 AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFD--INDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:cd18578 69 YFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:cd18578 149 AFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIF 368
Cdd:cd18578 229 KGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIF 308
|
....*....
gi 9961252 369 DIIDNNPKI 377
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
982-1228 |
1.73e-74 |
|
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: 261.99 E-value: 1.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 982 KFEGNITFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL 1061
Cdd:TIGR01846 451 ELRGAITFENIRFRYAPDS-PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 RAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARA 1141
Cdd:TIGR01846 530 RRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1142 LIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFS 1221
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
....*..
gi 9961252 1222 MVSVQAG 1228
Cdd:TIGR01846 688 LWQQQSG 694
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
963-1219 |
5.59e-73 |
|
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: 258.34 E-value: 5.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 963 LFERQPLIDSYSEEglkPDKFEGNITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPL 1042
Cdd:TIGR03796 457 LLEEPEGSAATSEP---PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPW 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1043 AGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVG 1122
Cdd:TIGR03796 533 SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1123 DKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLSTIQNADLIVVFQNGR 1202
Cdd:TIGR03796 611 EGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGK 688
|
250
....*....|....*..
gi 9961252 1203 VKEHGTHQQLLAQKGIY 1219
Cdd:TIGR03796 689 VVQRGTHEELWAVGGAY 705
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
795-1226 |
1.56e-71 |
|
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: 253.34 E-value: 1.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 795 MLRQDMSWFDDHknSTGALSTRlatdaaqVQGATGTRLALIAQNIANLGTGI--IIS----FIYGWQLTL----LLLAVV 864
Cdd:TIGR03797 219 LLRLPVSFFRQY--STGDLASR-------AMGISQIRRILSGSTLTTLLSGIfaLLNlglmFYYSWKLALvavaLALVAI 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 865 PIIAVSGIVemkllagNAKRDKKELEAAGKIATEAIENIRTVVSL----TQERKFesMYVEKLYGPYR------------ 928
Cdd:TIGR03797 290 AVTLVLGLL-------QVRKERRLLELSGKISGLTVQLINGISKLrvagAENRAF--ARWAKLFSRQRklelsaqrienl 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 929 ----------VFSAIVFGAV-------------------ALGHASSFAPDYAKAKLSAAHLFMLFER-QPLIDS---YSE 975
Cdd:TIGR03797 361 ltvfnavlpvLTSAALFAAAisllggaglslgsflafntAFGSFSGAVTQLSNTLISILAVIPLWERaKPILEAlpeVDE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 976 EGLKPDKFEGNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAK 1054
Cdd:TIGR03797 441 AKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1055 KLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsrVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQ 1134
Cdd:TIGR03797 519 GLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1135 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|..
gi 9961252 1215 QKGIYFSMVSVQ 1226
Cdd:TIGR03797 674 REGLFAQLARRQ 685
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
295-640 |
2.17e-71 |
|
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: 250.19 E-value: 2.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 295 ISANISMgIAFLLIyasyalafwyGSTLVISKEYTIGNAMTV--FFSILIGAFSvgQAAPCIDAFANARGAAYVIFDIID 372
Cdd:TIGR01192 248 MASTISM-MCILVI----------GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 373 NNPKIDSFSERGHKPDsIKGNLEFNDVHFSYPSRAnvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGT 452
Cdd:TIGR01192 315 SVFQREEPADAPELPN-VKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 453 INIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQ 532
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 612
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
330 340
....*....|....*....|....*...
gi 9961252 613 SHSELMKKEGVYFKLvnMQTSGSQIQSE 640
Cdd:TIGR01192 552 SFQELIQKDGRFYKL--LRRSGLLTNQP 577
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
392-612 |
1.16e-67 |
|
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: 227.09 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
356-600 |
1.38e-66 |
|
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: 234.87 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 356 AFANARGAAYVIFDIIDNNPKIdsFSERGHKPDSIKGNLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGK 435
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 436 STTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFI 515
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 516 MKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVR 595
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 9961252 596 NADVI 600
Cdd:TIGR02857 522 LADRI 526
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
985-1203 |
6.85e-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: 6.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQ 1064
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 LGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIR 1144
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
392-613 |
8.42e-66 |
|
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: 221.60 E-value: 8.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENICyGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
123-657 |
2.35e-65 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 232.30 E-value: 2.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 123 LGAGVLVAA--YIQVSFWTL----AAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:PRK10789 39 IGTMVLIAVvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 197 QAVATFFAGFIVGFIR-GWKLTLVIMAISPILGLSAAVWAKIL--------SAFSdkelaayaKAGAVAEEALGAIRTVI 267
Cdd:PRK10789 119 DSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLherfklaqAAFS--------SLNDRTQESLTSIRMIK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 268 AFGgqnkeLERYQKHL--ENAKEIGIKKA----ISANISMGIaFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 341
Cdd:PRK10789 191 AFG-----LEDRQSALfaADAEDTGKKNMrvarIDARFDPTI-YIAIGMANLLAIGGGSWMVVNGSLTLG-QLTSFVMYL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 342 igafsvGQAAPCIDAFA---N--ARG-AAYV-IFDIIDNNPKIDSfserGHKP-DSIKGNLEFNDVHFSYPsRANVKILK 413
Cdd:PRK10789 264 ------GLMIWPMLALAwmfNivERGsAAYSrIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPALE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 414 GLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYG 493
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 494 RGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQA 573
Cdd:PRK10789 413 RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 574 ALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQtsgsQIqseEFELNDEKAATRM 653
Cdd:PRK10789 493 NLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ----QL---EAALDDAPEIREE 565
|
....
gi 9961252 654 APNG 657
Cdd:PRK10789 566 AVDA 569
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
953-1215 |
2.14e-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: 229.25 E-value: 2.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 953 AKLSAAHLFMLFERQPLidsySEEGLKPDKFEGNITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVV 1032
Cdd:COG4618 301 ARQAYRRLNELLAAVPA----EPERMPLPRPKGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1033 QLLERFYDPLAGTVLLDGQEAKklnvQWLRAQLG--I--VSQEPILFDCSIAENIA-YGDnsrvVSQDEIVSAAKAANIH 1107
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLS----QWDREELGrhIgyLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVH 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1108 PFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRL 1186
Cdd:COG4618 448 EMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP 527
|
250 260
....*....|....*....|....*....
gi 9961252 1187 STIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:COG4618 528 SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-630 |
6.26e-64 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 239.16 E-value: 6.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 28 KQKRKKTKTVKMIgVLTLFRYSdwQDKLFMSLGTIMAiahGSGLPLMMIVFGemtdKFVDTAGNFSFpvnfslsllnpgk 107
Cdd:PTZ00265 804 KRKPKAPNNLRIV-YREIFSYK--KDVTIIALSILVA---GGLYPVFALLYA----KYVSTLFDFAN------------- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 108 iLEEEMTRYAYYYSGLGAGVLVAAYIQvSFWTLAAGRQIRK-IRQKFFHAILRQEIGWFDINDTTE--LNTRLTDDISKI 184
Cdd:PTZ00265 861 -LEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDQDKHAPglLSAHINRDVHLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 185 SEGIGDKVGMFFQAVATFFAGFIVGF----IRGWKLTLV------IMAISPILGLSAAVWAKIL----SAF---SDKELA 247
Cdd:PTZ00265 939 KTGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVAAVLTGTyfifmrVFAIRARLTANKDVEKKEInqpgTVFaynSDDEIF 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 248 AYAKAGAvaEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKE 327
Cdd:PTZ00265 1019 KDPSFLI--QEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGT 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 328 YTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHK---PDSIKGNLEFNDVHFSYP 404
Cdd:PTZ00265 1097 ILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYI 1176
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD------------------------------------- 447
Cdd:PTZ00265 1177 SRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvn 1256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 448 -----------------PDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEAN 510
Cdd:PTZ00265 1257 efsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAA 1336
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 511 AYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL----DKAreGRTTIV 586
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIIT 1414
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 9961252 587 IAHRLSTVRNADVIAGFED----GVIVE-QGSHSELMK-KEGVYFKLVNM 630
Cdd:PTZ00265 1415 IAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
412-1222 |
8.43e-64 |
|
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: 238.69 E-value: 8.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdirnfNVNYlreiigvVSQEPVLFSTTIAENIC 491
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------SVAY-------VPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 492 YGRGnvTMDEIKKAVKEANAYEFIMK-LPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 570
Cdd:TIGR00957 721 FGKA--LNEKYYQQVLEACALLPDLEiLPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 571 VqaaLDKA------REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFK-LVNMQTSGSQIQSEEFE 643
Cdd:TIGR00957 799 I---FEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfLRTYAPDEQQGHLEDSW 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 644 LNDEKAATRMAPNGWKSRLFRHSTQKNLKNsQMCQKSLDVETDGLEANvpPVSFLKVLKLNKTEWPYF-----VVGTV-- 716
Cdd:TIGR00957 876 TALVSGEGKEAKLIENGMLVTDVVGKQLQR-QLSASSSDSGDQSRHHG--SSAELQKAEAKEETWKLMeadkaQTGQVel 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 717 -------CAIangGLQPAFSVIF---SEIIAIFGPG-------DDAV---KQQKCNIFSLIFLFLGIISFFTFFLQGFTF 776
Cdd:TIGR00957 953 svywdymKAI---GLFITFLSIFlfvCNHVSALASNywlslwtDDPMvngTQNNTSLRLSVYGALGILQGFAVFGYSMAV 1029
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 777 GKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIAN-LGTGIIISFIygwq 855
Cdd:TIGR00957 1030 SIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGALIVILLA---- 1103
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 856 lTLLLLAVVPIIAVSGIVEMKLLAGNAkRDKKELEAAGKIA-----TEAIENIRTVVSLTQERKFESMY------VEKLY 924
Cdd:TIGR00957 1104 -TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQSdlkvdeNQKAY 1181
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 925 GPYRVFS-------------AIVFGAV-ALGHASSFAPDYAKAKLS-----AAHLFMLFERQPLIDS----------YSE 975
Cdd:TIGR00957 1182 YPSIVANrwlavrlecvgncIVLFAALfAVISRHSLSAGLVGLSVSyslqvTFYLNWLVRMSSEMETnivaverlkeYSE 1261
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 976 ---------EGLKPDKF---EGNITFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA 1043
Cdd:TIGR00957 1262 tekeapwqiQETAPPSGwppRGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAE 1340
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1044 GTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGD 1123
Cdd:TIGR00957 1341 GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAE 1417
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1124 KGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:TIGR00957 1418 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
890
....*....|....*....
gi 9961252 1204 KEHGTHQQLLAQKGIYFSM 1222
Cdd:TIGR00957 1498 AEFGAPSNLLQQRGIFYSM 1516
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
123-631 |
1.83e-63 |
|
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: 229.84 E-value: 1.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 123 LGAGVLVAAYIQVSFwTLAAGRQIRKIRQKFFHAI--------LRQEIGWFDINDTTELNTRlTDDISKISEGIGDKvgM 194
Cdd:TIGR03797 178 IALALLAAAVGAAAF-QLAQSLAVLRLETRMDASLqaavwdrlLRLPVSFFRQYSTGDLASR-AMGISQIRRILSGS--T 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 195 FFQAVATFFAGFIVG--FIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 272
Cdd:TIGR03797 254 LTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 273 NKELERYQKHLENAKEIGIKKAISANI-SMGIAFLLIYASYALaFWYGSTLVISKEYTIGNAMTvfFSILIGAFSVGqaa 351
Cdd:TIGR03797 334 NRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVLTSAAL-FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA--- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 352 pcIDAFANARGAAYVIF-------DIIDNNPKIDsfsERGHKPDSIKGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQT 424
Cdd:TIGR03797 408 --VTQLSNTLISILAVIplwerakPILEALPEVD---EAKTDPGKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEF 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 425 VALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICyGRGNVTMDEIKK 504
Cdd:TIGR03797 482 VAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 505 AVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRtt 584
Cdd:TIGR03797 561 AARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR-- 638
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 9961252 585 IVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:TIGR03797 639 IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
783-1226 |
2.15e-63 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 226.52 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 783 LTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR-LALIAQNIANLGTGIIISFIYGWQLTLLLL 861
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 862 AVVPIIAVSgivemkllagnAKRDKKELEAAGKIATEAIE--NIRTVVSLT-------------QERKFE---------S 917
Cdd:PRK10789 145 LPMPVMAIM-----------IKRYGDQLHERFKLAQAAFSslNDRTQESLTsirmikafgledrQSALFAadaedtgkkN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 918 MYVEKL---YGPyRVFSAI---------------VFGAVALGHASSFA--------PDYAKAKL-------SAAH--LFM 962
Cdd:PRK10789 214 MRVARIdarFDP-TIYIAIgmanllaigggswmvVNGSLTLGQLTSFVmylglmiwPMLALAWMfnivergSAAYsrIRA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 963 LFERQPLIDSySEEGLKPDKfeGNITFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPL 1042
Cdd:PRK10789 293 MLAEAPVVKD-GSEPVPEGR--GELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1043 AGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVG 1122
Cdd:PRK10789 369 EGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1123 DKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGR 1202
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGH 526
|
490 500
....*....|....*....|....
gi 9961252 1203 VKEHGTHQQLLAQKGIYFSMVSVQ 1226
Cdd:PRK10789 527 IAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
400-1231 |
4.45e-62 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 233.33 E-value: 4.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 400 HFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPDEGTINIDGQdirnfnvnylreiIGVVSQE 478
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 479 PVLFSTTIAENICYGrGNVTMDEIKKAVkEANAYEFIMKL-PQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:PLN03232 688 SWIFNATVRENILFG-SDFESERYWRAI-DVTALQHDLDLlPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 558 EATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLvnMQTSGSQ 636
Cdd:PLN03232 766 DPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--MENAGKM 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 637 IQSEEFELNDEKAaTRMAPN---GWKSRLFrHSTQKNLKNSQMCQKSLDVETDGLEANVppvsflkVLKLNKTEWPYFVV 713
Cdd:PLN03232 844 DATQEVNTNDENI-LKLGPTvtiDVSERNL-GSTKQGKRGRSVLVKQEERETGIISWNV-------LMRYNKAVGGLWVV 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 714 GT--VCAIANGGLQPAFSVIFSeiiaiFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMA 791
Cdd:PLN03232 915 MIllVCYLTTEVLRVSSSTWLS-----IWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAM 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 792 FKAMLRQDMSWFddHKNSTGALSTRLATDAAQvqgatgtrlalIAQNIANLGTGIIISFiygWQL--TLLLLAVVPIIAV 869
Cdd:PLN03232 990 LNSILRAPMLFF--HTNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL---WQLlsTFALIGTVSTISL 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 870 SGIVEMKLL-------AGNAKRDKKELEAA----------------------------GKIATEAIEN-IRTVVSLTQER 913
Cdd:PLN03232 1054 WAIMPLLILfyaaylyYQSTSREVRRLDSVtrspiyaqfgealnglssiraykaydrmAKINGKSMDNnIRFTLANTSSN 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 914 KFESMYVEKLyGPYRVFSAIVFGAVALGHASS---FAPDYA---KAKLSAAHLFMLFERQP---------------LIDS 972
Cdd:PLN03232 1134 RWLTIRLETL-GGVMIWLTATFAVLRNGNAENqagFASTMGlllSYTLNITTLLSGVLRQAskaenslnsvervgnYIDL 1212
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 973 YSE-----EGLKPDK---FEGNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA 1043
Cdd:PLN03232 1213 PSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK 1290
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1044 GTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGD 1123
Cdd:PLN03232 1291 GRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSE 1367
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1124 KGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:PLN03232 1368 GGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
890 900
....*....|....*....|....*...
gi 9961252 1204 KEHGTHQQLLAQKGIYFSMVSVQAGTQN 1231
Cdd:PLN03232 1448 LEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
924-1197 |
4.72e-62 |
|
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: 221.78 E-value: 4.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 924 YGPYRVFSAivfgavaLGHASsfapdyAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEgnITFNEVVFNYPTRAnvP 1003
Cdd:TIGR02857 274 YLPLRQLGA-------QYHAR------ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRR--P 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1083
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENI 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 AYGDnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE 1163
Cdd:TIGR02857 417 RLAR--PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
250 260 270
....*....|....*....|....*....|....
gi 9961252 1164 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVV 1197
Cdd:TIGR02857 495 AEVLEALRALAQGRTVLLVTHRLALAALADRIVV 528
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-960 |
2.80e-61 |
|
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: 211.95 E-value: 2.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIF-----GPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTR 785
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVP 865
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 866 IIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKL---------------------- 923
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALekarkagikkglvsglglgllf 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 924 ------------YGPYR-------------VFSAIVFGAVALGHASSFAPDYAKAKLSAAHL 960
Cdd:cd18577 239 fiifamyalafwYGSRLvrdgeispgdvltVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
391-620 |
1.81e-60 |
|
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: 218.08 E-value: 1.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 391 KGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIAENICygR-GNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIA--RfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
129-629 |
2.59e-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: 221.15 E-value: 2.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDdISKISEGIGDKVGMFFQAVATFFA-GFI 207
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 208 VGFiRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGqnkELERYQK---HLE 284
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsEFG 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 285 NAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTvfFSILIGAFsvgqaapcIDAFANargaa 364
Cdd:TIGR01193 366 DYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLIT--FNALLSYF--------LTPLEN----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 365 yvifdIIDNNPK----------------IDSFSERGHKPDS---IKGNLEFNDVHFSYPSRANvkILKGLNLKVQSGQTV 425
Cdd:TIGR01193 431 -----IINLQPKlqaarvannrlnevylVDSEFINKKKRTElnnLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKT 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 426 ALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYG-RGNVTMDEIKK 504
Cdd:TIGR01193 504 TIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWA 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 505 AVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTT 584
Cdd:TIGR01193 584 ACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTI 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 9961252 585 IVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVN 629
Cdd:TIGR01193 663 IFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
758-1232 |
2.92e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 218.05 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 758 FLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQ 837
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 838 NIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFES 917
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 918 MYVEKLYGPYR------------------VFSAIVF------------GAVALGHASSFApDY----------------- 950
Cdd:PRK10790 229 RMGEASRSHYMarmqtlrldgfllrpllsLFSALILcgllmlfgfsasGTIEVGVLYAFI-SYlgrlneplielttqqsm 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 951 -AKAKLSAAHLFMLFE--RQPL-IDSYSEEGlkpdkfeGNITFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGC 1026
Cdd:PRK10790 308 lQQAVVAGERVFELMDgpRQQYgNDDRPLQS-------GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1027 GKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdnsRVVSQDEIVSAAKAANI 1106
Cdd:PRK10790 379 GKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1107 HPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1186
Cdd:PRK10790 456 AELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 9961252 1187 STIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTQNL 1232
Cdd:PRK10790 536 STIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEEL 581
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
333-627 |
3.87e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 217.39 E-value: 3.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 333 AMTVF-----FSILI---GAFS-VGQaapCIdafanarGAAYVIFDIIDNNPKIdSFSERgHKPDSIKGNLEFNDVHFSY 403
Cdd:PRK11160 281 ALFVFaalaaFEALMpvaGAFQhLGQ---VI-------ASARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTY 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 404 PSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFS 483
Cdd:PRK11160 349 PDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 484 TTIAENICYGRGNVTmDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 563
Cdd:PRK11160 428 ATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 564 DTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
985-1208 |
9.30e-60 |
|
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: 204.26 E-value: 9.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITFNEVVFNYptRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRA 1063
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALI 1143
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
389-1223 |
2.45e-59 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 224.62 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 389 SIKgnlefnDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPDEGTINIDGqdirnfNVNY 467
Cdd:PLN03130 616 SIK------NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG------TVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 lreiigvVSQEPVLFSTTIAENICYGrGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARAL 547
Cdd:PLN03130 684 -------VPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 548 VRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFK 626
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 627 LvnMQTSGS--QIQSEEFELNDEKAATRMAPNGWKSRLFRHSTQKNLKNSQmcqKSLDVETDGLEANVppVSFlKVLKLN 704
Cdd:PLN03130 836 L--MENAGKmeEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEG---KSVLIKQEERETGV--VSW-KVLERY 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 705 KTEWP-YFVVGTV--CAIANGGLQPAFSVIFSEIIAIFGPgddavKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGE 781
Cdd:PLN03130 908 KNALGgAWVVMILflCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSL 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 782 ILTRRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDaaqvqgatgtrLALIAQNIANLGTGIIISFiygWQL--TLL 859
Cdd:PLN03130 983 YAAKRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQLlsTFV 1046
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 860 LLAVVPIIAVSGIveMKLLAG---------NAKRDKKEL-------------EAAGKIAT----EAIE------------ 901
Cdd:PLN03130 1047 LIGIVSTISLWAI--MPLLVLfygaylyyqSTAREVKRLdsitrspvyaqfgEALNGLSTirayKAYDrmaeingrsmdn 1124
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 902 NIR-TVVSLTQERkFESMYVEKLYGPYRVFSAI--VFGAVALGHASSFAP------DYA-------KAKLSAAHL----F 961
Cdd:PLN03130 1125 NIRfTLVNMSSNR-WLAIRLETLGGLMIWLTASfaVMQNGRAENQAAFAStmglllSYAlnitsllTAVLRLASLaensL 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 962 MLFER-QPLIDSYSE-----EGLKPDK---FEGNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTV 1031
Cdd:PLN03130 1204 NAVERvGTYIDLPSEaplviENNRPPPgwpSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSM 1281
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1032 VQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIE 1111
Cdd:PLN03130 1282 LNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIR 1358
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1112 TLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTI 1189
Cdd:PLN03130 1359 RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTI 1436
|
890 900 910
....*....|....*....|....*....|....*
gi 9961252 1190 QNADLIVVFQNGRVKEHGTHQQLLAQKGIYFS-MV 1223
Cdd:PLN03130 1437 IDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
956-1222 |
1.59e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.60 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 956 SAAHLFMLFERQPLIDSYSEEGLKPDKfeGNITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1035
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1036 ERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYgdnsrvvsqdeivsAAKAANIHPFIETL-- 1113
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqq 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1114 ---------PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1184
Cdd:PRK11160 453 vgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260 270
....*....|....*....|....*....|....*...
gi 9961252 1185 RLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1222
Cdd:PRK11160 533 RLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
711-940 |
2.01e-55 |
|
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: 194.01 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQqKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSM 790
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ-ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 791 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS 870
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 871 GIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYR------VFSAIVFGAVAL 940
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKagikkaVANGLSFGITQF 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
756-1225 |
1.37e-54 |
|
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: 203.82 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 756 LIFLFLGIISFFtfflQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGATG-TRLAL 834
Cdd:TIGR01193 204 IAYIIQQILSYI----QIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRR--TGEIVSRF-TDASSIIDALAsTILSL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 835 IAqniaNLGTGIIISFIYGWQ---LTLLLLAVVPIIAVSGIVEMKLLAgnaKRDKKELEAAGKIATEAIEN---IRTVVS 908
Cdd:TIGR01193 277 FL----DMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVIIILFKRTFN---KLNHDAMQANAVLNSSIIEDlngIETIKS 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 909 LTQE----RKFESMYVEKLYGPYRVFSA--------------------------IVFGAVALGHASSFA----------- 947
Cdd:TIGR01193 350 LTSEaerySKIDSEFGDYLNKSFKYQKAdqgqqaikavtklilnvvilwtgaylVMRGKLTLGQLITFNallsyfltple 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 948 ------PDYAKAKLSAAHLFMLFerqpLIDSYSEEGLKPDKFE---GNITFNEVVFNYPTraNVPVLQGLSLEVKKGQTL 1018
Cdd:TIGR01193 430 niinlqPKLQAARVANNRLNEVY----LVDSEFINKKKRTELNnlnGDIVINDVSYSYGY--GSNILSDISLTIKMNSKT 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1019 ALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdNSRVVSQDEIV 1098
Cdd:TIGR01193 504 TIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIW 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1099 SAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREgRT 1178
Cdd:TIGR01193 583 AACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KT 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 9961252 1179 CIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSV 1225
Cdd:TIGR01193 662 IIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
141-591 |
2.21e-54 |
|
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: 199.12 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 141 AAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDIskisEGIGDkvgMFFQAVATFFAGFIVGFIrgwkLTLVI 220
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGAA----AVAAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 221 MAISP----ILGLSAAVWAKILSAFS-----DKELAAYAKAGAVAEEALGAIR---TVIAFGGQNKELERYQKHLENAKE 288
Cdd:TIGR02868 149 AVLSVpaalILAAGLLLAGFVAPLVSlraarAAEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVGQAAP-CIDAFANARGAAYVI 367
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAALPaAAQQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 368 FDIIDNNPKIDSFSERGHKPDSIKG-NLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLY 446
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 447 DPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLV 526
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 527 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 591
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
392-643 |
3.05e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 200.33 E-value: 3.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENICYGRgNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
250
....*....|..
gi 9961252 632 TSGSQIQSEEFE 643
Cdd:PRK10790 576 LAGEELAASVRE 587
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
258-620 |
4.07e-54 |
|
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: 198.73 E-value: 4.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 258 EALGAIRTViafggQNKELERYQKHLENAKEIGIKKAISANISMgiAFLLIYASYALAFwyGSTLVISKEYTIGnaMTVF 337
Cdd:TIGR01842 194 EAMGMMGNL-----TKRWGRFHSKYLSAQSAASDRAGMLSNLSK--YFRIVLQSLVLGL--GAYLAIDGEITPG--MMIA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 338 FSILigafsVGQAAPCID-------AFANARGAAYVIFDIIDNNPkidsFSERGHKPDSIKGNLEFNDVHFSYPSrANVK 410
Cdd:TIGR01842 263 GSIL-----VGRALAPIDgaiggwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPPG-GKKP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENI 490
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 570
Cdd:TIGR01842 413 ARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQA 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 571 VQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:TIGR01842 493 LANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-624 |
5.04e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.60 E-value: 5.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 356 AFANARGAAYVIFDIIDNNpkiDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGK 435
Cdd:PRK11174 313 AKAQAVGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 436 STtvqLIQRL--YDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYE 513
Cdd:PRK11174 390 TS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 514 FIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 593
Cdd:PRK11174 467 FLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
250 260 270
....*....|....*....|....*....|.
gi 9961252 594 VRNADVIAGFEDGVIVEQGSHSELMKKEGVY 624
Cdd:PRK11174 547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
394-621 |
4.61e-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: 182.53 E-value: 4.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPV--LFSTTIAENICYG---RGnVTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIA 544
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLG-LPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-618 |
6.90e-52 |
|
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: 191.27 E-value: 6.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN--VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 ---IGVVSQEPV--LF-STTIAENICYG---RGNVTMDEIKKAVKEANA-----YEFIMKLPqkfdtlvgergAQLSGGQ 537
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....
gi 9961252 615 SELM 618
Cdd:COG1123 490 EEVF 493
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1008-1222 |
9.33e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 192.75 E-value: 9.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGD 1087
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1088 NSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQ 1167
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1168 EALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1222
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
395-606 |
2.23e-51 |
|
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: 179.97 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQKQRIAIARALVRN 550
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
394-617 |
2.85e-51 |
|
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: 180.45 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD-----PDEGTINIDGQDIR--NFNVN 466
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 YLREIIGVVSQEPVLFSTTIAENICYG---RGNVTMDEIKKAVKEANAyefIMKLPQKFDTLVGERGaqLSGGQKQRIAI 543
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALR---KAALWDEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 544 ARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
950-1215 |
4.26e-51 |
|
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: 189.87 E-value: 4.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 950 YAKAKLSAAHLFMLFERQPLidsySEEGLKPDKFEGNITFNEVVFnYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKS 1029
Cdd:TIGR01842 284 FSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1030 TVVQLLERFYDPLAGTVLLDGQEAKklnvQWLRAQLG----IVSQEPILFDCSIAENIA-YGDNsrvVSQDEIVSAAKAA 1104
Cdd:TIGR01842 359 TLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGkhigYLPQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1105 NIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIA 1183
Cdd:TIGR01842 432 GVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVIT 511
|
250 260 270
....*....|....*....|....*....|..
gi 9961252 1184 HRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:TIGR01842 512 HRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
394-608 |
1.43e-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: 173.56 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVI 608
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
394-617 |
4.51e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.41 E-value: 4.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--RNFNVNYLREI 471
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFS-TTIAENICYG----RGnvtmdeIKKAVKEANAYEFIMK--LPQKFDtlvgERGAQLSGGQKQRIAIA 544
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvKK------MSKAEAEERAMELLERvgLADKAD----AYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
394-613 |
3.19e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.65 E-value: 3.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI- 471
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 --IGVVSQEPVLFST-TIAENICY-----GrgnVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQL 533
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAEllelvglsdkADAY------P-----------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 534 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 610
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 9961252 611 QGS 613
Cdd:COG1135 222 QGP 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
987-1216 |
3.82e-48 |
|
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: 171.36 E-value: 3.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPI--LFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIAR 1140
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1141 ALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
992-1203 |
4.28e-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: 169.32 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 992 VVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1071
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 PILFDCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1152 DEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
412-561 |
5.24e-48 |
|
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: 167.82 E-value: 5.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFS-TTIAENI 490
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 491 CYGRgnvTMDEIKKAVKEANAYEFIMKLPQKF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
987-1212 |
1.03e-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: 170.05 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVLLDGQE--AKKLNVQ 1059
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1060 WLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQ----DEIVSAA--KAAnihpfietLPhkyeTRVGDK--GTQLSGG 1131
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLkeelDERVEEAlrKAA--------LW----DEVKDRlhALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1210
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTE 225
|
..
gi 9961252 1211 QL 1212
Cdd:cd03260 226 QI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
394-612 |
1.53e-47 |
|
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: 167.88 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNvNYLREIIG 473
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
394-612 |
3.53e-47 |
|
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: 168.45 E-value: 3.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLR 469
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 470 EIIGVVSQEPvlFST-----TIAENIC-----YGRGNvtmdeiKKAVKEANAYEFIMKLPQKfDTLVGERGAQLSGGQKQ 539
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAeplriHGKLS------KKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
394-589 |
7.85e-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: 7.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENI----CYGRGNVTMDEIKKAVKEANayefimkLPQKF-DTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9961252 549 RNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
987-1215 |
8.97e-47 |
|
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: 176.25 E-value: 8.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN--VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWL 1061
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 RAQLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVSQDEIvsAAKAANI-------HPFIETLPHkyetrvgdkgtQLSG 1130
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAER--RERVAELlervglpPDLADRYPH-----------ELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1131 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 9961252 1208 THQQLLAQ 1215
Cdd:COG1123 488 PTEEVFAN 495
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
394-617 |
1.40e-46 |
|
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: 166.99 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI- 471
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 --IGVVSQEPVLFST-TIAENICYGR--GNVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQLSGG 536
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLeiAGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 613
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....
gi 9961252 614 HSEL 617
Cdd:cd03258 225 VEEV 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
394-611 |
2.18e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.37 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI- 471
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 ---IGVVSQEPVLFST-TIAENICYGRgnvTMDEIKKAVKEANAYEFIMKLpqkfdtLVGERG----AQLSGGQKQRIAI 543
Cdd:COG1136 85 rrhIGFVFQFFNLLPElTALENVALPL---LLAGVSRKERRERARELLERV------GLGDRLdhrpSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 544 ARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVEQ 611
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
394-619 |
2.62e-46 |
|
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: 166.69 E-value: 2.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 -IGVVSQEPVLFST-TIAENICYG---RGNVTMDEIKKAVkeanayefIMKLpqkfdTLVGERGA------QLSGGQKQR 540
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 9961252 618 MK 619
Cdd:COG1127 230 LA 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1003-1203 |
3.94e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.99 E-value: 3.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1082
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IA--YGDNSRVVSQDEIVSAAKAANIHPFIetlphkYETRVgdkgTQLSGGQKQRIAIARALIRQPQILLLDEATSALDT 1160
Cdd:COG4619 94 LPfpFQLRERKFDRERALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 1161 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:COG4619 164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
987-1207 |
3.98e-46 |
|
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: 163.64 E-value: 3.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLG 1066
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkGTQLSGGQKQRIAIARALIRQP 1146
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1207
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
989-1202 |
8.39e-46 |
|
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: 164.18 E-value: 8.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 989 FNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIV 1068
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1069 SQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARAL 1142
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1143 IRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
394-612 |
9.11e-46 |
|
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: 163.84 E-value: 9.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrnFNVNYLREIIG 473
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENICYG--RGNVTMDEIKKAVKEAnayEFIMKLpqkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVREL---LELVGL----EGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 612
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
394-608 |
1.40e-45 |
|
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: 163.81 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN----YL 468
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 REIIGVVSQEPVLFST-TIAENI---CYGRGnvtmdeIKKAVKEANAYEFI--MKLPQKFDTLVgergAQLSGGQKQRIA 542
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVelpLLLAG------VPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVI 608
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
394-629 |
1.76e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.08 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlREIIG 473
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENICY-GRgnvtMDEIKKAVKEANAYEFI--MKLPQKFDTLVGergaQLSGGQKQRIAIARALVR 549
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfAR----LYGLPRKEARERIDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQGSHSELMKK--EGVYF 625
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFL 228
|
....
gi 9961252 626 KLVN 629
Cdd:COG1131 229 ELTG 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
987-1186 |
6.15e-45 |
|
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: 171.39 E-value: 6.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:TIGR02868 335 LELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAEN--IAYGDnsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIR 1144
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1186
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-618 |
7.74e-45 |
|
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: 170.47 E-value: 7.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFNVNYLRE 470
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEP--VLFSTTIAENICYG--RGNVTMDEIKKAVKEANAYEFImklpqkfDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
394-618 |
1.08e-44 |
|
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: 162.08 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFS-TTIAENIcygrGNV-TMDEIKKAVKEANAYEFI--MKLPQKfdTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADELLalVGLDPA--EFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELM 618
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
394-617 |
1.67e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI-------RNfnvn 466
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 ylreiIGVVSQEPVLFS-TTIAENICYG---RGnVTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQKQRIA 542
Cdd:COG3842 79 -----VGMVFQDYALFPhLTVAENVAFGlrmRG-VPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
394-621 |
1.82e-44 |
|
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: 162.21 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-NVNYLREII 472
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQKfdtlvgergaqLSGGQKQRIAIA 544
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
394-606 |
4.55e-44 |
|
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: 157.73 E-value: 4.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR--NFNVNYLREI 471
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFST-TIAENICYGrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRN 550
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
392-613 |
8.29e-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: 158.34 E-value: 8.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENI-CYGRgnVTMDEIKKAVKeanayefimklpqkfdtlVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
999-1214 |
1.40e-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: 159.20 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 999 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL---- 1074
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 ---FDCSIAE--NIAYGDNSrvvsQDEIVSAAKAANIHP-FIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQI 1148
Cdd:COG1124 95 rhtVDRILAEplRIHGLPDR----EERIAELLEQVGLPPsFLDRYPH-----------QLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1149 LLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:COG1124 160 LLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
985-1208 |
1.83e-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: 157.19 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRA 1063
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAakaanihpfietlphkyeTRVGDKGTQLSGGQKQRIAIARALI 1143
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
394-619 |
4.87e-43 |
|
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: 156.89 E-value: 4.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 -IGVVSQEPVLF-STTIAENICYG---RGNVTMDEIKKAVKeanayefiMKLpqkfdTLVGERG------AQLSGGQKQR 540
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEAEVQA-ALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 9961252 618 MK 619
Cdd:cd03261 225 RA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
987-1205 |
6.78e-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: 156.09 E-value: 6.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEakklnVQWLRAQL 1065
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIEtlphkyetRVGDKGT------QLSGGQKQRIAI 1138
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1139 ARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQN--GRVKE 1205
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
394-589 |
1.56e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.40 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfnvnyLREII 472
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICYGrgnVTMDEIKKAVKEANAYEFImklpqkfdTLVGERGA------QLSGGQKQRIAIAR 545
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
394-619 |
1.88e-42 |
|
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: 155.73 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRA-NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREII 472
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVL-----FS--TTIAENI-CYGRGNVtMDEIKKAVKEANayefimkLPqkfDTLVGERGAQLSGGQKQRIAIA 544
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLrIHGLPDR-EERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
394-608 |
2.36e-42 |
|
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: 154.22 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRN--FNVNYLREI 471
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFS-TTIAENICYGRgnVTMDEIKKAVKEANAYEFIMK--LPQKFDtlvgERGAQLSGGQKQRIAIARALV 548
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 549 RNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
998-1207 |
2.77e-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: 153.83 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD- 1076
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1153 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1207
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
395-606 |
4.02e-42 |
|
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: 151.24 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQepvlfsttiaenicygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961252 555 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDG 606
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
116-629 |
4.20e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 169.00 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 116 YAYYYSGLGAGvLVAAYIQVSFWTLAAG-RQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGM 194
Cdd:PLN03232 952 YIVVYALLGFG-QVAVTFTNSFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 195 F----FQAVATFFAGFIVGFIRGWkltlvimAISPILGLSAAVWAKILSAFSD-KELAAYAKAGAVAE--EALGAIRTVI 267
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLW-------AIMPLLILFYAAYLYYQSTSREvRRLDSVTRSPIYAQfgEALNGLSSIR 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 268 AFGGQNKELERYQKHLENAKEIGIKkAISAN-------ISMGIAFLLIYASYALAFW--------YGSTLVISKEYTIgN 332
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVLRNgnaenqagFASTMGLLLSYTL-N 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 333 AMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGhkpdSIKgnleFNDVHFSYpsRANVK-I 411
Cdd:PLN03232 1182 ITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG----SIK----FEDVHLRY--RPGLPpV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENI- 490
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNId 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CYGRGNVTmdEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 570
Cdd:PLN03232 1332 PFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 571 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEG-VYFKLVN 629
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVH 1469
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1005-1156 |
5.08e-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: 150.88 E-value: 5.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-DCSIAENI 1083
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1084 AYGDNSRvvsqdEIVSAAKAANIHPFIETL--PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:pfam00005 81 RLGLLLK-----GLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
996-1207 |
8.56e-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: 153.05 E-value: 8.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 996 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL---RAQLGIVSQE 1071
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 PI-----LFdcSIAENIAygdnsrvvsqdEIVSAAKAANIHPFIETLPHKYETRVGDKGT-------QLSGGQKQRIAIA 1139
Cdd:cd03257 91 PMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1140 RALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
85-367 |
1.53e-41 |
|
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: 154.64 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 85 FVDTAGNFSFPVnFSLSLLN--PGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEI 162
Cdd:cd18557 6 LISSAAQLLLPY-LIGRLIDtiIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 163 GWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFS 242
Cdd:cd18557 85 AFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 243 DKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTL 322
Cdd:cd18557 165 KEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9961252 323 VISKEYTIGNAMT-VFFSILIgAFSVGQAAPCIDAFANARGAAYVI 367
Cdd:cd18557 245 VLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
394-589 |
2.10e-41 |
|
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: 151.86 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPS-RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylreiI 472
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICYGrgnVTMDEIKKAVKEANAYEFImklpqkfdTLVGERGA------QLSGGQKQRIAIAR 545
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
987-1205 |
2.25e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGTVLLDGQEAKKLN----V 1058
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1059 QWLRAQLGIVSQEPILFDC-SIAENIA----YGDNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQK 1133
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1134 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1205
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
987-1215 |
2.84e-41 |
|
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: 160.07 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGTVLLDGQEAKKLNVQWLRA 1063
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEPI--LFDCSIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIA 1137
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEArarvLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 9961252 1215 Q 1215
Cdd:COG1123 233 A 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
394-617 |
2.84e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 155.62 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYL----R 469
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLppkdR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 470 EIiGVVSQEPVLF-STTIAENICYG---RGnVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIAR 545
Cdd:COG3839 76 NI-AMVFQSYALYpHMTVYENIAFPlklRK-VPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 546 ALVRNPKILLLDEATSALD------TESE-AEVQAALdkareGRTTIVIAH------RLstvrnADVIAGFEDGVIVEQG 612
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
....*
gi 9961252 613 SHSEL 617
Cdd:COG3839 217 TPEEL 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
394-621 |
4.55e-41 |
|
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: 152.12 E-value: 4.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVL-FSTTIAENICYGR-------GNVT---MDEIKKAVKEANAYEFIMKLpqkFDTlvgergaqLSGGQKQRIA 542
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 9961252 620 KE 621
Cdd:COG1120 228 PE 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1001-1215 |
7.11e-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: 150.91 E-value: 7.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPLAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1075
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 -DCSIAENIAYGdnSRVVSQdeiVSAAKAanihpfiETLPHKYETRVG--DKG----TQLSGGQKQRIAIARALIRQPQI 1148
Cdd:COG1126 90 pHLTVLENVTLA--PIKVKK---MSKAEA-------EERAMELLERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1149 LLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:COG1126 158 MLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
987-1208 |
1.00e-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: 154.10 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLG 1066
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILF-DCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARA 1141
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1142 LIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGT 1208
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
987-1205 |
2.38e-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: 150.24 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEakklnVQWLRAQL 1065
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIAR 1140
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1141 ALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVFQN--GRVKE 1205
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
987-1213 |
2.93e-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: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPIL-FDCSIAENIAYG------DNSRVVSQD-EIVSAA-KAANIHPFIetlphkyETRVgdkgTQLSGGQKQRIA 1137
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlgLFGRPSAEDrEAVEEAlERTGLEHLA-------DRPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
987-1216 |
5.61e-40 |
|
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: 149.50 E-value: 5.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAK-KLNVQWLRAQL 1065
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEPilfD----CSIAEN-IAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHKyetrvgdkgtqLSGGQKQRI 1136
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1137 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 9961252 1215 QK 1216
Cdd:TIGR04520 226 QV 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
394-612 |
1.05e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.26 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD--PD---EGTINIDGQDI--RNFNVN 466
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 YLREIIGVVSQEPVLFSTTIAENICYG------RGNVTMDEI-----KKA-----VKeanayefimklpqkfDTLvGERG 530
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAalwdeVK---------------DRL-KKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGF 603
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFF 226
|
....*....
gi 9961252 604 EDGVIVEQG 612
Cdd:COG1117 227 YLGELVEFG 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
394-617 |
1.31e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.51 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 -IGVVSQEPVLFS-TTIAENICYGR-----------GNVTMDEIKKAvkeanayefimklpqkFDTL--VG------ERG 530
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVLAGRlgrtstwrsllGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGV 607
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 9961252 608 IVEQGSHSEL 617
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
394-622 |
1.98e-39 |
|
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: 146.93 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIiG 473
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENICY-GRGNvtmdEIKKAVKEANAYEFI--MKLPQKFDTLVGErgaqLSGGQKQRIAIARALVR 549
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELY----GLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEG 622
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
394-610 |
3.35e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.58 E-value: 3.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQD---IRNFNVNYLRE 470
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQE-PVLFSTTIAENICY-----GRgnvTMDEIKKAVKEAnayefIMK--LPQKFDTLVgergAQLSGGQKQRIA 542
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFEDGVIVE 610
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
987-1202 |
5.62e-39 |
|
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: 144.15 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANV--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPLAGTVLLDGQEAkklnvqwlr 1062
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGSIA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 aqlgIVSQEPILFDCSIAENIAYG---DNSRVvsqDEIVsaaKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIA 1139
Cdd:cd03250 70 ----YVSQEPWIQNGTIRENILFGkpfDEERY---EKVI---KACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1140 RALIRQPQILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVFQNGR 1202
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
394-608 |
6.79e-39 |
|
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: 142.92 E-value: 6.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaQLSGGQKQRIAIARALVRNPK 552
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 553 ILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
987-1215 |
7.66e-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: 145.03 E-value: 7.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGTVLLDGQEAKKLN---VQ 1059
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1060 WLRAQLGIVSQEPILFDC-SIAENIAYGDNSRVVSQDEIvsaakAANIHPFIET--LPHKYETRVGdkgtQLSGGQKQRI 1136
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEI-----EERVLELLELvgLEDKADAYPA----QLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1137 AIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
..
gi 9961252 1214 AQ 1215
Cdd:cd03258 230 AN 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
395-616 |
9.17e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 9.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:PRK11153 3 ELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 -IGVVSQE-PVLFSTTIAENICYGR--GNVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQLSGGQ 537
Cdd:PRK11153 83 qIGMIFQHfNLLSSRTVFDNVALPLelAGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
..
gi 9961252 615 SE 616
Cdd:PRK11153 226 SE 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
987-1215 |
1.08e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWlRAQLG 1066
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILF-DCSIAENIAYGDNSRVVSQDEIvsaakAANIHPFIET--LPHKYETRVGdkgtQLSGGQKQRIAIARALI 1143
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEA-----RERIDELLELfgLTDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
987-1215 |
1.19e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.93 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPilfD-----CSIAENIAYGDNSRVVSQDEIV----SAAKAANIHPFIETLPHKyetrvgdkgtqLSGGQKQRIA 1137
Cdd:PRK13635 85 MVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVervdQALRQVGMEDFLNREPHR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 9961252 1213 LAQ 1215
Cdd:PRK13635 228 FKS 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
394-619 |
3.28e-38 |
|
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: 145.97 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDP---DEGTINIDGQDIRNFNVNYLR 469
Cdd:COG0444 2 LEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 470 EI----IGVVSQEPvlFS---------TTIAENICYGRGnVTMDEIKKAVKEA-------NAYEFIMKLPQkfdtlvger 529
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 530 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIA- 601
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|
gi 9961252 602 --GfedGVIVEQGSHSELMK 619
Cdd:COG0444 224 myA---GRIVEEGPVEELFE 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
987-1208 |
7.15e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 145.61 E-value: 7.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGTVLLDGQEAKKLNVQWLR 1062
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 A---QLGIVSQEPILFD-CSIAENIAY-----GdnsrvVSQDEIvsAAKAAnihpfiETLphkyeTRVG--DKG----TQ 1127
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEI--RKRVA------ELL-----ELVGlsDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1128 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVK 1204
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 9961252 1205 EHGT 1208
Cdd:COG1135 221 EQGP 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
985-1223 |
7.20e-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: 142.74 E-value: 7.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQ 1064
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 LGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIR 1144
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK-GIYFSMV 1223
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1004-1212 |
7.28e-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: 7.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--PLA---GTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1076
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYG-----DNSRVVsQDEIVSAA--KAAnihpfietLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQIL 1149
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlrKAA--------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1150 LLDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVFQNGRVKEHGTHQQL 1212
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
987-1218 |
7.62e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.21 E-value: 7.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPilfD-----CSIAENIAYGDNSRVVSQDE----IVSAAKAANIHPFIETLPHKyetrvgdkgtqLSGGQKQRIA 1137
Cdd:PRK13632 87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
...
gi 9961252 1216 KGI 1218
Cdd:PRK13632 233 KEI 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
394-606 |
9.87e-38 |
|
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: 9.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANV--KILKGLNLKVQSGQTVALVGSSGCGKSTtvqLIQRL---YDPDEGTINIDGQdirnfnvnyl 468
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 reiIGVVSQEPVLFSTTIAENICYGRgnvTMDEIK-KAVKEANAYEFIMK-LPQKFDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK---PFDEERyEKVIKACALEPDLEiLPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEV--QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 606
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
988-1202 |
1.71e-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: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 988 TFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGI 1067
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1068 VSQepilfdcsiaeniaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIRQPQ 1147
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1148 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGR 1202
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
998-1202 |
3.10e-37 |
|
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: 138.09 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN--VQWLRAQLGIVSQEPILF 1075
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 -DCSIAENIAYGdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1155 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
395-621 |
6.16e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.51 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:PRK13632 9 KVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQEP--VLFSTTIAENICYGRGN--VTMDEIKK----AVKEANAYEFIMKLPQKfdtlvgergaqLSGGQKQRIAIARA 546
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKMKDiiddLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
394-617 |
8.72e-37 |
|
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: 139.24 E-value: 8.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 -IGVVSQEPVLFS-TTIAENICYGR-----------GNVTMDEIKKAvkeanayefiMKLPQKF--DTLVGERGAQLSGG 536
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRA----------LAALERVglLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVR-NADVIAGFEDGVIVEQGS 613
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGP 228
|
....
gi 9961252 614 HSEL 617
Cdd:cd03256 229 PAEL 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
987-1203 |
9.56e-37 |
|
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: 138.39 E-value: 9.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL---- 1061
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 RAQLGIVSQE----PILfdcSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIET--LPHKYETRVGdkgtQLSGGQKQR 1135
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1136 IAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVFQNGRV 1203
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
987-1217 |
1.05e-36 |
|
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: 139.22 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNvQWLRAQLG 1066
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFD-CSIAENIAYGDNSRVVSQDEIvsAAKAANIHPFIEtLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQ 1145
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFAELYGLFDEEL--KKRIEELIELLG-LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1217
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
394-621 |
1.13e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfnvnyLREIIG 473
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVL---FSTTIAENI---CYGRGNVTM---DEIKKAVKEA----NAYEFImklpqkfDTLVGErgaqLSGGQKQR 540
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsRADREAVDEAlervGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFEDGVIVEqGSHSELM 618
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 9961252 619 KKE 621
Cdd:COG1121 227 TPE 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
987-1214 |
1.29e-36 |
|
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: 138.40 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNV---QWLRA 1063
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEPILFDC-SIAENIAY-----GDNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIA 1137
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
394-617 |
1.89e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.44 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--------RNfnv 465
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlppreRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 nylreiIGVVSQEPVLF-STTIAENICYG--RGNVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQ 532
Cdd:COG1118 77 ------VGFVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdkaRE-----GRTTIVIAH-RLSTVRNADVIAGFEDG 606
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWL---RRlhdelGGTTVFVTHdQEEALELADRVVVMNQG 210
|
250
....*....|.
gi 9961252 607 VIVEQGSHSEL 617
Cdd:COG1118 211 RIEQVGTPDEV 221
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
108-364 |
2.40e-36 |
|
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: 139.61 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 108 ILEEEMTRYAYYYSGLGAGVLVAA---YIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKI 184
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRAllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 185 SEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIR 264
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 265 TVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGA 344
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGML 268
|
250 260
....*....|....*....|.
gi 9961252 345 FS-VGQAAPCIDAFANARGAA 364
Cdd:cd07346 269 FGpIQRLANLYNQLQQALASL 289
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
416-618 |
3.09e-36 |
|
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: 138.55 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI----IGVVSQEPVLF-STTIAENI 490
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CYG---RGnvtmdeIKKAVKEANAYEFImklpqkfdTLVGERG------AQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:cd03294 124 AFGlevQG------VPRAEREERAAEAL--------ELVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 562 ALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELM 618
Cdd:cd03294 190 ALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
110-350 |
4.28e-36 |
|
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: 138.92 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 110 EEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIG 189
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 190 DKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAF 269
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 270 GGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFfsiLIGAFSVGQ 349
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSF---LLYTLTVAM 273
|
.
gi 9961252 350 A 350
Cdd:cd18780 274 S 274
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1003-1214 |
5.98e-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: 136.65 E-value: 5.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNV---QWLRAQLGIVSQEPILFDC-S 1078
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYG-DNSRVVSQDEIVSAA----KAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVleklELVGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1154 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
391-627 |
6.19e-36 |
|
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: 148.94 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 391 KGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIAENIcYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNL-DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
987-1203 |
1.06e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.34 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRA 1063
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEPILFD-CSIAENI---AYGDNS------RVVSQDEIVSAAKAanihpfIET--LPHKYETRVGdkgtQLSGG 1131
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERALEA------LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
394-612 |
1.70e-35 |
|
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: 134.69 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYL----R 469
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-----VTDLppkdR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 470 EIiGVVSQEPVLF-STTIAENICYG--RGNVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03301 73 DI-AMVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
394-588 |
1.73e-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: 134.46 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLRE 470
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFST-TIAENICYGR--GNVTMDEIKKAVKEANAyefIMKLPQKFDTLvgerGAQLSGGQKQRIAIARAL 547
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA 588
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
111-332 |
2.13e-35 |
|
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: 136.90 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 332
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
395-597 |
3.91e-35 |
|
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: 133.43 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFnvnylREIIGV 474
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQEPVL---FSTTIAENI---CYGRGNVTMdEIKKAVKEA--NAYEFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARA 546
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGHKGLFR-RLSKADKAKvdEALER-VGLSELADRQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA 597
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
412-629 |
4.75e-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: 134.00 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLF-STTIAENI 490
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CYGRGNVTMD--EIKKAVKEANAYEFImklpqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 568
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLEIAEMLGI-------DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 569 AEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGshselmKKEGVYFKLVN 629
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVG------KPEEVFKKPKN 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
987-1215 |
5.84e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.20 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGTVLLDGQEAK-KLNVQwlR 1062
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 AQLGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIvsAAKAA------NIHPFIETLPHkyetrvgdkgtQLSGGQKQR 1135
Cdd:COG1118 75 RRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEI--RARVEellelvQLEGLADRYPS-----------QLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1136 IAIARALIRQPQILLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVFQNGRVKE 1205
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
250
....*....|
gi 9961252 1206 HGTHQQLLAQ 1215
Cdd:COG1118 215 VGTPDEVYDR 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1004-1203 |
8.89e-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: 132.27 E-value: 8.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF-DCSIA 1080
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIAYGD-NSRVVSQDEIVSAAKaanihpfietlphKYETRVG--DKGT----QLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:cd03262 95 ENITLAPiKVKGMSKAEAEERAL-------------ELLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1154 ATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:cd03262 162 PTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-1224 |
9.28e-35 |
|
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: 145.05 E-value: 9.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 401 FSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnvnylreiIGVVSQEPV 480
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 481 LFSTTIAENICYGrgnVTMDEIK--KAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 559 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVY------------- 624
Cdd:TIGR01271 575 PFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdnf 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 625 ------------------------------------------------------------FKLVNMQTSGSQIQSEE--- 641
Cdd:TIGR01271 655 saerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVQMGPQKAQATTIEdav 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 642 -------FEL---NDEKAATRMAPNGWKSRL--------------------------FRHSTQKNLKNSQMCQKS--LDV 683
Cdd:TIGR01271 735 repserkFSLvpeDEQGEESLPRGNQYHHGLqhqaqrrqsvlqlmthsnrgenrreqLQTSFRKKSSITQQNELAseLDI 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 684 ETDGL------------------------EANVPPV----SFLKVLKLNKTewPYFVVGTVCAIANGGLQPAFSVIFseI 735
Cdd:TIGR01271 815 YSRRLskdsvyeiseeineedlkecfadeRENVFETttwnTYLRYITTNRN--LVFVLIFCLVIFLAEVAASLLGLW--L 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 736 IAIFGPGDDAVKQQKCNIFSLIFLFLGII----SFFTF--------------FLQGFTFGKAGEILTRRLRSMAFKAMLR 797
Cdd:TIGR01271 891 ITDNPSAPNYVDQQHANASSPDVQKPVIItptsAYYIFyiyvgtadsvlalgFFRGLPLVHTLLTVSKRLHEQMLHSVLQ 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 798 QDMSWFDDHKnsTGALSTRLATDAAQVQGATG-TRLALIAQNIANLGTGIIISFIYGWqltlLLLAVVPIIAVSGIVEMK 876
Cdd:TIGR01271 971 APMAVLNTMK--AGRILNRFTKDMAIIDDMLPlTLFDFIQLTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAY 1044
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 877 LLAGNAKRDKKELEAAGKIATEAIENIR---TVVSLTQERKFESMYVEKL---------------YGPYRV-------FS 931
Cdd:TIGR01271 1045 FLRTSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALnlhtanwflylstlrWFQMRIdiifvffFI 1124
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 932 AIVFGAVAlghASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGL------------------KPDK----------- 982
Cdd:TIGR01271 1125 AVTFIAIG---TNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLmrsvsrvfkfidlpqeepRPSGgggkyqlstvl 1201
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 983 ------------FEGNITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPlAGTVLLDG 1050
Cdd:TIGR01271 1202 vienphaqkcwpSGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDG 1279
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1051 QEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSG 1130
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSN 1356
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1131 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQ 1210
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQ 1436
|
1050
....*....|....
gi 9961252 1211 QLLAQKGIYFSMVS 1224
Cdd:TIGR01271 1437 KLLNETSLFKQAMS 1450
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
408-617 |
9.64e-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: 133.13 E-value: 9.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 408 NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLFS-TTI 486
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENICYG--RGNVTMDEIKKAVKEAnayefiMKLPQkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:cd03300 90 FENIAFGlrLKKLPKAEIKERVAEA------LDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 565 TESEAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03300 163 LKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
987-1214 |
1.36e-34 |
|
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: 132.81 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILF-DCSIAENIAYGDNSRVVSQDEIvsAAKAANIHPFIETLPHKYETRVGDkgtQLSGGQKQRIAIARALIRQ 1145
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKI--RERADELLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
987-1207 |
2.48e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.33 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRA 1063
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQDEIVSAAKAAnihpfIET--LPHKYETRVGdkgtQLSGGQKQR 1135
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREV-----LDLvgLSDKAKALPH----ELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1136 IAIARALIRQPQILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVFQNGRVKEHG 1207
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
392-628 |
2.95e-34 |
|
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: 132.34 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYPSraNVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIAENICYGRgNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELM-KKEGVYFKLV 628
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
406-618 |
3.33e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 134.47 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI---IGVVSQEPvlF 482
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 483 S---------TTIAENICYgRGNVTMDEIKKAVKEA------NAyEFIMKLPQKFdtlvgergaqlSGGQKQRIAIARAL 547
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 548 VRNPKILLLDEATSALDTESEAEV-------QAALdkareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
410-612 |
3.56e-34 |
|
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: 130.88 E-value: 3.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQ---SGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ---DIR-NFNVNYLREIIGVVSQEPVLF 482
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 483 S-TTIAENICYGRGNVTMDEIKKAVKEANAYefiMKLpqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:cd03297 88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961252 562 ALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
392-634 |
1.13e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 141.80 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYpsRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIAENI-CYGRGNVTmdEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdPFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYF-KLV 628
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFsKMV 1471
|
....*.
gi 9961252 629 nmQTSG 634
Cdd:PLN03130 1472 --QSTG 1475
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-619 |
1.85e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDE----IKKAVKEANAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1004-1213 |
2.29e-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: 128.99 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1082
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAYGDNSRVVSQDEIvsAAKAANIHPF--IETLPHKYETRvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEATSALDT 1160
Cdd:cd03299 92 IAYGLKKRKVDKKEI--ERKVLEIAEMlgIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1161 ESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:cd03299 163 RTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
394-618 |
2.36e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 129.44 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDV--HFsypsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNyLREI 471
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 ---IGVVSQEPVLFSTTIA-ENICYG----RGnvtmdeIKKAVKEANAYEFIMKlpqkfdtlVG--ERG----AQLSGGQ 537
Cdd:PRK09493 76 rqeAGMVFQQFYLFPHLTAlENVMFGplrvRG------ASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 615
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQ 221
|
...
gi 9961252 616 ELM 618
Cdd:PRK09493 222 VLI 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
394-613 |
2.53e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.15 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-----NVNyl 468
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVN-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 reiigVVSQEPVLFS-TTIAENICYG--RGNVTMDEIKKAVKEAnayefiMKLPQkFDTLVGERGAQLSGGQKQRIAIAR 545
Cdd:PRK09452 90 -----TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALdKA--RE-GRTTIVIAH----RLSTvrnADVIAGFEDGVIVEQGS 613
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
987-1212 |
3.53e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.12 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQeakklNVQWLRAQ-- 1064
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPKdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 -LGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPhkyetrvgdkgTQLSGGQKQRIAI 1138
Cdd:COG3839 76 nIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIdrrvREAAELLGLEDLLDRKP-----------KQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1139 ARALIRQPQILLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGT 1208
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
....
gi 9961252 1209 HQQL 1212
Cdd:COG3839 218 PEEL 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
410-1223 |
3.74e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 139.91 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInidgqdirnfnvnYLREIIGVVSQEPVLFSTTIAEN 489
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 490 ICYgrgnvtMDE-----IKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PTZ00243 741 ILF------FDEedaarLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 565 TE-SEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEgVYFKL-----VNMQTSGSQIQ 638
Cdd:PTZ00243 815 AHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLaaelkENKDSKEGDAD 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 639 SEEFELNDEKAATRMaPNGWKSRLFRHSTQKNLKNSQMCQKSLDVETDGLEANVPPVSFLKVLKLnktewpyfvVGTVCA 718
Cdd:PTZ00243 894 AEVAEVDAAPGGAVD-HEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRF---------CGGLHA 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 719 IanGGLQPAFSVifSEIIAI-------------FGPGDDavkqqkcnIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTR 785
Cdd:PTZ00243 964 A--GFVLATFAV--TELVTVssgvwlsmwstrsFKLSAA--------TYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSR 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFiygWQLTLLLLAVVP 865
Cdd:PTZ00243 1032 NMHRDLLRSVSRGTMSFFD--TTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTS---ASQPFVLVALVP 1106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 866 ------------------IIAVSGIVEMKL--LAGNAKRDKKELEAAGK---IATEAIENIRTVVSltqerkfeSMYVEK 922
Cdd:PTZ00243 1107 cgylyyrlmqfynsanreIRRIKSVAKSPVftLLEEALQGSATITAYGKahlVMQEALRRLDVVYS--------CSYLEN 1178
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 923 LYGPY---RV--FSAIVFGAVAL-------GHASSfaPDYAKAKLSAAHLFMLFE------RQ----------------- 967
Cdd:PTZ00243 1179 VANRWlgvRVefLSNIVVTVIALigvigtmLRATS--QEIGLVSLSLTMAMQTTAtlnwlvRQvatveadmnsverllyy 1256
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 968 ---------PLIDSY-----SEEGLKPDKF-------------------EGNITFNEVVFNYptRANVP-VLQGLSLEVK 1013
Cdd:PTZ00243 1257 tdevphedmPELDEEvdaleRRTGMAADVTgtvviepasptsaaphpvqAGSLVFEGVQMRY--REGLPlVLRGVSFRIA 1334
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1014 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVS 1093
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEAS 1411
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1094 QDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALI-RQPQILLLDEATSALDTESEKVVQEALDK 1172
Cdd:PTZ00243 1412 SAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMS 1491
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1173 AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL-LAQKGIYFSMV 1223
Cdd:PTZ00243 1492 AFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
395-612 |
4.70e-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: 126.40 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQepvlfsttiaenicygrgnvtmdeikkAVKEANAYEFIMKLpqkFDTLvgergaqlSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNEL--------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 555 LLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 612
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
996-1215 |
5.29e-33 |
|
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: 130.56 E-value: 5.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 996 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GTVLLDGQEAKKLNVQWLRA----QLGI 1067
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1068 VSQEP---------ILFdcSIAENI-AYGDNSRVVSQDEIVSAAKAANIHPFIETL---PHkyetrvgdkgtQLSGGQKQ 1134
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1135 RIAIARALIRQPQILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1207
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233
|
....*...
gi 9961252 1208 THQQLLAQ 1215
Cdd:COG0444 234 PVEELFEN 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1001-1212 |
8.67e-33 |
|
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: 127.35 E-value: 8.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAkkLNVQWLRAQLGIVSQEPILF-DCSI 1079
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1160 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1212
Cdd:cd03300 163 LKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
987-1203 |
1.08e-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: 124.82 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLG 1066
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILF-DCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtQLSGGQKQRIAIARALIRQ 1145
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
998-1197 |
1.12e-32 |
|
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: 126.05 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-D 1076
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIA-----YGdnsRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9961252 1152 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1197
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
411-617 |
1.40e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.56 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI---RNFN-----VNYLREIIGVVSQEPVLF 482
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 483 S-TTIAENICygRGNVTMDEIKKAVKEANAYEFIMKLpqkfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK11264 98 PhRTVLENII--EGPVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 559 ATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
987-1215 |
1.49e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLnvqwlRAQLG 1066
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQE-------PIlfdcSIAENIAYGDNSRV-------VSQDEIVSAA-KAANIHPFIETlphkyetRVGdkgtQLSGG 1131
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrpsRADREAVDEAlERVGLEDLADR-------PIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFqNGRVKEHGTH 1209
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 9961252 1210 QQLLAQ 1215
Cdd:COG1121 223 EEVLTP 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1002-1215 |
1.83e-32 |
|
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: 127.76 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPILF-D 1076
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYGDNSRVVSQDEIVSAA----KAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1153 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
394-617 |
3.66e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFST-TIAENICYGR---GNVTMDEiKKAVKEANAyefIMK---LPQKFDTLVGErgaqLSGGQKQRIAIAR 545
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGReprRGGLIDW-RAMRRRARE---LLArlgLDIDPDTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 546 ALVRNPKILLLDEATSALdteSEAEVQAALD-----KAReGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1129 154 ALSRDARVLILDEPTASL---TEREVERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
394-618 |
4.17e-32 |
|
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: 124.85 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY-LREII 472
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFST-TIAENICYGRGNVTMDEIKKAVKEAnaYEFIMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNP 551
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQGSHSELM 618
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELL 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
998-1212 |
6.02e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.93 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1074
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FDC-----SIAENIAYG-DNSRVVSQDEIvsAAKAANI-------HPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARA 1141
Cdd:COG4608 105 YASlnprmTVGDIIAEPlRIHGLASKAER--RERVAELlelvglrPEHADRYPH-----------EFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1142 LIRQPQILLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:COG4608 172 LALNPKLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
987-1203 |
6.89e-32 |
|
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: 124.99 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE---AKKLNVQWLRA 1063
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEPILFD-CSIAENIAYGDNSRV---------VSQDEIVSAAKAanihpfIET--LPHKYETRVGdkgtQLSGG 1131
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQRALAA------LERvgLLDKAYQRAD----QLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1203
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1002-1203 |
9.87e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQ-LGI--VSQEPILF-DC 1077
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQaAGIaiIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYGD---NSRVVSQDEIVSAAKAA------NIHPfietlphkyETRVGDkgtqLSGGQKQRIAIARALIRQPQI 1148
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlglDIDP---------DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1149 LLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:COG1129 162 LILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
394-617 |
1.15e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.89 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD--PD---EGTINIDGQDIRNFNVNY- 467
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 -LREIIGVVSQEPVLFSTTIAENICYG------RGNVTMDE-IKKAVKEANAYEFIMKlpQKFDTLVGergaqLSGGQKQ 539
Cdd:PRK14239 83 dLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
412-617 |
1.86e-31 |
|
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: 123.60 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLFS-TTIAENI 490
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CYG------RGNVTMDEIKKAVKEanayefIMKLPQkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:cd03296 96 AFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 565 TESEAEVQAALDKARE--GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03296 169 AKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-618 |
2.49e-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: 130.19 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN--------VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLyDPDEGTINIDGQDIRNFNV 465
Cdd:COG4172 276 LEARDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLREI---IGVVSQEPvlFST-----TIAENICYG----RGNVTMDEIKKAVKEA-----------NAY--EFimklpq 520
Cdd:COG4172 355 RALRPLrrrMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRYphEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 521 kfdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTV 594
Cdd:COG4172 427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*
gi 9961252 595 RN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
393-621 |
2.57e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.94 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 393 NLEFNDVHFSYPSRAnvkilKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVnYLREIi 472
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICYG---RGNVTMDEiKKAVKEANA----YEFIMKLPqkfdtlvgergAQLSGGQKQRIAIA 544
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGlrpGLKLTAEQ-RAQVEQALErvglAGLLDRLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
992-1207 |
3.02e-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: 121.00 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 992 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQe 1071
Cdd:cd03214 5 LSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 pilfdcsiaeniaygdnsrvvsqdeivsAAKAANIHPFIetlphkyetrvgDKG-TQLSGGQKQRIAIARALIRQPQILL 1150
Cdd:cd03214 81 ----------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1151 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1207
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1001-1212 |
3.60e-31 |
|
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: 122.83 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSI 1079
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYG----DNSRVVSQDEIvsAAKAANIHPFI--ETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:cd03296 92 FDNVAFGlrvkPRSERPPEAEI--RAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1154 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1212
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
987-1215 |
5.41e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.69 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPhkyetrvgdkgTQLSGGQKQRIAIAR 1140
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1141 ALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
394-617 |
5.77e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.65 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL--REI 471
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEP--VLFSTTIAENICYGRGNV--TMDEIKKAVKEA------NAYEfiMKLPQkfdtlvgergaQLSGGQKQRI 541
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavgmEGFE--NKPPH-----------HLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 542 AIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1003-1208 |
6.14e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.22 E-value: 6.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAE 1081
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSA 1157
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1158 LDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:PRK09452 175 LDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
410-619 |
6.18e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--RNFNVNYLREIIGVVSQEP--VLFSTT 485
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 486 IAENICYGRGNVTM--DEIKKAVKEANAyefIMKLPqkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 563
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 564 DTESEAEVQAALDKARE--GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1005-1203 |
7.74e-31 |
|
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: 121.25 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-D 1076
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYG-----DNSRVVSQDEIVSAAkaaNIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1152 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
998-1215 |
8.27e-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: 128.65 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPLAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1074
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FDC-----SIAENIAYG------DNSRVVSQDEIVSAAKAANIHPfiETL---PHkyetrvgdkgtQLSGGQKQRIAIAR 1140
Cdd:COG4172 372 FGSlsprmTVGQIIAEGlrvhgpGLSAAERRARVAEALEEVGLDP--AARhryPH-----------EFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1141 ALIRQPQILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:COG4172 439 ALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 9961252 1214 AQ 1215
Cdd:COG4172 515 DA 516
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
989-1207 |
8.34e-31 |
|
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: 121.10 E-value: 8.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 989 FNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLnvqwlRAQLGIV 1068
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1069 SQEPIL---FDCSIAENIAYGDNSRVVSQdEIVSAAKAANIHPFIET--LPHKYETRVGdkgtQLSGGQKQRIAIARALI 1143
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLF-RRLSKADKAKVDEALERvgLSELADRQIG----ELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFqNGRVKEHG 1207
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
394-600 |
1.05e-30 |
|
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: 120.28 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlREIIG 473
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENIC-----YGRgNVTMDEIKKAVKEanayefiMKLPQKFDTLVGergaQLSGGQKQRIAIARAL 547
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNADVI 600
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
398-589 |
1.15e-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: 120.44 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 398 DVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdiRNFNVNYLREIIGVVSQ 477
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 478 EP--VLFSTTIAENICYGRGNVTMD--EIKKAVKEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961252 554 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 589
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
994-1224 |
1.25e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.54 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 994 FNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1071
Cdd:PRK13647 12 FRYKdgTKA----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 P--ILFDCSIAENIAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQ 1145
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGPVNMGLDKDEVERrveeALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG-----THQQLLAQKGI 1218
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
|
....*.
gi 9961252 1219 YFSMVS 1224
Cdd:PRK13647 237 RLPLVA 242
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
714-947 |
1.44e-30 |
|
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: 122.67 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 714 GTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVkqqkcNIFSLIFLFLGII---SFFTFFlQGFTFGKAGEILTRRLRSM 790
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD-----VLNELALILLAIYllqSVFTFV-RYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 791 AFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS 870
Cdd:cd18557 75 LFSSLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 871 GIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRV-FSAIVFGAVALGhASSFA 947
Cdd:cd18557 153 SKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLaRKKALANALFQG-ITSLL 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
394-617 |
1.53e-30 |
|
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: 120.30 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENICY-----GRGNVTMDEikkavkEANAYEFIMKLPQKFDTLVGergaQLSGGQKQRIAIARAL 547
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
85-331 |
1.62e-30 |
|
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: 122.62 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 85 FVDTAGNFSFPVNF--SLSLLNPGKILEEEMTRYAYYYSGLGAGVLV----AAYIQVSFWTLAAGRQIRKIRQKFFHAIL 158
Cdd:cd18573 6 LVSSAVTMSVPFAIgkLIDVASKESGDIEIFGLSLKTFALALLGVFVvgaaANFGRVYLLRIAGERIVARLRKRLFKSIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 159 RQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKIL 238
Cdd:cd18573 86 RQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 239 SAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWY 318
Cdd:cd18573 166 RKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYY 245
|
250
....*....|...
gi 9961252 319 GSTLVISKEYTIG 331
Cdd:cd18573 246 GGSLVASGELTVG 258
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
394-617 |
1.92e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1002-1214 |
2.11e-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: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1078
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIaygdnsrvvsqdeiVSAAKAANIHPFIETLPHKYE------TRVGDKGTQLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:cd03224 92 VEENL--------------LLGAYARRRAKRKARLERVYElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1153 EATSALdteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVFQNGRVKEHGTHQQLLA 1214
Cdd:cd03224 158 EPSEGL---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
974-1231 |
2.15e-30 |
|
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: 130.84 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 974 SEEGLKPDKFE--------GN-ITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG 1044
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgeGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1045 TVLLDGQEAkklnvqwlraqlgIVSQEPILFDCSIAENIAYGdnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDK 1124
Cdd:TIGR00957 694 HVHMKGSVA-------------YVPQQAWIQNDSLRENILFG---KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1125 GTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVFQNG 1201
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
250 260 270
....*....|....*....|....*....|
gi 9961252 1202 RVKEHGTHQQLLAQKGIYFSMVSVQAGTQN 1231
Cdd:TIGR00957 838 KISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
987-1208 |
3.45e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 122.99 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPLAGTVLLDGQEAKKLNVQWLR 1062
Cdd:PRK11153 2 IELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 A---QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQDEIvsaakAANIHPFIEtlphkyetRVG--DKG----TQ 1127
Cdd:PRK11153 79 KarrQIGMIFQHfNLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1128 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVFQNGRVK 1204
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLV 220
|
....
gi 9961252 1205 EHGT 1208
Cdd:PRK11153 221 EQGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
987-1183 |
1.01e-29 |
|
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: 117.89 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRA 1063
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQE-PILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIETLPHKYETRvgDKGTQLSGGQKQRIAIARAL 1142
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9961252 1143 IRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1183
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
394-617 |
1.39e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.43 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
394-609 |
1.76e-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: 115.60 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQepvlfsttiaenicygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPK 552
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 553 ILLLDEATSALdteSEAEVQAALD----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 609
Cdd:cd03216 103 LLILDEPTAAL---TPAEVERLFKvirrLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-604 |
1.93e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.60 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD-----EGTINIDGQDI--RNFNVN 466
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 YLREIIGVVSQEPVLFSTTIAENICYG------RGNVTMDEI-KKAVKEANAYEFIMKLPQKfdtlvgeRGAQLSGGQKQ 539
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFE 604
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
711-923 |
2.73e-29 |
|
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: 119.19 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDavkQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSM 790
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 791 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS 870
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 871 GIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKL 923
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREAN 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
394-621 |
4.03e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDE---GTINIDGQDIRNFNVNYLRE 470
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEANA----YEFIMKLPQkfdtlvgergaQLSGGQKQRIA 542
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 9961252 621 E 621
Cdd:PRK13640 234 V 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1004-1208 |
4.56e-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: 116.77 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLGIVS--QEPILF-DCSIA 1080
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIA--------YGDNSRVVSQDEIVSAAKAANIhpfIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILL 1150
Cdd:cd03219 94 ENVMvaaqartgSGLLLARARREEREARERAEEL---LERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1151 LDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1208
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1001-1203 |
5.66e-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: 114.06 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQ-LGIvsqepilfdcsi 1079
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 aeniaygdnsrvvsqdeivsaakaANIHpfietlphkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSAL- 1158
Cdd:cd03216 78 ------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 1159 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
394-623 |
8.07e-29 |
|
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: 115.85 E-value: 8.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylrEI-- 471
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH---RIar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 --IGVVSQEPVLFST-TIAENI---CYGRGNvtmdeiKKAVKEAnaYEFIMKLpqkFDTLvGER----GAQLSGGQKQRI 541
Cdd:COG0410 78 lgIGYVPEGRRIFPSlTVEENLllgAYARRD------RAEVRAD--LERVYEL---FPRL-KERrrqrAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 542 AIARALVRNPKILLLDEATSALdteseA-----EVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQG 612
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEG 218
|
250
....*....|.
gi 9961252 613 SHSELMKKEGV 623
Cdd:COG0410 219 TAAELLADPEV 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
394-621 |
9.44e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
394-621 |
1.09e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.77 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVKiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
125-364 |
2.31e-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: 116.43 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 125 AGVLVA----AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVA 200
Cdd:cd18576 43 LGLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 201 TFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 280
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 281 KHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIGAfSVGQAAPCIDAFAN 359
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQK 281
|
....*
gi 9961252 360 ARGAA 364
Cdd:cd18576 282 ALGAS 286
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
394-621 |
2.65e-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: 114.80 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEG-TINIDGQDIRNFNVNYLREII 472
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVS---QEPVLFSTTIAENICYGR-------GNVTMDEIKKAVKEANAYEFimklpqkfDTLVGERGAQLSGGQKQRIA 542
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARELLELLGL--------AHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGF------EDGVIVEQGSH 614
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGRVVAAGPK 227
|
....*..
gi 9961252 615 SELMKKE 621
Cdd:COG1119 228 EEVLTSE 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1004-1204 |
2.81e-28 |
|
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: 113.51 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeaKKLNVQWLRAQLGIVSQEP--ILFDCSIAE 1081
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:cd03226 92 ELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961252 1162 SEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK 1204
Cdd:cd03226 161 NMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
986-1215 |
2.83e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITFNEVVFNYPTRAnvpvLQgLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVqwlrAQ- 1064
Cdd:COG3840 1 MLRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 -LGIVSQEPILFD-CSIAENIAYGDNSR----VVSQDEIVSAAKAANIHPFIETLPhkyetrvgdkgTQLSGGQKQRIAI 1138
Cdd:COG3840 72 pVSMLFQENNLFPhLTVAQNIGLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1139 ARALIRQPQILLLDEATSALD----TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
..
gi 9961252 1214 AQ 1215
Cdd:COG3840 219 DG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1001-1207 |
2.99e-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: 113.50 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ-----EAKKLNVqwlraqlGIVSQEPILF 1075
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 -DCSIAENIAYGDNSRVVSQDEIV----SAAKAANIhpfiETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILL 1150
Cdd:cd03301 85 pHMTVYDNIAFGLKLRKVPKDEIDervrEVAELLQI----EHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1151 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1207
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
712-929 |
3.54e-28 |
|
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: 115.81 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 712 VVGTVCAIAnggLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFfLQGFTFGKAGEILTRRLRSMA 791
Cdd:cd18780 6 LVSSGTNLA---LPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATF-LRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 792 FKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSG 871
Cdd:cd18780 82 FSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 872 IVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRV 929
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLL 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
410-618 |
3.58e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR-------------NFNVNYLREIIGVVS 476
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 477 QEPVLFS-TTIAENICygRGNVTMDEIKKAVKEANAYEFIMKLPQKfDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:PRK10619 99 QHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 556 LDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-EDGVIVEQGSHSELM 618
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
987-1213 |
3.62e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.13 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGTVLLDGQ--------EAKKLNV 1058
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1059 QWLRAQLGIVSQEPILFDCSIAENIAYGDN----SRVVSQDEIV-SAAKAANIHPFIETLPHKyetrvgdKGTQLSGGQK 1133
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVeSALKDADLWDEIKHKIHK-------SALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1134 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQN-----GRVKE 1205
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236
|
....*...
gi 9961252 1206 HGTHQQLL 1213
Cdd:PRK14258 237 FGLTKKIF 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
394-610 |
4.39e-28 |
|
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: 113.68 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL---- 468
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 REIIGVVSQ-EPVLFSTTIAENicygrgnVTM--------DEIKKAVKEANAYEfimklpqkfdtlVGERG----AQLSG 535
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALEN-------VMLplelagrrDARARARALLERVG------------LGHRLdhypAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 536 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVE 610
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
987-1214 |
4.40e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.08 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN-VQWLRAQL 1065
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpFIETLPHKYETRvgdKGTQLSGGQKQRIAIARALI 1143
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
394-609 |
4.71e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 121.37 E-value: 4.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPS-RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL---- 468
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 REIIGVVSQEPVLFSTTIAENicygrgNVTMDEI----KKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQ------NVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIV 609
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
987-1213 |
5.42e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.65 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAK--KLNVQWLRAQ 1064
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 LGIVSQEPILFDCSIA-ENIAYGDNSrvvsqdeiVSAAKAANIHPFIETLPHK--YETRVGDKGTQLSGGQKQRIAIARA 1141
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1142 LIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLL 1213
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-591 |
6.66e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.41 E-value: 6.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVH--FsYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYLRE 470
Cdd:COG1101 2 LELKNLSktF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 -----IIGVVSQEPVL---FSTTIAEN--ICYGRGN-------VT---MDEIKKAVKEANayefiMKLPQKFDTLVGerg 530
Cdd:COG1101 76 ykrakYIGRVFQDPMMgtaPSMTIEENlaLAYRRGKrrglrrgLTkkrRELFRELLATLG-----LGLENRLDTKVG--- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 531 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRL 591
Cdd:COG1101 148 -LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1005-1215 |
9.31e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.72 E-value: 9.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA-----GTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1077
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYGD--NSRVVSQDEIV--SAAKAAnihpfietLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVerSLRQAA--------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1154 ATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1000-1201 |
1.06e-27 |
|
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: 112.42 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVL----LDGQEAKKLNVQWLRAQLGIVSQEPILF 1075
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DCSIAENIAYGDNsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEAT 1155
Cdd:cd03290 92 NATVEENITFGSP---FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961252 1156 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNG 1201
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
267-590 |
1.41e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.14 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 267 IAF-GGQNKELERYQKHLENAKEIgIKKAISANISMGiAFLLIYASYALAFWY--GSTLVISKEYTIGNAMTV--FFSIL 341
Cdd:COG4178 234 IALyRGEAAERRRLRRRFDAVIAN-WRRLIRRQRNLT-FFTTGYGQLAVIFPIlvAAPRYFAGEITLGGLMQAasAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 342 IGAFSVgqaapCIDAFAN-ARGAAYVI-----FDIIDNNPKIDSFSERGHKPDSikGNLEFNDVHFSYPSRAnvKILKGL 415
Cdd:COG4178 312 QGALSW-----FVDNYQSlAEWRATVDrlagfEEALEAADALPEAASRIETSED--GALALEDLTLRTPDGR--PLLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINI-DGQDIrnfnvnyLreiigVVSQEPVLFSTTIAENICY-- 492
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-----FLPQRPYLPLGTLREALLYpa 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 493 GRGNVTMDEIKKAVKEANayefIMKLPQKFDTlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 572
Cdd:COG4178 451 TAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
330
....*....|....*...
gi 9961252 573 AALDKAREGRTTIVIAHR 590
Cdd:COG4178 526 QLLREELPGTTVISVGHR 543
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
393-615 |
1.86e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 393 NLEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFN-------V 465
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSqkpsekaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLREIIGVVSQE----PVLfstTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLvgerGAQLSGGQKQRI 541
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 542 AIARALVRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 615
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
394-620 |
2.17e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.34 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRA--NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN-YLRE 470
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 I---IGVVSQ--EPVLFSTTIAENICYGRGNVTMDeikkaVKEANAYEFIMKLPQKFDTLVGERGA-QLSGGQKQRIAIA 544
Cdd:PRK13646 83 VrkrIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-----LDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
998-1161 |
2.45e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPIL 1074
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FD-CSIAENIAYG---DNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILL 1150
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 9961252 1151 LDEATSALDTE 1161
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1005-1215 |
2.65e-27 |
|
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: 114.81 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPLAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEP 1072
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1073 ILFD-CSIAENIAYG-----DNSRVVSQDEIVsaaKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQP 1146
Cdd:COG4148 87 RLFPhLSVRGNLLYGrkrapRAERRISFDEVV---ELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1147 QILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:COG4148 153 RLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
987-1215 |
3.90e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNY---PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQW-LR 1062
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 AQLGIVSQEPilfDCSIA-----ENIAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHkyetrvgdkgtQLSGGQK 1133
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1134 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQ 1211
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 9961252 1212 LLAQ 1215
Cdd:PRK13633 231 IFKE 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
394-612 |
4.27e-27 |
|
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: 109.56 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHF---SYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDGQDIRNFNvnyL 468
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 REIIGVVSQEPVLFST-TIAENIcygrgnvtmdeikkavkeanayEFIMKLpqkfdtlvgeRGaqLSGGQKQRIAIARAL 547
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQG 612
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQG 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
415-620 |
4.51e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlREIIgVVSQEPVLFS-TTIAENICYG 493
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDIC-MVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 494 RG--NVTMDEIKKAVKEANAyefIMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEV 571
Cdd:PRK11432 103 LKmlGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLSNLD----ANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 572 QAAL-DKARE-----GRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:PRK11432 172 RRSMrEKIRElqqqfNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
409-623 |
6.84e-27 |
|
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: 110.60 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylrEI----IGVVSQEPVLFST 484
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIarlgIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 -TIAENI-----CYGRGNVTMDEIKKAVKEAN--AYEFI--MKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03219 90 lTVLENVmvaaqARTGSGLLLARARREEREARerAEELLerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 555 LLDEATSALdteSEAEVQAALDK----AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEGV 623
Cdd:cd03219 166 LLDEPAAGL---NPEETEELAELirelRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1000-1215 |
6.95e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.14 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPilfd 1076
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 csiaeniaYGD-NSR-VVSQ---------DEIVSAAKAANIHPFIETL----------PHKYetrvgdkgtqlSGGQKQR 1135
Cdd:PRK11308 102 --------YGSlNPRkKVGQileepllinTSLSAAERREKALAMMAKVglrpehydryPHMF-----------SGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1136 IAIARALIRQPQILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
...
gi 9961252 1213 LAQ 1215
Cdd:PRK11308 243 FNN 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-617 |
7.43e-27 |
|
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: 116.71 E-value: 7.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD----EGTINIDGQDIRNFNVNYL 468
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 REI----IGVVSQEPV-----LFS--TTIAENIcygrgnvtmdEIKKAVKEANAYEFIMKLPQkfdtLVGERGA------ 531
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLHTigKQIAEVL----------RLHRGLSGAAARARALELLE----RVGIPDPerrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 532 ---QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFED 605
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 9961252 606 GVIVEQGSHSEL 617
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1005-1208 |
7.96e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.68 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEP--ILFDCSIA 1080
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIAYGDNSRVVSQDEIVSAAKAAnihpfIETLPHKYETrVGDKGT-QLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1160 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1208
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1002-1215 |
8.74e-27 |
|
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: 116.32 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1073
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 -----LFdcSIAENIAygdnsrvvsqdEIVS--------AAKAANIHPFIET-LPHKyETRVGDKGTQLSGGQKQRIAIA 1139
Cdd:COG4172 103 tslnpLH--TIGKQIA-----------EVLRlhrglsgaAARARALELLERVgIPDP-ERRLDAYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1140 RALIRQPQILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:COG4172 169 MALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
...
gi 9961252 1213 LAQ 1215
Cdd:COG4172 245 FAA 247
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
411-610 |
9.41e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.93 E-value: 9.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLREIIGVVSQEPV------- 480
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 481 LFSTTIAENIcygRGNVTMDEikkAVKEANAYEFI--MKLPqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK10419 107 TVREIIREPL---RHLLSLDK---AERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 559 ATSALDTESEAEVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFEDGVIVE 610
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1003-1184 |
1.02e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.78 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKklNVQWLRAQLGIVSQEPILF-DCSIAE 1081
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGdnsrvVSQDEIVSAAKAANIHPFIeTLPHKYETrVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:PRK11607 111 NIAFG-----LKQDKLPKAEIASRVNEML-GLVHMQEF-AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180
....*....|....*....|....*
gi 9961252 1162 SEKVVQ-EALD-KAREGRTCIVIAH 1184
Cdd:PRK11607 184 LRDRMQlEVVDiLERVGVTCVMVTH 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
387-623 |
1.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 387 PDSIkgnLEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFN 464
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 465 VNYLREIIGVVSQEP--VLFSTTIAENICYGRGNVTM--DEIKKAVKEANAYEFIMKLPQKfdtlvgeRGAQLSGGQKQR 540
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
....*.
gi 9961252 618 MKKEGV 623
Cdd:PRK13636 230 FAEKEM 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
394-620 |
1.17e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANV--KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI----RNFNVNY 467
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 LREIIGVVSQ--EPVLFSTTIAENICYGRGN--VTMDEIKKAVKEANAY-----EFIMKLPqkFDtlvgergaqLSGGQK 538
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIELvglpeELLARSP--FE---------LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 539 QRIAIARALVRNPKILLLDEATSALDTESEAEVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
....*.
gi 9961252 615 SELMKK 620
Cdd:PRK13634 231 REIFAD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
992-1214 |
1.25e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 992 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1071
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 P--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpFIETLPHKYETRvgdKGTQLSGGQKQRIAIARALIRQPQIL 1149
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA----LLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1150 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-617 |
1.29e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 408 NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD--PD---EGTINIDGQDIRNFNVNYLREIIGVVSQEPVLF 482
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 483 ST-TIAENICYG----RGNVTMDEIKKAVKEAnayefiMKLPQKFDTL---VGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
394-612 |
1.37e-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: 108.73 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkilKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIG 473
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFS-TTIAENICYGRG------NVTMDEIKKAVKEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARA 546
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
394-612 |
1.63e-26 |
|
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: 108.43 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTvALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAEN----ICYGRGnVTMDEIKKAVKEAnayefiMKLPQKFDTLvGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03264 76 YLPQEFGVYPNFTVREfldyIAWLKG-IPSKEVKARVDEV------LELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
406-611 |
1.65e-26 |
|
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: 110.28 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN----YLREIIGVVSQEPVL 481
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrraFRRDVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 FS--TTIAENICYGRGNVTmdEIKKAVKEANAYEFI--MKLPqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:TIGR02769 101 VNprMTVRQIIGEPLRHLT--SLDESEQKARIAELLdmVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 558 EATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQ 611
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1005-1212 |
1.66e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1077
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYGDNSRVVSQDEIVSAA-----KAANIhpFIETLPHKYETRVGdkgtqLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAvekslKGASI--WDEVKDRLHDSALG-----LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1153 EATSALDTESEKVVQEALDKAREGRTCIVIAHRL---STIqnADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
394-564 |
1.66e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFSTTIAENICYGRgnvtmdEIKKAVKEANAY-EFIMK--LPqkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 9961252 551 PKILLLDEATSALD 564
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
394-589 |
2.07e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.95 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYP-SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylReii 472
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICYG---RGnvtmdeIKKAVKEANAYEFImklpqkfdTLVGERGA------QLSGGQKQRIA 542
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
999-1216 |
2.56e-26 |
|
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: 109.89 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 999 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRA---QLGIVSQepilf 1075
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DC--------SIAENIayGDNSR-VVSQDEIVSAAKAANIHPFIEtLPHKYETRVGdkgTQLSGGQKQRIAIARALIRQP 1146
Cdd:TIGR02769 96 DSpsavnprmTVRQII--GEPLRhLTSLDESEQKARIAELLDMVG-LRSEDADKLP---RQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
407-621 |
2.62e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.33 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVL-FSTT 485
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 486 IAENICYGR-------GNVTMDEiKKAVKEAnayefiMKLPQkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK11231 93 VRELVAYGRspwlslwGRLSAED-NARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 559 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1008-1216 |
2.63e-26 |
|
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: 112.13 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DCSIAEN 1082
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAYG-----DNSRVVSQDEIVsaaKAANIHPFIETLPHKyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEATSA 1157
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVI---ELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1158 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1004-1214 |
2.67e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.07 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV-----LLDGQE---AKKLNVQWLRAQLGIVSQEPILF 1075
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DC-SIAENIAYGDnsrVVSQDEIVSAAKAanihpfietLPHKYETRVGDKGTQ------LSGGQKQRIAIARALIRQPQI 1148
Cdd:PRK11264 98 PHrTVLENIIEGP---VIVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1149 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK11264 166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
426-618 |
2.75e-26 |
|
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: 112.12 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 426 ALVGSSGCGKSTTVQLIQRLYDPDEGTINIDG---QDIRNfNVN---YLREIiGVVSQEPVLFST-TIAENICYGRgnvt 498
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSAR-GIFlppHRRRI-GYVFQEARLFPHlSVRGNLLYGR---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 499 mdeiKKAVKEANAYEFimklpqkfDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 569
Cdd:COG4148 103 ----KRAPRAERRISF--------DEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 570 EVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG4148 171 EILPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
394-619 |
3.56e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.92 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYP--SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR----NFNVNY 467
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 LREIIGVVSQ--EPVLFSTTIAENICYGRGN--VTMDEIKKAvkeanAYEFIMKLPQKfDTLVGERGAQLSGGQKQRIAI 543
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEK-----ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 544 ARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHrlstvrNADVIAGFEDGVIVEQgsHSELMK 619
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVLE--HGKLIK 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
394-622 |
3.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVK---ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-NVNYLR 469
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 470 EIIGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRI 541
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 542 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG------S 613
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGtpkeifK 233
|
....*....
gi 9961252 614 HSELMKKEG 622
Cdd:PRK13633 234 EVEMMKKIG 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1003-1201 |
3.64e-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: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLL-DGQEAkklnvqwlraqLgIVSQEPILFDCSIAE 1081
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVSAAKAANIHPFIETLphkyeTRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9961252 1162 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNG 1201
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1001-1214 |
4.46e-26 |
|
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: 108.15 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DC 1077
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIaygdnsrvvsqdeIVSAAKAANIHPFIETLPHKYET------RVGDKGTQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:COG0410 94 TVEENL-------------LLGAYARRDRAEVRADLERVYELfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1152 DEATSALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:COG0410 161 DEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
987-1212 |
5.73e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.69 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPI-LFDCSIAE-NIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIAR 1140
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1141 ALIRQPQILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1004-1215 |
7.56e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1082
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAYGDNSRVVSQDEIVSAAKAAnihpfIETLP-HKYETRVGDkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEA-----LELVDlAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1162 SEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK11432 171 LRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
394-624 |
1.02e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.80 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFND--VHFSYPSR--------ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF 463
Cdd:PRK15079 9 LEVADlkVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 464 NVNYLREI---IGVVSQEPvLFSTT--------IAENICYGRGNVTMDEIKKAVKEanayeFIMK---LPQkfdtLVGER 529
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDP-LASLNprmtigeiIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 530 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLSTVRNadviagFEDGV 607
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKH------ISDRV 232
|
250
....*....|....*...
gi 9961252 608 IVEQGSHS-ELMKKEGVY 624
Cdd:PRK15079 233 LVMYLGHAvELGTYDEVY 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
393-564 |
1.36e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 393 NLEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYL---- 468
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-----VNELepad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 469 REIiGVVSQEPVLFS-TTIAENICYG---RGnVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK11650 76 RDI-AMVFQNYALYPhMSVRENMAYGlkiRG-MPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 9961252 545 RALVRNPKILLLDEATSALD 564
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
987-1184 |
1.45e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.26 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYP-TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEakklnVQWLRAQL 1065
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSAAkaanihpfietlpHKYETRVGDKGT------QLSGGQKQRIAI 1138
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-------------EELLALVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961252 1139 ARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1184
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
395-621 |
1.46e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.09 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQEPVLFST-TIAENICYGR-----GNVTmDEIKKAVKEANAYEFIMKLPQKF-DtlvgergaQLSGGQKQRIAIARAL 547
Cdd:COG4604 80 LRQENHINSRlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 9961252 621 E 621
Cdd:COG4604 227 E 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
412-603 |
2.03e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.18 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD-----PDEGTINIDGQDIRNFNVN--YLREIIGVVSQEPVLFST 484
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 TIAENICYG------RGNvtMDE-IKKAVKEANAY-EFIMKLPQKfdtlvgerGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK14243 106 SIYDNIAYGaringyKGD--MDElVERSLRQAALWdEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961252 557 DEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGF 603
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFF 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
394-615 |
2.33e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirNFN--------- 464
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 465 VNYLREIIGVVSQEPVLFS-TTIAENI----CYGRGnvtMDEiKKAVKEANAYEFIMKLPQKFDTLvgerGAQLSGGQKQ 539
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPhLTVQQNLieapCRVLG---LSK-DQALARAEKLLERLRLKPYADRF----PLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 615
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
397-617 |
2.65e-25 |
|
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: 107.25 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 397 NDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnvnylreiIGVVS 476
Cdd:cd03291 38 NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 477 QEPVLFSTTIAENICYGrgnVTMDEI--KKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03291 105 QFSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 555 LLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
987-1216 |
3.52e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ--EAKKLNVQWLR 1062
Cdd:PRK13636 6 LKVEELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 AQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKyetrvgdKGTQLSGGQKQRIAIAR 1140
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1141 ALIRQPQILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
.
gi 9961252 1216 K 1216
Cdd:PRK13636 233 K 233
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
752-923 |
3.57e-25 |
|
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: 107.21 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR 831
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 832 LALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQ 911
Cdd:cd18573 119 LSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAA 198
|
170
....*....|..
gi 9961252 912 ERKFESMYVEKL 923
Cdd:cd18573 199 ERKEVERYAKKV 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1008-1207 |
3.89e-25 |
|
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: 104.50 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAENIAYG 1086
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1087 DNSRV----VSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1162
Cdd:cd03298 95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961252 1163 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-595 |
4.50e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPS-RANVKIlkglNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFNVNyLRE 470
Cdd:COG3845 6 LELRGITKRFGGvVANDDV----SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDA-IAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFST-TIAENICYGR-----GNVTMDEIKKAVKE-ANAYEFIMKLpqkfDTLVGergaQLSGGQKQRIAI 543
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLeptkgGRLDRKAARARIRElSERYGLDVDP----DAKVE----DLSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961252 544 ARALVRNPKILLLDEATSALdTESEA-EVQAALDK-AREGRTTIVIAHRLSTVR 595
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-TPQEAdELFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
987-1214 |
5.72e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLL------DGQEAKKL 1056
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1057 NVqwLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIET--LPHKYETRvgdKGTQLSGGQ 1132
Cdd:PRK13634 81 KP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1133 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1208
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*.
gi 9961252 1209 HQQLLA 1214
Cdd:PRK13634 230 PREIFA 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
392-629 |
5.94e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.34 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYpsRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIaenicygRGNV------TMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTV-------RQNVdpfleaSSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 545 RALV-RNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL-MKKEG 622
Cdd:PTZ00243 1458 RALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQS 1537
|
....*..
gi 9961252 623 VYFKLVN 629
Cdd:PTZ00243 1538 IFHSMVE 1544
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
393-612 |
5.96e-25 |
|
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: 104.66 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 393 NLEFNDVhFSYPSRAN--VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDE---GTINIDGQDIRNFNVny 467
Cdd:cd03234 3 VLPWWDV-GLKAKNWNkyARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 lREIIGVVSQEPVLFST-TIAENICYG---RGNVTM-DEIKKAVKEanayefIMKLPQKFDTLVG-ERGAQLSGGQKQRI 541
Cdd:cd03234 80 -QKCVAYVRQDDILLPGlTVRETLTYTailRLPRKSsDAIRKKRVE------DVLLRDLALTRIGgNLVKGISGGERRRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 542 AIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
393-580 |
7.14e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.86 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 393 NLEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLReiI 472
Cdd:PRK10851 2 SIEIANIKKSF---GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICYG------RGNVTMDEIKKAVkeanayefiMKLPQ--KFDTLVGERGAQLSGGQKQRIAI 543
Cdd:PRK10851 77 GFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961252 544 ARALVRNPKILLLDEATSALDTESEAEVQAALDKARE 580
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHE 184
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-617 |
7.48e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.13 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ------DIRNFNVNYLREIIGVVSQEPVLFS- 483
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 484 TTIAENICY---GRGNVTMDEIKKAVKEANAYEFIMKlpQKFDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 561 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
990-1216 |
8.45e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.54 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 990 NEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL--RAQLGI 1067
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1068 VSQEP--ILFDCSIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARA 1141
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1142 LIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
997-1207 |
8.61e-25 |
|
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: 103.01 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 997 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGTVLLDGqeaKKLNVQWLRAQLGIVSQEPIL 1074
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FDC-SIAENIAYgdnsrvvsqdeivsaakAANIhpfietlphkyetrvgdKGtqLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:cd03213 94 HPTlTVRETLMF-----------------AAKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1154 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHG 1207
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
996-1212 |
8.77e-25 |
|
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: 103.74 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 996 YPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILF 1075
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 D-CSIAENIAYgdNSRV--VSQDEIvsaakAANIHPFIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILL 1150
Cdd:cd03263 88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1151 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1002-1205 |
8.82e-25 |
|
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: 104.05 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGTVLLDGQEAKKLN----VQWLRAQLGIVSQE--- 1071
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 -PILfdcSIAENIAY-----GDNSrvvsqdeivSAAKAAnihpfiETLphkyeTRVGDKG------TQLSGGQKQRIAIA 1139
Cdd:COG4181 102 lPTL---TALENVMLplelaGRRD---------ARARAR------ALL-----ERVGLGHrldhypAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1140 RALIRQPQILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1205
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1001-1207 |
8.88e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP-IL 1074
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FDCSIAENIAYGD--NSRVVSQDEIVSAAKAAnihpfIET--LPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILL 1150
Cdd:PRK14247 95 PNLSIFENVALGLklNRLVKSKKELQERVRWA-----LEKaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1151 LDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVFQNGRVKEHG 1207
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
415-618 |
1.14e-24 |
|
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: 107.12 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDG---QDIR-NFNVNYLREIIGVVSQEPVLFS-TTIAEN 489
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRkGIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 490 ICYGRGNVTMDEikKAVKEANAYEFImklpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 569
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 570 EVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSELM 618
Cdd:TIGR02142 169 EILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1002-1203 |
1.20e-24 |
|
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: 104.74 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVqWLRAQLGIVS--QEPILF-DCS 1078
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIA----YGDNSRVVS---------QDEIVSAAKAANIhpfIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALI 1143
Cdd:COG0411 96 VLENVLvaahARLGRGLLAallrlprarREEREARERAEEL---LERvgLADRADEPAGN----LSYGQQRRLEIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1144 RQPQILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:COG0411 169 TEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
396-589 |
1.21e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 396 FNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqDIRnfnvnylreiIGVV 475
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 476 SQEPVLFST-TIAENICYGRGNV--TMDEIKKAVK--------------------EANAYEF------IMK---LPQK-F 522
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAklaepdedlerlaelqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 523 DTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAEVqaaldKAREGrTTIVIAH 589
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
986-1209 |
1.35e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE---AKKLN---VQ 1059
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSekaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1060 WLRAQLGIVSQE----PILfdcSIAENIAYGDnSRVVSQDEIVSAAKAANIhpfIETLphkyetRVGDKGT----QLSGG 1131
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEAP-CKVLGLSKEQAREKAMKL---LARL------RLTDKADrfplHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTH 1209
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
997-1207 |
1.75e-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: 102.83 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 997 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD 1076
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 -CSIAENIAYGDNSRVVSQDEIVSA----AKAANIHPFIETlphkyetRVGDkgtqLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:cd03266 92 rLTARENLEYFAGLYGLKGDELTARleelADRLGMEELLDR-------RVGG----FSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1152 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
394-624 |
1.77e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.82 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSR-------ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN-- 464
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 465 -VNYLREIIGVVSQEPvlfsttiaenicYG----RGNV--TMDE-------IKKAVKEANAYEFIMKlpqkfdtlVGERG 530
Cdd:PRK11308 86 aQKLLRQKIQIVFQNP------------YGslnpRKKVgqILEEpllintsLSAAERREKALAMMAK--------VGLRP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 531 AQ-------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIV-IAHRLSTVRN-ADVI 600
Cdd:PRK11308 146 EHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEV 225
|
250 260
....*....|....*....|....
gi 9961252 601 AGFEDGVIVEQGShselmkKEGVY 624
Cdd:PRK11308 226 MVMYLGRCVEKGT------KEQIF 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
394-612 |
2.04e-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: 102.83 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSY-PSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFNVNYLREII 472
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICY--GRGNVTMDEIKKAVKEanayefimkLPQKFDT--LVGERGAQLSGGQKQRIAIARAL 547
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
987-1208 |
2.61e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.50 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GTVLLDGQEAKKLNVQWLRA 1063
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 QLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPhkyetrvgdkgTQLSGGQKQRIA 1137
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVladvGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
394-621 |
3.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEP--VLFSTTIAENICYGRGNVTMDE------IKKAVKEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1004-1207 |
3.33e-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: 101.89 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAEN 1082
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAY-----GDNSRVVSQdEIVSAAKAANIHPFietlphkYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSA 1157
Cdd:cd03264 93 LDYiawlkGIPSKEVKA-RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1158 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
985-1224 |
3.45e-24 |
|
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: 103.78 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGTVLLDGQEAKKLNVQWLRAQ 1064
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1065 LGIVSQEPILFDCSIAENI-AYGDNSrvvsQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALI 1143
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMV 1223
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
.
gi 9961252 1224 S 1224
Cdd:cd03289 235 S 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-612 |
3.55e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.00 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD-----EGTINIDGQDIRNFNVN--YLREIIGVVSQEPVLFS 483
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 484 -TTIAENICYG-------RGNVTMDE-IKKAVKEANAYEfimklpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFEDGVIVEQG 612
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
412-617 |
4.03e-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: 102.06 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNyLREIIGVVSQEPvlfsttIAENIC 491
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 492 YGRGNVTM---------DEIKKAVKEANAYefiMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 563 LDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
394-620 |
4.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPS------RAnvkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN- 466
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 ---YLREIIGVVSQ--EPVLFSTTIAENICYGRGN--VTMDEIKKAVKEANAYEFIMklpqkfDTLVGERGAQLSGGQKQ 539
Cdd:PRK13649 79 dikQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
...
gi 9961252 618 MKK 620
Cdd:PRK13649 233 FQD 235
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
756-924 |
4.51e-24 |
|
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: 103.78 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 756 LIFLFLGIIS-FFTFfLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 834
Cdd:cd18572 40 LLLLLLSVLSgLFSG-LRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 835 IAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERK 914
Cdd:cd18572 117 FLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEER 196
|
170
....*....|
gi 9961252 915 FESMYVEKLY 924
Cdd:cd18572 197 EARRYERALD 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
999-1213 |
4.55e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 999 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDC 1077
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYG--DNSRVVSQD-EIVSAAKAanihpfiET-LPHkYETRvgdKGTQLSGGQKQRIAIARALIR------QPQ 1147
Cdd:PRK13548 92 TVEEVVAMGraPHGLSRAEDdALVAAALA-------QVdLAH-LAGR---DYPQLSGGEQQRVQLARVLAQlwepdgPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1148 ILLLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK13548 161 WLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
394-623 |
4.64e-24 |
|
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: 102.24 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY-LREII 472
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLF-STTIAENIcygrgnvtmdeikKAVKEanayefIMKLP-----QKFDTLVGE---------RGAQLSGGQ 537
Cdd:cd03218 78 GYLPQEASIFrKLTVEENI-------------LAVLE------IRGLSkkereEKLEELLEEfhithlrksKASSLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HR----LSTVRNADVIAgfeDGVIVEQG 612
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYIIY---EGKVLAEG 215
|
250
....*....|.
gi 9961252 613 SHSELMKKEGV 623
Cdd:cd03218 216 TPEEIAANELV 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
394-606 |
4.82e-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: 101.64 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKST----TVQLIQRL------YDPDEGTINIDGQDIRNf 463
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLegkvhwSNKNESEPSFEATRSRN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 464 nvnylREIIGVVSQEPVLFSTTIAENICYGrgNVTMDEIKKAVKEANAYE-FIMKLPQKFDTLVGERGAQLSGGQKQRIA 542
Cdd:cd03290 78 -----RYSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 543 IARALVRNPKILLLDEATSALDTE-SEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDG 606
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
412-589 |
5.19e-24 |
|
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: 102.16 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLreiigVVSQEPVLFS-TTIAENI 490
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CYGRGNVtMDEIKKAVKEANAYEFImklpqkfdTLVG------ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 9961252 565 TESEAEVQAALDKARE--GRTTIVIAH 589
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1005-1201 |
5.76e-24 |
|
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: 101.77 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLraqlgIVSQEPILFD-CSIAENI 1083
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 AYGDNS-----RVVSQDEIVSAakaaniHPFIETLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSAL 1158
Cdd:TIGR01184 76 ALAVDRvlpdlSKSERRAIVEE------HIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 1159 DTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNG 1201
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1004-1215 |
5.78e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 102.74 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE-------------AKKLNVQWLRAQLGIVSQ 1070
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1071 EPILFD-CSIAENIAYGDnSRVVSQDEIVSAAKAAnihpfietlphKYETRVG-DKGTQ------LSGGQKQRIAIARAL 1142
Cdd:PRK10619 100 HFNLWShMTVLENVMEAP-IQVLGLSKQEARERAV-----------KYLAKVGiDERAQgkypvhLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1143 IRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLLAQ 1215
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLFGN 242
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
129-347 |
6.92e-24 |
|
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: 103.27 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSV 347
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
111-364 |
9.55e-24 |
|
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: 102.95 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIgAFSVGQ 349
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGElSQFVFYAVLA-AGSVGA 271
|
250
....*....|....*
gi 9961252 350 AAPCIDAFANARGAA 364
Cdd:cd18575 272 LSEVWGDLQRAAGAA 286
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
987-1208 |
1.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.52 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE----AKKLNVQW 1060
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1061 LRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKaanihpfiETLphkyeTRVG------DKGT-QLSGG 1131
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAR--------EKL-----ALVGiseslfEKNPfELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1208
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
394-621 |
1.03e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 106.67 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLF-STTIAENICYG--RGNVTMDEIKKAVKEANAYefiMKLPQKFDTL-VGERgaqlsggqkQRIAIARALV 548
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 549 RNPKILLLDEATSALdTESEAE-----VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAETErlfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
416-618 |
1.85e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.43 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLFS-TTIAENICYG- 493
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 494 ----RGNV----TMDEIKKAVKEANayeFIMKLPqkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PRK10771 97 npglKLNAaqreKLHAIARQMGIED---LLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 566 ESEAEVQAALDKAREGR--TTIVIAHRLS-TVRNAD---VIAgfeDGVIVEQGSHSELM 618
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
987-1213 |
2.04e-23 |
|
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: 100.93 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG-TVLLDGQEAKKLNVQWLRAQL 1065
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEpilfdcsIAENIAYGDNSR--VVS------------QDEIVSAAKAAnihpfIETL--PHKYETRVGdkgtQLS 1129
Cdd:COG1119 81 GLVSPA-------LQLRFPRDETVLdvVLSgffdsiglyrepTDEQRERAREL-----LELLglAHLADRPFG----TLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1130 GGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVFQNGRV 1203
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRV 221
|
250
....*....|
gi 9961252 1204 KEHGTHQQLL 1213
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1004-1212 |
2.34e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.24 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1082
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAYG---------DNSRVVSQD-----EIVSAAKAANIHPfietlphkyetrvgdkgTQLSGGQKQRIAIARALIRQPQI 1148
Cdd:PRK10851 95 IAFGltvlprrerPNAAAIKAKvtqllEMVQLAHLADRYP-----------------AQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1149 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1005-1216 |
2.50e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQ--EPILFDCS 1078
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDNSRVVSQDEIVSAAKaanihpfietlphKYETRVG------DKGT-QLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKAL-------------KWLKKVGlsedliSKSPfELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1152 DEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:PRK13641 170 DEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
403-617 |
3.41e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.19 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 403 YPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdiRNFNVNYLREIIGVVSQEPVLF 482
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 483 S-TTIAENICYGR--GNVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:PRK11000 88 PhLSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 560 TSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
986-1159 |
4.08e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.61 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpLAGTVLLDGQeakklnvqwlr 1062
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGR----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 aqlgIVSQ-EPILFDC-------------SIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPHkyetrvgdk 1124
Cdd:PRK11650 67 ----VVNElEPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIeervAEAARILELEPLLDRKPR--------- 133
|
170 180 190
....*....|....*....|....*....|....*
gi 9961252 1125 gtQLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:PRK11650 134 --ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
409-624 |
4.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINID----GQD--------------IRNFNvnYLRE 470
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKknnhelitnpyskkIKNFK--ELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEP--VLFSTTIAENICYGrgNVTMDEIKKAVKEANAYeFIMKLPQKFDTLvgERGA-QLSGGQKQRIAIARAL 547
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKF-YLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 548 VRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEGVY 624
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
394-612 |
4.30e-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: 98.44 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIiG 473
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFST-TIAENICYGRgnVTMDEIKKAVKEANAYefimklpqkfdtlVGERGA------QLSGGQKQRIAIARA 546
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLA--RLLGIRKKRIDEVLDV-------------VGLKDSakkkvkGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1003-1206 |
4.30e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEakklnVQWLRAQLGIVSQ-EPILFDCSIAE 1081
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1162 SEKVVQEALDK--AREGRTCIVIAHrlsTIQNA-----DLIVVFQN-GRVKEH 1206
Cdd:PRK11248 163 TREQMQTLLLKlwQETGKQVLLITH---DIEEAvfmatELVLLSPGpGRVVER 212
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
100-339 |
4.38e-23 |
|
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: 100.97 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 100 LSLLNPG-------KILEEEMTRYAYYYSG--LGAGVL--VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDIN 168
Cdd:cd18542 14 LNLLIPLlirriidSVIGGGLRELLWLLALliLGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 169 DTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKIL-SAFSDK--- 244
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVrPAFEEIreq 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 245 --ELaayakaGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTL 322
Cdd:cd18542 174 egEL------NTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYL 247
|
250
....*....|....*..
gi 9961252 323 VISKEYTIGNaMTVFFS 339
Cdd:cd18542 248 VINGEITLGE-LVAFIS 263
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1003-1199 |
4.81e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1082
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAYGDNSRVVSQDEivsAAKAANIHPFieTLPhkyETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1162
Cdd:PRK10247 101 LIFPWQIRNQQPDP---AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 9961252 1163 EKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVFQ 1199
Cdd:PRK10247 173 KHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1004-1203 |
5.73e-23 |
|
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: 98.88 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE---RFYDPLAGTVLLDGQEAKKlnVQWLRaQLGIVSQEPILFDC-SI 1079
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYGDNSRV-VSQDEIVSAAKAAnihpfIETLPHKYETRVGDKG-TQLSGGQKQRIAIARALIRQPQILLLDEATSA 1157
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961252 1158 LDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVFQNGRV 1203
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
996-1215 |
6.05e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 996 YPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP--I 1073
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 LFDCSIAENIAYGDNSRVVSQDEIV----SAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQIL 1149
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1150 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
394-623 |
6.52e-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: 98.75 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL-REII 472
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFST-TIAENICYGrgnvtMDEIKKAVKE--ANAYEFimkLPQKFDTLvGERGAQLSGGQKQRIAIARALVR 549
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTG-----LAALPRRSRKipDEIYEL---FPVLKEML-GRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSElMKKEGV 623
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDE-LDEDKV 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1000-1207 |
6.60e-23 |
|
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: 98.12 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeaKKLNVQwLRAQLGIVSQEPILF-DCS 1078
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDNSRVVSQDEIvsaakAANIHPFIET--LPHKYETRVgdkgTQLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:cd03269 87 VIDQLVYLAQLKGLKKEEA-----RRRIDEWLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1157 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:cd03269 158 GLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
714-946 |
6.82e-23 |
|
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: 100.25 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 714 GTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAvkqqkcNIFSLIFLFLGII---SFFTFFlQGFTFGKAGEILTRRLRS 789
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIdAALGGGDTA------SLNQIALLLLGLFllqAVFSFF-RIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 790 MAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18576 74 DLYRHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 870 SGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERkFESM-YVEKLygpYRVFSAIVFGAVALGHASSF 946
Cdd:cd18576 152 VAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKAL---ERVVKLALKRARIRALFSSF 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
993-1219 |
7.44e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 993 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV---------------LLDGQEAKKL- 1056
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheLITNPYSKKIk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1057 NVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEivsAAKAANIH--------PFIETLPHkyetrvgdkgt 1126
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSPF----------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1127 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVK 1204
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 9961252 1205 EHGTHQQLLAQKGIY 1219
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
987-1207 |
9.54e-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: 97.67 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWlrAQLG 1066
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFD-CSIAENIAYGDNSRVVSQdeivsaakaANIHPFIETLPHKYETRvgDKGTQLSGGQKQRIAIARALIRQ 1145
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRK---------KRIDEVLDVVGLKDSAK--KKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1009-1216 |
9.75e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1009 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD-CSIAENIAYGD 1087
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1088 NS----RVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALD---- 1159
Cdd:PRK10771 97 NPglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1160 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1002-1202 |
1.00e-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: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQE-----AKKLNVQWL---RAQLGIVSQ--- 1070
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1071 ------------EPILfdcsiaeniaygdnSRVVSQDEivSAAKAA------NIHpfiETLPHKYETrvgdkgTqLSGGQ 1132
Cdd:COG4778 104 viprvsaldvvaEPLL--------------ERGVDREE--ARARARellarlNLP---ERLWDLPPA------T-FSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1133 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
394-613 |
1.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.29 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN-VNYLREII 472
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEP--VLFSTTIAENICYGRGNVTMD--EIKKAVKEANAYEFIMKLPQKfdtlvgeRGAQLSGGQKQRIAIARALV 548
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 549 RNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1000-1216 |
1.25e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCS 1078
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDN------SRVVSQDE-IVSAAKAANihpFIETLPHKyetRVgdkgTQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:PRK11231 93 VRELVAYGRSpwlslwGRLSAEDNaRVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1152 DEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:PRK11231 163 DEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
998-1213 |
1.53e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FD 1076
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYGDN---SRVVSQDEIVSAAKAanihpfiETLPHKYETRVGDKG-TQLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1153 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
412-657 |
1.69e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI----IGVVSQEPVLFS-TTI 486
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENICYGrgnVTMDEIKKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 567 SEAEVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELMKKEG-----VYFKLVNMqtsgSQIQ 638
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrTFFRGVDI----SQVF 274
|
250
....*....|....*....
gi 9961252 639 SeefelndEKAATRMAPNG 657
Cdd:PRK10070 275 S-------AKDIARRTPNG 286
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1004-1210 |
2.09e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDG------QEAKKLNVQWLRAQLGIVSQE----PI 1073
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 LfdcSIAENIAYGDnSRVVSQDEIVSAAKAANIhpfIETLphkyetRVGDKGT----QLSGGQKQRIAIARALIRQPQIL 1149
Cdd:PRK11124 97 L---TVQQNLIEAP-CRVLGLSKDQALARAEKL---LERL------RLKPYADrfplHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1150 LLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1210
Cdd:PRK11124 164 LFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
415-589 |
2.57e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.68 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNvNYLREIiGVVSQEPVLFS-TTIAENICYG 493
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPI-NMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 494 --RGNVTMDEIKKAVKE----ANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE- 566
Cdd:PRK11607 116 lkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180
....*....|....*....|....*.
gi 9961252 567 ---SEAEVQAALDkaREGRTTIVIAH 589
Cdd:PRK11607 185 rdrMQLEVVDILE--RVGVTCVMVTH 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1009-1213 |
2.93e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.88 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1009 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFDCSIAENI 1083
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 AYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYEtrvgdkgTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE 1163
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1164 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
409-613 |
2.97e-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: 97.42 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVnylREII--GVVS--QEPVLFST 484
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP---HRIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 -TIAENI---CYGRGNVTM-----------DEIKKAVKEANAY-EFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:COG0411 94 lTVLENVlvaAHARLGRGLlaallrlprarREEREARERAEELlER-VGLADRADEPAGN----LSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 549 RNPKILLLDEATSALdteSEAEVQAALD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 613
Cdd:COG0411 169 TEPKLLLLDEPAAGL---NPEETEELAElirrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
986-1203 |
2.98e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITfneVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVqWLRAQL 1065
Cdd:COG1101 6 NLS---KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 -GIVSQEPILFDC---SIAEN--IAYGDNSRVvsqdEIVSAAKAANIHPFIET-------LPHKYETRVGdkgtQLSGGQ 1132
Cdd:COG1101 82 iGRVFQDPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1133 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1203
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1004-1205 |
4.77e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.45 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRA-----QLgiVSQEPI----- 1073
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQM--VFQDSIsavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 --LFDCSIAENIAYgdnsrVVSQDEIVSAAKAANIHPFIETLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:PRK10419 105 rkTVREIIREPLRH-----LLSLDKAERLARASEMLRAVDLDDSVLDKRPP----QLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1152 DEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1205
Cdd:PRK10419 176 DEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
402-598 |
5.13e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 402 SYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdirNFNVNYLREIIGVVSQEPVl 481
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 fstTIAENICYGR-------GNVTMDEiKKAVKEAnayefIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:NF040873 73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961252 555 LLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRNAD 598
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1004-1184 |
5.25e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.83 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF- 1075
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DCSIAENIAYGD--NSRVVSQ---DEIVSAA--KAAnihpfietLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQI 1148
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKkelDERVEWAlkKAA--------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961252 1149 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1184
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
405-580 |
5.33e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFNVnYLREIiGVVSQEPVL 481
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA-EQRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 FS-TTIAENICYG-----RGNVTMDEIKKAVKEANAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170 180
....*....|....*....|....*.
gi 9961252 556 LDEATSALDTESEAEVQA-ALDKARE 580
Cdd:COG4136 157 LDEPFSKLDAALRAQFREfVFEQIRQ 182
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
995-1216 |
5.57e-22 |
|
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: 97.62 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 995 NYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQlgivsqepil 1074
Cdd:cd03291 44 NLCLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 fdcSIAENIAYGdnsrvVSQDEI--VSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:cd03291 113 ---TIKENIIFG-----VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1153 EATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:cd03291 185 SPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
987-1208 |
5.95e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.50 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVvfNYPTRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV----LLDGQEAKKLNV 1058
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1059 QWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEI--VSAAKAANI---HPFIETLPHkyetrvgdkgtQLSGG 1131
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAekIAAEKLEMVglaDEFWEKSPF-----------ELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1208
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
986-1203 |
6.98e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.87 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NIT--FNEVVfnyptrANvpvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEakklnVQW--- 1060
Cdd:COG3845 10 GITkrFGGVV------AN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-----VRIrsp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1061 ---LRAQLGIVSQEPILFDC-SIAENIAYGDNSRvvsQDEIVSAAKAANIhpfIETLPHKY------ETRVGDkgtqLSG 1130
Cdd:COG3845 75 rdaIALGIGMVHQHFMLVPNlTVAENIVLGLEPT---KGGRLDRKAARAR---IRELSERYgldvdpDAKVED----LSV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1131 GQKQRIAIARALIRQPQILLLDEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1203
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
394-608 |
7.68e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInIDGqdirNFNVNYLREIIG 473
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLFS-TTIAENICYG-RGNVTMD--EIKKAVKEANAyefimklpqkfdtlVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGlKGQWRDAalQALAAVGLADR--------------ANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVI 608
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
394-621 |
8.73e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVL-FSTTIAENICYGRGnvTMDEIKKAVKEanayefimkLPQKFDTLVGERG------AQLSGGQKQRIAIARA 546
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRA--PHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 547 LVR------NPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVlRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
....
gi 9961252 618 MKKE 621
Cdd:PRK13548 229 LTPE 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
410-621 |
1.25e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF------------------------NV 465
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLREIIGVVSQ--EPVLFSTTIAENICYGRGNVTMDEiKKAVKEANAYEFIMKLPQKFDtlvgERGA-QLSGGQKQRIA 542
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTV--RNADVIAgFEDGVIVEQGSHSELMK 619
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDILS 254
|
..
gi 9961252 620 KE 621
Cdd:PRK13651 255 DN 256
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
394-590 |
1.26e-21 |
|
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: 92.99 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVhfSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfNVNYLreiig 473
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 vvSQEPVLFSTTIAENICYGRGNVtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961252 554 LLLDEATSALDTESEAEVqaaLDKAREGRTTIV-IAHR 590
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
394-612 |
1.31e-21 |
|
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: 94.27 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNvnylREIIG 473
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLF-STTIAENICY-GRgnvtmdeiKKAVKEANAYEFIMKLPQKFD--TLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQ--------LKGLKKEEARRRIDEWLERLElsEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 550 NPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:cd03269 146 DPELLILDEPFSGLDPVN-VELlkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-622 |
1.32e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN---YLRE 470
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 iigvvsqEPVLF-STTIAENICY-GR--GnVTMDEIKKAVKEanayefimkLPQKFDtlVGERGA----QLSGGQKQRIA 542
Cdd:COG4152 79 -------ERGLYpKMKVGEQLVYlARlkG-LSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 543 IARALVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVN-VELlkDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRR 218
|
...
gi 9961252 620 KEG 622
Cdd:COG4152 219 QFG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1003-1215 |
1.44e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----LAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1073
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 L-------FDCSIAENIA-YGDNSRVVSQDEIVSAAKAANIHpfietlphKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1145
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1146 PQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
111-350 |
1.88e-21 |
|
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: 96.23 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18784 113 NLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQA 350
Cdd:cd18784 193 NEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
394-589 |
1.98e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlreiiG 473
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQ-EPVLFSTTIAENICYGrgnVTMDEIKKAVKEANAYEFIMKlpqkfdtlVGERGA------QLSGGQKQRIAIARA 546
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1004-1213 |
2.12e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---LAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-D 1076
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFieTLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1157 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
394-620 |
2.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANV--KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqDI------RNFNV 465
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLREIIGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKE-----ANAYEFIMKLPqkfdtlvgergAQLSGG 536
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 9961252 615 SELMKK 620
Cdd:PRK13643 229 SDVFQE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
394-613 |
2.47e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVK--------ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPDEGTINIDGQDIRNFNV 465
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYL---REIIGVVSQEP---------VLfsTTIAENIcygrgNVTMDEIKKAVKEANAYEFIMKLpqKFDTLVGER-GAQ 532
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGL-----RVHQPTLSAAQREQQVIAVMEEV--GLDPETRHRyPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNA--DVIAgFEDGVI 608
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIV-LRQGEV 504
|
....*
gi 9961252 609 VEQGS 613
Cdd:PRK15134 505 VEQGD 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
402-558 |
2.49e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.33 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 402 SYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTT----VQLIQrlydPDEGTINIDGQDIRNFNVnYLREI--IGVV 475
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLPM-HKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 476 SQEPVLF-STTIAENIcygrgnvtmdeikKAVKEanayefIMKLP-----QKFDTLVGE---------RGAQLSGGQKQR 540
Cdd:COG1137 84 PQEASIFrKLTVEDNI-------------LAVLE------LRKLSkkereERLEELLEEfgithlrksKAYSLSGGERRR 144
|
170
....*....|....*...
gi 9961252 541 IAIARALVRNPKILLLDE 558
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
392-653 |
2.64e-21 |
|
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: 95.31 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPdEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENI-CYGRGNvtMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STVRNADVIAGF--EDGVIVEQGSH 614
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeamlecqrflvieeNKVRQYDSIQKLlnEKSHFKQAISP 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 9961252 615 SELMKKEGVYFKLVNMQTSGSQIQSEEFELNDEKAATRM 653
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRKPRPQIQALQEETEEEVQDTRL 275
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1003-1214 |
2.77e-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: 94.15 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DCSI 1079
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYGDNSRVVSQDEIVSAAKAAnIHPF-IETLPHKyetrvgdKGTQLSGGQKQRIAIARALIRQPQILLLDEATSAL 1158
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKLEEL-LEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1159 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
144-364 |
4.79e-21 |
|
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: 94.81 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 144 RQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAI 223
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 224 SPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGI 303
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 304 AFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 364
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
394-591 |
4.85e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.15 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDiRNFNVNYLREI-- 471
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNGPKSSQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFST-TIAENICYGRGNVT-MDEI--KKAVKEANAYEFIMKLPQKFDTLVGErgaqLSGGQKQRIAIARAL 547
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGREFVNrFGRIdwKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 548 VRNPKILLLDEATSAL-DTESEA------EVQAaldkarEGRTTIVIAHRL 591
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRL 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
996-1198 |
6.13e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 996 YPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwlraqlgiVSQEPILF 1075
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPF----IETLPHKyetRVGDkgtqLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALervgLADLAGR---QLGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961252 1152 DEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1198
Cdd:NF040873 144 DEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1004-1208 |
6.59e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.96 E-value: 6.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQW---LRAQ-LGIVSQ-EPILFDCS 1078
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAY----GDNSRVVSQDEIVSAAKAANIhpfietlphkyETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGL-----------EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1155 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
394-620 |
7.08e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.21 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSypsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDGQDIRNFNVN----- 466
Cdd:COG0396 1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDerara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 -------YLREIIGV-VSQepvlFSTTIAENIcyGRGNVTMDEIKKAVKEANAyefIMKLPQKFdtlvGERG--AQLSGG 536
Cdd:COG0396 78 giflafqYPVEIPGVsVSN----FLRTALNAR--RGEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 9961252 614 hSELMKK 620
Cdd:COG0396 225 -KELALE 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1004-1214 |
7.40e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGTVLLDGQEAKKLNVQWL---RAQLGIVSQEP---ILFDC 1077
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYG------DNSRVVSQDEIVSAAKAANIHPfieTLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:PRK15134 380 NVLQIIEEGlrvhqpTLSAAQREQQVIAVMEEVGLDP---ETRHRYPA-------EFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1152 DEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK15134 450 DEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
412-608 |
8.68e-21 |
|
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: 92.50 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQD---------------IRnfnvnylREIIGVVS 476
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspreilaLR-------RRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 477 QepvlFSTTI----AENIcygrgnVTMDEIKKAVKEANAYEFIMKLPQKFDtlVGERGAQL-----SGGQKQRIAIARAL 547
Cdd:COG4778 100 Q----FLRVIprvsALDV------VAEPLLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHrlstvrNADVIAGFEDGVI 608
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH------DEEVREAVADRVV 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
983-1214 |
1.67e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 983 FEGNITFNEVVFNYPTRAnvpvlqglslevkkgqTLALVGSSGCGKSTVVQLLERFYDPLAG-----TVLLDGQEA-KKL 1056
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1057 NVQWLRAQLGIVSQEPILFDCSIAENIAYGDNS-RVVSQDEIVSAAKAAnihpFIET-LPHKYETRVGDKGTQLSGGQKQ 1134
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAhKLVPRKEFRGVAQAR----LTEVgLWDAVKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1135 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
.
gi 9961252 1214 A 1214
Cdd:PRK14271 251 S 251
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1004-1208 |
1.86e-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: 91.43 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWlRAQLGI--VSQEPILF-DCSIA 1080
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIAYGDNSRvvsqdeivsAAKAANIHPFIETL-PHKYETRvGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:TIGR03410 94 ENLLTGLAAL---------PRRSRKIPDEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1160 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGT 1208
Cdd:TIGR03410 164 PSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1001-1208 |
2.44e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.67 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPLAGTVLLDGQEAKKLNVQwLRAQLGI-VS-QEPI-- 1073
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 --------LfdcSIAENIAYGDNSRVV-SQDEIVSAAKAANihpfietLPHKYETR---VGdkgtqLSGGQKQRIAIARA 1141
Cdd:COG0396 90 pgvsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1142 LIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1004-1224 |
2.53e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 97.93 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVlldgqeakklnvqWLRAQLGIVSQEPILFDCSIAENI 1083
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 AYGDNSRvvsQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE-S 1162
Cdd:PTZ00243 742 LFFDEED---AARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1163 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVS 1224
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAA 879
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1004-1214 |
2.53e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqEAKKLNVQWLRAQLGIVSQ----EPilfDCSI 1079
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIaygdnsRVVSQDEIVSAAKA-ANIHPFIE--TLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:PRK13537 98 RENL------LVFGRYFGLSAAAArALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1157 ALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK13537 168 GLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
986-1212 |
2.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITFnevVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV------------------- 1046
Cdd:PRK13651 7 NIVK---IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1047 ----LLDGQEAKKL-NVQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAanihpFIET--LPHKY 1117
Cdd:PRK13651 84 leklVIQKTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1118 ETRvgdKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLI 1195
Cdd:PRK13651 159 LQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*...
gi 9961252 1196 VVFQNGR-VKEHGTHQQL 1212
Cdd:PRK13651 236 IFFKDGKiIKDGDTYDIL 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1002-1215 |
3.86e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQ-WLRAQLGIVSQEPILF-DCSI 1079
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYGD--NSR-VVSQDEIVSAAKAANIHPFIETLPhkyETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:PRK11288 97 AENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1157 ALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNGR-VKEHG-----THQQLLAQ 1215
Cdd:PRK11288 170 SLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRyVATFDdmaqvDRDQLVQA 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-621 |
4.00e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQ----EPvlfSTTIAENI-CYGRG-NVTMDEIKKAVkeANAYEFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARAL 547
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
405-612 |
4.09e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVL-FS 483
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 484 TTIAENICYGRGN-----VTMDEI-KKAVKEA-NAYEFIMKLPQKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTETdRAAVERAmERTGVAQFADRPVTS--------LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 557 DEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 612
Cdd:PRK09536 164 DEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
382-621 |
4.33e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 382 ERGHKPDSIkgnLEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR 461
Cdd:PRK10575 3 EYTNHSDTT---FALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 462 NFNVN-YLREIIGVVSQEPVLFSTTIAENICYGR-------GNVTMDEIKKaVKEANAYEFIMKLPQKfdtLVGergaQL 533
Cdd:PRK10575 77 SWSSKaFARKVAYLPQQLPAAEGMTVRELVAIGRypwhgalGRFGAADREK-VEEAISLVGLKPLAHR---LVD----SL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 534 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVE 610
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIA 228
|
250
....*....|.
gi 9961252 611 QGSHSELMKKE 621
Cdd:PRK10575 229 QGTPAELMRGE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1003-1214 |
4.77e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ--EAKKLNVQWLRAQLGIVSQEP--ILFDCS 1078
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDNSRVVSQDEIVSAAKAAnihpfiETLPHKYETRvgDKGTQ-LSGGQKQRIAIARALIRQPQILLLDEATSA 1157
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1158 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-623 |
4.90e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFNVNYLREI 471
Cdd:PRK13638 2 LATSDLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEANayefimklpqkfdTLVGERGAQ------LSGGQKQRI 541
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 542 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG------S 613
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfA 225
|
250
....*....|
gi 9961252 614 HSELMKKEGV 623
Cdd:PRK13638 226 CTEAMEQAGL 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
987-1216 |
5.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDG----QEAKKLNVQW 1060
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1061 LRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAkaanihpFIETLPHKYETRVGDKGT-QLSGGQKQRIA 1137
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 9961252 1215 QK 1216
Cdd:PRK13646 236 DK 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
394-610 |
5.86e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNV-NYLREII 472
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQE----PVLfstTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFD--TLVGErgaqLSGGQKQRIAIARA 546
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 547 LVRNPKILLLDEATSALdTESEAEVQAALDKA--REGRTTIVIAHRLSTV-RNADVIAGFEDGVIVE 610
Cdd:PRK11288 155 LARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1004-1203 |
6.64e-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: 88.64 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNV-QWLRAQLGIVSQEP----ILFDCS 1078
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAygdnsrvvsqdeivsaakaanihpfietLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSAL 1158
Cdd:cd03215 95 VAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1159 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1203
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1007-1212 |
6.91e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1007 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN-VQWL--RAQLGIVSQEPILF---DCSIA 1080
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIA------YGDNSRVVSQDEIVSAAKAANIHP-FIETLPHKYetrvgdkgtqlSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1154 ATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK15079 188 PVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
409-606 |
7.07e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD---EGTINIDGQDIRNFNVnylREI----IGVVSQEPVL 481
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNI---RDTeragIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 FST-TIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK13549 94 VKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961252 561 SALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:PRK13549 172 ASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
987-1185 |
1.00e-19 |
|
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: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeakklnvqwlRAQLG 1066
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIAYgdnsrvvsqdeivsaakaanihPFietlphkyetrvgdkGTQLSGGQKQRIAIARALIRQP 1146
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----------------------PW---------------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1185
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
394-610 |
1.06e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIdGQDIRnfnvnylreiIG 473
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVLF--STTIAENICYGRGNVTmdeikkaVKEANAYefimkL------PQKFDTLVGErgaqLSGGQKQRIAIAR 545
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGT-------EQEVRGY-----LgrflfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 546 ALVRNPKILLLDEATSALDTESEAEVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFEDGVIVE 610
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1002-1202 |
1.19e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGTVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-D 1076
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYGD---NSRVVSQDEIVSAAKA------ANIHPfietlphkyETRVGDkgtqLSGGQKQRIAIARALIRQPQ 1147
Cdd:PRK13549 97 LSVLENIFLGNeitPGGIMDYDAMYLRAQKllaqlkLDINP---------ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1148 ILLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:PRK13549 164 LLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1008-1215 |
1.25e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.28 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWlRAQLgI--VSQEPilfdcsiaeNIAY 1085
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKH-IrmIFQDP---------NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1086 GDNSRVVSQDEI--------VSAAKAANIhpfIETLphkyeTRVG-------DKGTQLSGGQKQRIAIARALIRQPQILL 1150
Cdd:COG4167 101 NPRLNIGQILEEplrlntdlTAEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1151 LDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:COG4167 173 ADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1004-1203 |
1.43e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----LAGTVLL-DGQEAKKLNVQWLRaqlgivsqepILFDC 1077
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYG--DNSRvvsqDEIVSAAKAANIhpfietlphkyETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEAT 1155
Cdd:PRK11247 97 KVIDNVGLGlkGQWR----DAALQALAAVGL-----------ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1156 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1203
Cdd:PRK11247 162 GALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
406-618 |
1.58e-19 |
|
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: 93.71 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTIN-------IDGQDIRNFNVNYLREIIGVVSQE 478
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 479 PVLFS-TTIAENICYGRGNVTMDEI--KKAV--------KEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARAL 547
Cdd:TIGR03269 374 YDLYPhRTVLDNLTEAIGLELPDELarMKAVitlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-621 |
2.10e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPVL-FSTTIAEN-ICYGR-GNVTMDEIKKAVkeANAYEFiMKLPQKFDTLVgergAQLSGGQKQRIAIARALVRN 550
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRyFGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
103-342 |
2.53e-19 |
|
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: 89.78 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 103 LNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQvSFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDI 181
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 182 SKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKI-----------LSAFSDKelaaya 250
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKihkrfrkvqeaFSDLSDR------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 251 kagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTI 330
Cdd:cd18541 182 -----VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
250
....*....|....
gi 9961252 331 GN--AMTVFFSILI 342
Cdd:cd18541 257 GDlvAFNSYLGMLI 270
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1001-1207 |
2.93e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQ-----EAKKLNVqwlraqlGIVSQEPILF 1075
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGV-------GMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 -DCSIAENIAYGDNSRVVSQDEIvsaAKAANIHPFIETLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:PRK11000 88 pHLSVAENMSFGLKLAGAKKEEI---NQRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1155 TSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1207
Cdd:PRK11000 161 LSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1003-1216 |
5.16e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV-LLDGQEAKKlnVQWLRAQLGIVSQepilFD----- 1076
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPAR--ARLARARIGVVPQ----FDnldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAEN-IAYGDNSRVvSQDEIvsaakAANIHPFIE--TLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:PRK13536 129 FTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1154 ATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1216
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1002-1203 |
5.19e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.86 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFD 1076
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENI----AYGDNSRvvsqdeivsAAKAANIHPFIETLphKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:PRK10535 101 LTAAQNVevpaVYAGLER---------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1153 EATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
392-591 |
5.62e-19 |
|
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: 93.44 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 392 GNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDpDEGTINIDGQDIRNFNVNYLREI 471
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTIAENI-CYGRgnVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLdPYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 591
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
394-620 |
5.89e-19 |
|
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: 86.43 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSypsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRL--YDPDEGTINIDGQDIRNFNVN-YLRE 470
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSttiaenicygrgNVTMDEIKKAVKEAnayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRN 550
Cdd:cd03217 78 GIFLAFQYPPEIP------------GVKNADFLRYVNEG-----------------------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGSHS---ELMKK 620
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEKK 198
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
389-627 |
6.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 389 SIKGNLEFNDVHFSYPSRA--NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEG-TINIDGQDIRNFN- 464
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 465 ---VNYLREIIGVVSQEP--VLFSTTIAENICYGRGNVTMD--EIKKAVKEanayefIMKLPQKFDTLVGERGAQLSGGQ 537
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENkqEAYKKVPE------LLKLVQLPEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSH 614
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP 235
|
250
....*....|...
gi 9961252 615 SELMKKEGVYFKL 627
Cdd:PRK13645 236 FEIFSNQELLTKI 248
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
394-618 |
6.67e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 87.97 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAN------VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY 467
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 LREIIGVVSQEPvlfSTTIAENICYG-------RGNVTMDEIKKavkeanaYEFImklpqkFDTL--VGERGAQ------ 532
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEER-------EERI------FATLrlVGLLPEHanfyph 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 533 -LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQaaldkAREGRTTIVIAHRLSTVRN-ADVIAGF 603
Cdd:COG4167 149 mLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQ-----EKLGISYIYVSQHLGIVKHiSDKVLVM 223
|
250
....*....|....*
gi 9961252 604 EDGVIVEQGSHSELM 618
Cdd:COG4167 224 HQGEVVEYGKTAEVF 238
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
711-916 |
6.70e-19 |
|
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: 88.64 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQKCN---IFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRL 787
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 788 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPII 867
Cdd:cd18542 75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961252 868 AVSGIVEMKLLaGNAKRDKKELEAA-GKIATEAIENIRTVVSLTQER----KFE 916
Cdd:cd18542 153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREDyeieKFD 205
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
411-621 |
8.12e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.73 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVL-FSTTIAEN 489
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 490 ICYGRG------NVTMDEIKKAVKEANAYEFIMKLP-QKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 563 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK10253 174 LDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1005-1209 |
8.54e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 8.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEP-ILFDCSIA 1080
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIAYgdnsrvvsqDEIVSAAKAANIHPFIETLPHKyetrVG--DKG----TQLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:PRK10908 98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1155 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVFQNGRVkeHGTH 1209
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
989-1184 |
9.72e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 989 FNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQeakklnvqwlrAQLGIV 1068
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1069 SQEPILFD-CSIAENIAYGDNSRVVSQDEIVSA-----------AKAANIHPFIETL-PHKYETRVGD--KG-------- 1125
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALgGWEAEARAEEilSGlgfpeedl 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1126 ----TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1184
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
711-906 |
1.17e-18 |
|
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: 87.86 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgdDAVKQQKcNIFSLIFLFLGIISFFTF-----FLQGFTFGKAGEILTR 785
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLL-------DDIFVEK-DLEALLLVPLAIIGLFLLrglasYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVP 865
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9961252 866 IIAVSGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTV 906
Cdd:cd18552 151 LAALPIRRIGKRL---RKISRRSQESMGDLTSvlqETLSGIRVV 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
998-1183 |
2.01e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQ-EPILfd 1076
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 cSIAENIAYGDNSRVVSQDEIVSAAKAANIHPfIETLPHKYetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 9961252 1157 ALDTESEKVVQEALdKAREGRTCIVIA 1183
Cdd:PRK13539 157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
411-617 |
2.28e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD------EGTINIDGQDIRNFNVNYLREI----IGVVSQEPV 480
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 481 L-------FSTTIAENICYGRGnvtMDeikkavKEANAYEFIMKLPQkfdtlVGERGA---------QLSGGQKQRIAIA 544
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSLHRG---MR------REAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1005-1230 |
2.40e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL----------ERFYDPLAGTVLLDGQEAKklNVQWLRAQLGIVSQEPIL 1074
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FD-CSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLphkyeTRVG------DKGTQLSGGQKQRIAIARALIRQPQ 1147
Cdd:PRK09984 98 VNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1148 ILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK--GIYFSM 1222
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYRSI 252
|
....*...
gi 9961252 1223 VSVQAGTQ 1230
Cdd:PRK09984 253 NRVEENAK 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
409-647 |
2.51e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-IGVVSQE-PVLFSTTI 486
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENICYGR------GNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK09700 98 LENLYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 561 SALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEgvyfkLVNMQTsGSQIQ 638
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDD-----IVRLMV-GRELQ 247
|
....*....
gi 9961252 639 SEEFELNDE 647
Cdd:PRK09700 248 NRFNAMKEN 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
987-1206 |
2.75e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLdGQeakklNVQwlraqLG 1066
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDcsiaeniaygDNSRVVsqDEIVSAAKAANIHPFIETL------PHKYETRVGDkgtqLSGGQKQRIAIAR 1140
Cdd:COG0488 382 YFDQHQEELD----------PDKTVL--DELRDGAPGGTEQEVRGYLgrflfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1141 ALIRQPQILLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVFQNGRVKEH 1206
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
378-641 |
3.48e-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: 91.23 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 378 DSFSERGHkPDSIKGNLEFNDVHFSYPS-RANVKilkGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINID 456
Cdd:TIGR01257 915 DSFFEREL-PGLVPGVCVKNLVKIFEPSgRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 457 GQDIRNfNVNYLREIIGVVSQEPVLFS-TTIAENICYgrgnvtMDEIK-KAVKEANAYEFIMKLPQKFDTLVGERGAQLS 534
Cdd:TIGR01257 991 GKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF------YAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLS 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 535 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLStvrNADVIAgfEDGVIVEQG-- 612
Cdd:TIGR01257 1064 GGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQGrl 1138
|
250 260 270
....*....|....*....|....*....|....*.
gi 9961252 613 --SHSELMKKE----GVYFKLV-NMQTSGSQIQSEE 641
Cdd:TIGR01257 1139 ycSGTPLFLKNcfgtGFYLTLVrKMKNIQSQRGGCE 1174
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1004-1205 |
3.72e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQW---LRAQ-LGIVSQEPILFDCSI 1079
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 A-ENIAY-----GDNSRvVSQDEIVSAAKAANIHPFIETLPhkyetrvgdkgTQLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:PRK10584 105 AlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1154 ATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1205
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
400-612 |
3.96e-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: 84.51 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 400 HFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylreiigvVSQEP 479
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG--------GGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 480 VLfstTIAENIcYGRG---NVTMDEIKKavKEANAYEFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:cd03220 98 EL---TGRENI-YLNGrllGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 557 DEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
410-623 |
4.50e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.95 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN-YLREIIGVVSQEPVLFST-TIA 487
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 ENIcygrgnVTMDEIKKAVKEANAYEFIMKLPQKFDT--LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PRK10895 97 DNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 566 ESEAEVQAALDKARE-GRTTIVIAHR----LSTVRNADVIAgfeDGVIVEQGSHSELMKKEGV 623
Cdd:PRK10895 171 ISVIDIKRIIEHLRDsGLGVLITDHNvretLAVCERAYIVS---QGHLIAHGTPTEILQDEHV 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1000-1215 |
4.52e-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: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNvqwlRAQLGIVSQEPILF-DCS 1078
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAY-----GdnsrvVSQDEIVSAAKAanihpFIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:COG4152 88 VGEQLVYlarlkG-----LSKAEAKRRADE-----WLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1152 DEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:COG4152 154 DEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1002-1202 |
5.74e-18 |
|
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: 88.73 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGTVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-DC 1077
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 SIAENIAYGD----NSRVVSQDEIVSAAKAANIHPFIETLPhkyETR-VGDKGtqlsGGQKQRIAIARALIRQPQILLLD 1152
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1153 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1002-1207 |
8.17e-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: 83.74 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQeakklnVQW-LRAQLGIVSQ----EPILFD 1076
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIaeniaYGdnsrvVSQDEIvsAAKAANIHPFIEtLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:cd03220 109 GRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1157 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1207
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
394-606 |
9.36e-18 |
|
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: 81.34 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqdiRNFNVNYLreiig 473
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 vvsqepvlfsttiaenicygrgnvtmdeikkavkeanayefimklpqkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 554 LLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH-R--LSTVrnADVIAGFEDG 606
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-617 |
1.73e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 398 DVHFSYPSRANVKILKGLNLKVQSGQT---------VALVGSSGCGKSTTVQLIQRLYDP-----DEGTINIDGQDIRNF 463
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 464 -NVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIA 542
Cdd:PRK14271 94 rDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
409-564 |
1.87e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN---YLR-EIIGVVSQEPVLFST 484
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 TIAenicygRGNVTMDEIKKAVKEANAYEFIMKLPQKFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK10584 103 LNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 9961252 561 SALD 564
Cdd:PRK10584 175 GNLD 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
394-623 |
1.99e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-NVNYLREII 472
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEPVLFS-TTIAENICYGRGNVTMDEIKKAVKEAnaYEFIMKLPQKfdtlVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS--TVRNADVIAGFEDGVIVEQGSHSELMKKEGV 623
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
411-592 |
2.34e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ-----------DIRNfnvnylREiIGVVSQ-E 478
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaELRN------QK-LGFIYQfH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 479 PVLFSTTIAEnicygrgNVTMDEI--KKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK11629 97 HLLPDFTALE-------NVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961252 557 DEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS 592
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
386-609 |
2.68e-17 |
|
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: 82.77 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 386 KPDSIKGNLEfndvHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNV 465
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLREIIGVVSQE-------PVLFSTTIAENIcYgrgNVTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQK 538
Cdd:cd03267 91 KFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-Y---DLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 539 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIahrlsTVRNADVIAGFEDGVIV 609
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL-----TSHYMKDIEALARRVLV 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
399-594 |
2.71e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 399 VHFSYPSRANV---KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI---RNFNVNYLREII 472
Cdd:PRK10908 2 IRFEHVSKAYLggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEP-VLFSTTIAENICYGR--GNVTMDEIKKAVKEANAYEFIMKLPQKFDTlvgergaQLSGGQKQRIAIARALVR 549
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 550 NPKILLLDEATSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTV 594
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
422-612 |
2.97e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 422 GQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLREIIGVVSQEPVLfSTTIAENICYGrgnvT 498
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-SLDPRQTVGDS----I 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 499 MDEIK-------KAVKEANAY---------EFIMKLPQKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK10261 425 MEPLRvhgllpgKAAAARVAWllervgllpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 563 LDTESEAE-VQAALDKARE-GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:PRK10261 494 LDVSIRGQiINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1003-1208 |
3.67e-17 |
|
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: 87.76 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAE 1081
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVSAAKAanihpFIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEA-----MLEDtgLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1160 TESEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVFQNGRVKEHGT 1208
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
415-618 |
4.68e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 415 LNLKVQ-----SGQTvALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ---DIRNfNVN---YLREIiGVVSQEPVLFS 483
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK-GIClppEKRRI-GYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 484 -TTIAENICYGrgnvtMDEikkavkeanayefimKLPQKFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKI 553
Cdd:PRK11144 90 hYKVRGNLRYG-----MAK---------------SMVAQFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 554 LLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGS-----HSELM 618
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPleevwASSAM 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1004-1207 |
4.82e-17 |
|
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: 81.03 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFdcsi 1079
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 aENIAYGDNSRVVsqdeivsaakaanihpfietlphkyetrvgDKGtqLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:cd03217 90 -PGVKNADFLRYV------------------------------NEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1160 TESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHG 1207
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
983-1215 |
5.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 983 FEGNITFNEVVFNYPTRA--NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL-----LERFYDPLAGTVLLDGQEAKK 1055
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1056 LNVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSaaKAANIHPFIEtLPHKYETRvgdKGTQLSGGQK 1133
Cdd:PRK13645 83 KEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK--KVPELLKLVQ-LPEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1134 QRIAIARALIRQPQILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG-- 1207
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGsp 235
|
250
....*....|..
gi 9961252 1208 ----THQQLLAQ 1215
Cdd:PRK13645 236 feifSNQELLTK 247
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1003-1153 |
5.95e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPLAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPIL 1074
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 F-DCSIAENIaygdnsRVVSQDEIVSAAKAANIhpfIETLPHKYE-TRVGD-KGTQLSGGQKQRIAIARALIRQPQILLL 1151
Cdd:COG1137 90 FrKLTVEDNI------LAVLELRKLSKKEREER---LEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 9961252 1152 DE 1153
Cdd:COG1137 161 DE 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1005-1212 |
5.97e-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: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFDCSIA-ENI 1083
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 A-----YGDNSRVVSQdeivsaaKAANIHPFIEtLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSAL 1158
Cdd:cd03265 95 YiharlYGVPGAERRE-------RIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1159 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQL 1212
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1003-1203 |
7.43e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.07 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerF--YDPLAGTVLLDGQEAKKLNV-QWLRAQLGIVS----QEPILF 1075
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DCSIAENI---AYGDNSR--VVSQDEIVSAAKAanihpFIETL---PHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQ 1147
Cdd:COG1129 344 DLSIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1148 ILLLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1203
Cdd:COG1129 415 VLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
987-1208 |
8.47e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEP-ILFDCSIAENIAYG----DNSRVVSQD-EIVSAAkaanIHPF-IETLPHKYETrvgdkgtQLSGGQKQRIAIA 1139
Cdd:COG4604 79 ILRQENhINSRLTVRELVAFGrfpySKGRLTAEDrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1140 RALIRQPQILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVFQNGRVKEHGT 1208
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
994-1214 |
8.94e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 994 FNYPT----RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVS 1069
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1070 QEPI-----------LFDCSIAENIAYGDNSRvvsQDEIVSAAKAANIHP-FIETLPHkyetrvgdkgtQLSGGQKQRIA 1137
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQR---EKQIIETLRQVGLLPdHASYYPH-----------MLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1214
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
998-1212 |
1.08e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL---RAQLGIVSQEPIL 1074
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 F-DCSIAENIAYG-----------DNSRVVSQDEIVSAAKAANIHPfietlphkyetrvgdkgTQLSGGQKQRIAIARAL 1142
Cdd:PRK11831 96 FtDMNVFDNVAYPlrehtqlpaplLHSTVMMKLEAVGLRGAAKLMP-----------------SELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1143 IRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1002-1205 |
1.21e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.46 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGTVLLDGQEAKKLNvqwLRA--QLGIV--SQE--- 1071
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 -PILfdcSIAENIAYGdNSR----VVSQDEIVSAAKA------ANIHPfietlphkyETRVGDKGTqlsgGQKQRIAIAR 1140
Cdd:NF040905 90 iPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllakvgLDESP---------DTLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1141 ALIRQPQILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKE 1205
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
753-912 |
1.50e-16 |
|
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: 81.76 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 753 IFSLIFLFLGIISFFTFFLqgftFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 832
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 833 ALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIV---EMKLLAGNAkRDKkeLEAAGKIATEAIENIRTVVSL 909
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
|
...
gi 9961252 910 TQE 912
Cdd:cd18575 192 TRE 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1002-1208 |
1.55e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeakklNVQWLraqLGI-VSQEPILfdcSIA 1080
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgAGFHPEL---TGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENI-----AYGdnsrvVSQDEIvsAAKA------ANIHPFIETlPHKYetrvgdkgtqLSGGQKQRIAIARALIRQPQIL 1149
Cdd:COG1134 107 ENIylngrLLG-----LSRKEI--DEKFdeivefAELGDFIDQ-PVKT----------YSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1150 LLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1208
Cdd:COG1134 169 LVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
412-606 |
1.57e-16 |
|
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: 79.01 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-IGVVSQEP----VLFSTTI 486
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENIcygrgnvtmdeikkavkeanayefimklpqkfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961252 567 SEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDG 606
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
999-1183 |
2.03e-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: 78.94 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 999 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCS 1078
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAY-----GDNSRVVSQdeivsAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:TIGR01189 90 ALENLHFwaaihGGAQRTIED-----ALAAVGLTGFEDLPAA-----------QLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 9961252 1154 ATSALDTESEKVVQEALDkAREGRTCIVIA 1183
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
406-588 |
2.21e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVnylREIIGVVSQ----EPVL 481
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 fstTIAENI-----CYGRGNVTMDEIKKAVKEANayefIMKLPQKFdtlvgergaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK13539 89 ---TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 9961252 557 DEATSALDTESEAEVqAALDKAREGRTTIVIA 588
Cdd:PRK13539 152 DEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1004-1213 |
2.68e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCSIAEN 1082
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IAYG--------DNSRVVSQDEIVSAAKAANIhpfietlphkyeTRVGDKGTQ-LSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGI------------THLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1154 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
137-332 |
3.15e-16 |
|
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: 80.85 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 137 FWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKL 216
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 217 TLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAIS 296
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961252 297 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 332
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGS 254
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1007-1212 |
3.56e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.65 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1007 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLrAQLGIVS--QEPILF-DCSIAENI 1083
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 aygdnsrVVSQDEIVsaaKAANIHPFIET------------LPHKYETRVG-------DKGTqLSGGQKQRIAIARALIR 1144
Cdd:PRK11300 102 -------LVAQHQQL---KTGLFSGLLKTpafrraesealdRAATWLERVGllehanrQAGN-LAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1002-1201 |
3.58e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAK----KLNVQwlrAQLGIVSQEPILFD- 1076
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENIAYGDnsrvvsqdEIVSA----------AKAANIHPFIeTLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQP 1146
Cdd:PRK10762 94 LTIAENIFLGR--------EFVNRfgridwkkmyAEADKLLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1147 QILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNG 1201
Cdd:PRK10762 161 KVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
987-1218 |
3.64e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAkklnVQW-----L 1061
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 RAQLGIVSQEPILFD-CSIAENIAYGD--NSRVVSQDEIVSAakaanihpfIETLPHKYETRVGDKGTqLSGGQKQRIAI 1138
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1139 ARALIRQPQILLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
....*
gi 9961252 1214 AQKGI 1218
Cdd:PRK11614 226 ANEAV 230
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
129-346 |
4.50e-16 |
|
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: 80.63 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 289 IGIK-KAISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAFS 346
Cdd:cd18564 229 AGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPG-DLLVFLAYLKNLYK 285
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
394-609 |
5.95e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.54 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFND--VHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFN---V 465
Cdd:PRK09473 13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPekeL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLR-EIIGVVSQEPVL-------FSTTIAENICYGRG---------NVTMDEikkAVKEANAYEFIMKLPQKFdtlvge 528
Cdd:PRK09473 92 NKLRaEQISMIFQDPMTslnpymrVGEQLMEVLMLHKGmskaeafeeSVRMLD---AVKMPEARKRMKMYPHEF------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 529 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGFEDG 606
Cdd:PRK09473 163 -----SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGICDK 231
|
...
gi 9961252 607 VIV 609
Cdd:PRK09473 232 VLV 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1004-1170 |
6.00e-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: 77.92 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1083
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 AY--GDNSRvvsqDEIVSAAKAANIHPFiETLPhkyetrvgdkGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 9961252 1162 SEKVVQEAL 1170
Cdd:cd03231 160 GVARFAEAM 168
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
987-1202 |
6.42e-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: 75.95 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeakklnvqwlraqlg 1066
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 ivsqepilfdcsiAENIAYgdnsrvvsqdeivsaakaanihpfietlphkYEtrvgdkgtQLSGGQKQRIAIARALIRQP 1146
Cdd:cd03221 62 -------------TVKIGY-------------------------------FE--------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1147 QILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
711-924 |
6.86e-16 |
|
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: 79.78 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQqkcnIFSLIFLFlgIISFFTFFLQGFTFGKAGEILTRRLRSM 790
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGL----LALLVALF--LLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 791 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQgatgtrlALIAQNIANLGTGII-------ISFIYGWQLTLLLLAV 863
Cdd:cd18551 75 LWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLAV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 864 VPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTV-VSLTQERKFESMY--VEKLY 924
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVkASNAEERETKRGGeaAERLY 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1002-1203 |
7.33e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1078
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYEtrVGDkgtqlsggqKQRIAIARALIRQPQILLLDEATSAL 1158
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLE--VAD---------RQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9961252 1159 D-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1203
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
973-1215 |
9.15e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 9.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 973 YSEEGLKPDKFEG--NITFNEVVFNYPTR--ANVPVlqglSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLL 1048
Cdd:PRK10522 307 YKAEFPRPQAFPDwqTLELRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1049 DGQEAKKLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVSQDEivSAAKAANIHPFIETLPHKYETRVGD---KG 1125
Cdd:PRK10522 383 DGKPVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1126 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1203
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
250
....*....|...
gi 9961252 1204 KE-HGTHQQLLAQ 1215
Cdd:PRK10522 528 SElTGEERDAASR 540
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
379-613 |
1.10e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 379 SFSERGHKPDSIKGNLefndVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ 458
Cdd:COG1134 13 SYRLYHEPSRSLKELL----LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 459 dirnfnvnylreiigvVSqePVL-FST------TIAENIcYGRG---NVTMDEIKKAVKEANAY----EFImklpqkfDT 524
Cdd:COG1134 89 ----------------VS--ALLeLGAgfhpelTGRENI-YLNGrllGLSRKEIDEKFDEIVEFaelgDFI-------DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 525 LVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAEVQaalDKAREGRTTIVIAHRLSTVRN-ADV 599
Cdd:COG1134 143 PVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDR 215
|
250
....*....|....
gi 9961252 600 IAGFEDGVIVEQGS 613
Cdd:COG1134 216 AIWLEKGRLVMDGD 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
387-619 |
1.34e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 387 PDSIKGNLEFNDVHFSYPSRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIrn 462
Cdd:TIGR00955 15 AQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 463 fNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDE-IKKAVKEANAYEFI--MKLPQKFDTLVGERGAQ--LSGGQ 537
Cdd:TIGR00955 93 -DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRrVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLST--VRNADVIAGFEDGVIVEQGSH 614
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSP 251
|
....*
gi 9961252 615 SELMK 619
Cdd:TIGR00955 252 DQAVP 256
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
126-335 |
1.59e-15 |
|
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: 78.74 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 126 GVLVAAYIqvSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISK--------ISEGIgdkvgmffQ 197
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 198 AVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 277
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 278 RYQKHLENAKE--------IGIKKAISaNISMGIAFLLIYasyalafWYGSTLVISKEYTIGNAMT 335
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGDLMS 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
999-1215 |
1.66e-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: 81.00 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 999 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV-------LLDGQEAKKLNVQWLRAQLGIVSQE 1071
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 PILF-DCSIAENIaygdnSRVVSQDEIVSAAKAANIHPFIET-LPHKYETRVGDKGT-QLSGGQKQRIAIARALIRQPQI 1148
Cdd:TIGR03269 374 YDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1149 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
393-619 |
2.01e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.02 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 393 NLEFNDVHF---SYPSRANVKIlkglNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD-PDEGT---INIDGQDIRNFNV 465
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 466 NYLREIIG----VVSQEPVlfsTTIaeNICYGRGNVTMDEIK------KAVKEANAYEFImklpqkfdTLVG-----ER- 529
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 530 ---GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGF 603
Cdd:PRK11022 148 dvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVM 227
|
250
....*....|....*.
gi 9961252 604 EDGVIVEQGSHSELMK 619
Cdd:PRK11022 228 YAGQVVETGKAHDIFR 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
409-606 |
2.45e-15 |
|
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: 80.25 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD---EGTINIDGQDIRNFNV-NYLREIIGVVSQEPVLF-S 483
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 484 TTIAENICYG-----RGNVTMDEikKAVKEANAYEFIMKLPQKFDTL-VGERGaqlsGGQKQRIAIARALVRNPKILLLD 557
Cdd:TIGR02633 93 LSVAENIFLGneitlPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 558 EATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:TIGR02633 167 EPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
993-1207 |
2.53e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 993 VFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN---VQWLRAQLGIVS 1069
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1070 QEPILfDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIEtlphkyetRVGDKGT-------QLSGGQKQRIAIARAL 1142
Cdd:PRK10261 408 QDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQRICIARAL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1143 IRQPQILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1207
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
407-617 |
2.67e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD----EGTINIDGQDIrnfNVNYLREI-IGVVSQ---- 477
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV---APCALRGRkIATIMQnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 478 --EPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFdtlvgerGAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:PRK10418 91 afNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 556 LDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
410-625 |
3.50e-15 |
|
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: 75.36 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPD-EGTINIDGQDIrnfNVNYLReIIGVVSQEPVLFsttia 487
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPL---DKNFQR-STGYVEQQDVHS----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 enicygrGNVTmdeikkaVKEanAYEFIMKLpqkfdtlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:cd03232 92 -------PNLT-------VRE--ALRFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 568 EAEVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFeDGVIveqgshseLMKKEG--VYF 625
Cdd:cd03232 144 AYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKF-DRLL--------LLKRGGktVYF 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
986-1212 |
3.93e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITFNEvvfnypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLR--- 1062
Cdd:PRK10261 19 NIAFMQ------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1063 -----------AQLGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSQDEIVSAAKA-------ANIHPFIETLPHky 1117
Cdd:PRK10261 93 qsaaqmrhvrgADMAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKRmldqvriPEAQTILSRYPH-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1118 etrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQ 1190
Cdd:PRK10261 168 ---------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVA 233
|
250 260
....*....|....*....|...
gi 9961252 1191 N-ADLIVVFQNGRVKEHGTHQQL 1212
Cdd:PRK10261 234 EiADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1002-1201 |
4.66e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLG--IVSQEPILFD-CS 1078
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDN-SRVVSQDEIVSAAKA---ANIHPFIETLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:PRK09700 97 VLENLYIGRHlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961252 1155 TSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNG 1201
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
997-1203 |
4.98e-15 |
|
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: 75.83 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 997 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeakklNVQW-----LRAQLGIV--S 1069
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1070 QEPILFDCSIAENIAYgdNSRVVSQDEivsAAKAANIHPFIETLPHkyeTRVGDKGT-QLSGGQKQRIAIARALIRQPQI 1148
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--LAAIYDLPP---ARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1149 LLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
766-923 |
5.93e-15 |
|
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: 76.81 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 766 FFTFFLQG-FTF------GKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaqVQGATGTRLALIAQN 838
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTAD---VQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 839 IANLG--TGIIISFIY-GWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKF 915
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
....*...
gi 9961252 916 ESMYVEKL 923
Cdd:cd18574 204 LELYEEEV 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
409-610 |
6.31e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.06 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD---EGTINIDGQ-----DIRNfnvnylREIIGVV--SQE 478
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD------SEALGIViiHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 479 ----PVLfstTIAENICYG-----RGNVTMDEIKKAVKEanayefIMK---LPQKFDTLVGERGAqlsgGQKQRIAIARA 546
Cdd:NF040905 87 laliPYL---SIAENIFLGnerakRGVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 547 LVRNPKILLLDEATSAL-DTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 610
Cdd:NF040905 154 LSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1005-1213 |
7.16e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWL---------RAQLGIVSQEP--- 1072
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1073 ILFDCSIAENIA----------YGdNSRVVSQD-----EIVSAakaanihpfietlphkyetRVGDKGTQLSGGQKQRIA 1137
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG-DIRATAGDwlervEIDAA-------------------RIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1138 IARALIRQPQILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1210
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTD 237
|
...
gi 9961252 1211 QLL 1213
Cdd:PRK11701 238 QVL 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-609 |
7.55e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVhfSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 473 GVVSQEP-----VLfSTTIAENI--------CYGRGNVtmdeIKKAVKEANAYEFImklpQKFD-------TLVGergaQ 532
Cdd:COG3845 336 AYIPEDRlgrglVP-DMSVAENLilgryrrpPFSRGGF----LDRKAIRAFAEELI----EEFDvrtpgpdTPAR----S 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 609
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
55-332 |
9.01e-15 |
|
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: 76.29 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 55 LFMSLGTIMAIAhgsgLPLMMivfGEMTDKFVDTAGNfSFPVNFSlsllnpgkileeEMTRYAYYYSGLGAGVLVAAYIQ 134
Cdd:cd18547 6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGG-GGGVDFS------------GLLRILLLLLGLYLLSALFSYLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 135 VSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGW 214
Cdd:cd18547 66 NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 215 KLTLVIMAISPILGLSAAVWAKI--------------LSAFsdkelaayakagavAEEALGAIRTVIAFGGQNKELERYQ 280
Cdd:cd18547 146 LLTLIVLVTVPLSLLVTKFIAKRsqkyfrkqqkalgeLNGY--------------IEEMISGQKVVKAFNREEEAIEEFD 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 281 KHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 332
Cdd:cd18547 212 EINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGV 263
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
711-870 |
9.28e-15 |
|
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: 76.27 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQKCNI-----FSLIFLFLGIISFFTFFLQGFTFGKAGEILTR 785
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDLqglllLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVP 865
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
....*
gi 9961252 866 IIAVS 870
Cdd:cd18544 153 LLLLA 157
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
103-331 |
1.26e-14 |
|
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: 75.89 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 103 LNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDIS 182
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 183 KISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGA 262
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 263 IRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 331
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
743-936 |
1.35e-14 |
|
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: 75.81 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 743 DDAVKQQKCNIFSLIFLFLGIISFFTFFLQG-----FTFGKAGeiLTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRL 817
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 818 ATDaaqvqgaTGTRLALIAQNI----ANL--GTG-IIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELE 890
Cdd:cd18784 100 TSD-------TTTMSDTVSLNLniflRSLvkAIGvIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961252 891 AAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRVF--SAIVFG 936
Cdd:cd18784 173 KANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKikEALAYG 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1005-1213 |
1.47e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----LAGTVLLDGqeaKKLNVQWLRAQLGIVSQEPILFDCSIA 1080
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 EN----IAYGDNSRVVSQDE----------IVSAAKAANihpfietlphkyeTRVGDKGTQ--LSGGQKQRIAIARALIR 1144
Cdd:TIGR00955 117 REhlmfQAHLRMPRRVTKKEkrervdevlqALGLRKCAN-------------TRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1145 QPQILLLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1004-1214 |
1.67e-14 |
|
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: 77.92 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGTVL----------------LDGQEAKKLNVQwlraql 1065
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 gIVSQEPILFDCS------IAENIA---------YGDNSRVV----SQDEIVSAAKAAnIHPFIETLPH-KYETRVGDKG 1125
Cdd:TIGR03269 89 -LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1126 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|..
gi 9961252 1203 VKEHGTHQQLLA 1214
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
405-575 |
1.86e-14 |
|
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: 73.30 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFST 484
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 TIAENICYGRGNVTMDEIKKAVKEAN--AYEfimklpqkfDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGlnGFE---------DRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|...
gi 9961252 563 LDTESEAEVQAAL 575
Cdd:cd03231 156 LDKAGVARFAEAM 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
111-558 |
2.31e-14 |
|
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: 77.53 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 111 EEMTRYAYYYSGLGAGVLVAAYI-QVSFWTLAAgRQIRKIRQKFFHAILR------QEIGwfdindTTELNTRLTDDISK 183
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ-HAVARLRLRLSRRILAaplerlERIG------AARLLAALTEDVRT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 184 ISEGigdkvgmFFQAVATFFAGFIVGFirgwklTLVIMA-ISPILGLSAAVWAKILSAF---SDKELAAYAKAGAVAEEA 259
Cdd:COG4615 118 ISQA-------FVRLPELLQSVALVLG------CLAYLAwLSPPLFLLTLVLLGLGVAGyrlLVRRARRHLRRAREAEDR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 260 L-GAIRTVIafGGqNKEL------------ERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLV-IS 325
Cdd:COG4615 185 LfKHFRALL--EG-FKELklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwAD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 326 KEYTIGNAMTVFFsiLIGAfsVGQAAPCIDAFANARGAAyvifdiidnnPKIDSFSERGHKPDSIKGN------------ 393
Cdd:COG4615 262 PAVLSGFVLVLLF--LRGP--LSQLVGALPTLSRANVAL----------RKIEELELALAAAEPAAADaaappapadfqt 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRANVK--ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:COG4615 328 LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPVLFSTTiaenicYGRGNVTMDEikkavkEANAYEFIMKLPQK-------FDTLvgergaQLSGGQKQRIAIA 544
Cdd:COG4615 408 FSAVFSDFHLFDRL------LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALL 469
|
490
....*....|....
gi 9961252 545 RALVRNPKILLLDE 558
Cdd:COG4615 470 VALLEDRPILVFDE 483
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1008-1207 |
3.55e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LAGTVLLDgqEAKKLNVQWLRAQLGIVSQEPILF- 1075
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFD--AEKGICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DCSIAENIAYGDNSRVVSQ-DEIVSAAkaaNIHPFIETLPHKyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:PRK11144 90 HYKVRGNLRYGMAKSMVAQfDKIVALL---GIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1155 TSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVFQNGRVKEHG 1207
Cdd:PRK11144 156 LASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
394-617 |
3.83e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.03 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSypsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL---RE 470
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFS-TTIAENICYG-RGNVTMDE--IKKAVkeanayefIMKLPQkfdtlVGERGA------QLSGGQKQR 540
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKLEA-----VGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEA-------EVQAALdkareGRTTIVIAHR----LSTVRNADVIAgfeDGVIV 609
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGvlvklisELNSAL-----GVTCVVVSHDvpevLSIADHAYIVA---DKKIV 223
|
....*...
gi 9961252 610 EQGSHSEL 617
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
979-1213 |
3.90e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 979 KPDKFEGNITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN- 1057
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1058 ------VQWLRAQL----GIVSQEPIlfdcSIAENIAYGDNSRVVSQD-EIVSAAKA-ANIHPFIEtlphkyetRVGDkg 1125
Cdd:PRK10575 81 kafarkVAYLPQQLpaaeGMTVRELV----AIGRYPWHGALGRFGAADrEKVEEAISlVGLKPLAH--------RLVD-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1126 tQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVFQNG 1201
Cdd:PRK10575 147 -SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGG 224
|
250
....*....|..
gi 9961252 1202 RVKEHGTHQQLL 1213
Cdd:PRK10575 225 EMIAQGTPAELM 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
409-647 |
4.28e-14 |
|
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: 76.76 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRL--YDPDEGTI----------------NIDGQ------------ 458
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 459 --DIRNFNVNYLREIIGVVSqepVLFSTTIAeniCYGRGNVtMDEIKKAVKEAnAYEFIMKLPQKFDTL----VGER--- 529
Cdd:TIGR03269 93 evDFWNLSDKLRRRIRKRIA---IMLQRTFA---LYGDDTV-LDNVLEALEEI-GYEGKEAVGRAVDLIemvqLSHRith 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 530 -GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIAGFED 605
Cdd:TIGR03269 165 iARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 9961252 606 GVIVEQGSHSELMKKegvyFklvnMQTSGSQIQSEEFELNDE 647
Cdd:TIGR03269 245 GEIKEEGTPDEVVAV----F----MEGVSEVEKECEVEVGEP 278
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
410-594 |
4.79e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnvnyLReiIGVVSQEPVLFSTT--IA 487
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYLDTTLplTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 ENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKfdtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*....
gi 9961252 568 EAEVQAALDKARE--GRTTIVIAHRLSTV 594
Cdd:PRK09544 156 QVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
400-621 |
8.73e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 400 HFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPDE-------GTINIDGQDIRNFNVNYLREI 471
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQ--EPVlFSTTIAENICYGR----------GNVTMDEIKKAVKEANAyefimklpqkfDTLVGERGAQLSGGQKQ 539
Cdd:PRK13547 85 RAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 540 RIAIARAL---------VRNPKILLLDEATSALDTESEAEVQAAL-DKARE---GRTTIVIAHRLSTvRNADVIAGFEDG 606
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrRLARDwnlGVLAIVHDPNLAA-RHADRIAMLADG 231
|
250
....*....|....*
gi 9961252 607 VIVEQGSHSELMKKE 621
Cdd:PRK13547 232 AIVAHGAPADVLTPA 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1000-1207 |
1.02e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGTVLLDGQ--EAKKLN---------------- 1057
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvAPCALRgrkiatimqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1058 -VQWLRA-------QLGIVSQEPILFDCsiAENIAYGDNSRVVSqdeivsaakaanIHPFietlphkyetrvgdkgtQLS 1129
Cdd:PRK10418 94 pLHTMHTharetclALGKPADDATLTAA--LEAVGLENAARVLK------------LYPF-----------------EMS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1130 GGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1206
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
.
gi 9961252 1207 G 1207
Cdd:PRK10418 223 G 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
410-590 |
1.29e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLY--DPDEGTINIDGQDIrnfnvnylreiigvvSQEpvlfsTTIA 487
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 ENIcYGRGNVTMD-EIKKAVKEANAYEFImklpQKFDtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:COG2401 104 DAI-GRKGDFKDAvELLNAVGLSDAVLWL----RRFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 9961252 567 SEAEVQAALDK-AREGRTTIVIA-HR 590
Cdd:COG2401 171 TAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
406-613 |
1.29e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--RNFNVNYLREI------------ 471
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 472 IGVVSQEPV-----LFST--TIAENICYGRGnVTMDEikkAVKEANAYEFIMKLPQKfDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG-ASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRT--TIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 613
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1003-1185 |
1.33e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfydplagtVLLDGQEAKKLNVQWLraqlgivsqePILFDCSIAEN 1082
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDN----------QFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1083 IA-YGDNSRVVsqdEIVSAAKAANIHPFIETLPHkyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEATSALDTE 1161
Cdd:COG2401 106 IGrKGDFKDAV---ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 9961252 1162 SEKVVQEALDKA--REGRTCIVIAHR 1185
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHH 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
421-609 |
1.34e-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: 69.32 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 421 SGQTVALVGSSGCGKSTTVQLIQRLYDPDEGT-INIDGQDIRNFNVNYLREIIgvvsqepvlfsttiaenicygrgnvtm 499
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 500 deikkavkeanayefimklpqkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--- 576
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961252 577 ---KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIV 609
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
995-1203 |
1.34e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 995 NYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPLAGTVLLDGQEAKKLNV-QWLRAQLGIVSQE 1071
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1072 P-----ILfDCSIAENIAYGDNSR-------VVSQDEIVSAAKAAnihpfIEtlphKYETRVGDKGT---QLSGGQKQRI 1136
Cdd:COG3845 342 RlgrglVP-DMSVAENLILGRYRRppfsrggFLDRKAIRAFAEEL-----IE----EFDVRTPGPDTparSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1137 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
405-588 |
1.55e-13 |
|
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: 70.47 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFST 484
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 TIAENICYGRGnvTMDEIKKAVKEANAyefimklpqkfdtLVGERG------AQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:TIGR01189 89 SALENLHFWAA--IHGGAQRTIEDALA-------------AVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 9961252 559 ATSALDTESEAEVQAALDkAREGRTTIVIA 588
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
998-1203 |
1.88e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLN-----------VQWLRAQLG 1066
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKyeTRVGdkgtQLSGGQKQRIAIARALIRQP 1146
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHR--TQIG----SLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1147 QILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
412-617 |
2.35e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY-LREIIGVVS----QEPVLFSTTI 486
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENIC------YGRGNVtMDEiKKAVKEANAYefIMKL---PQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:COG1129 348 RENITlasldrLSRGGL-LDR-RRERALAEEY--IKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 558 EATSALDTESEAEVQAALDK-AREGRTTIVIahrlST-----VRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
410-613 |
3.77e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEG----------TINIDGQ---DIRNFnvnylREIIGVVS 476
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRlarDIRKS-----RANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 477 QEPVLFST-TIAENICYGRGNVT------MDEIKKAVKEaNAYEFIMKLPQKFdtLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PRK09984 93 QQFNLVNRlSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 550 NPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGS 613
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
122-345 |
6.61e-13 |
|
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: 70.89 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 122 GLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVAT 201
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 202 FFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQK 281
Cdd:cd18548 127 LIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDK 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 282 HLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-------AMTVFFSILIGAF 345
Cdd:cd18548 207 ANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvafinyLMQILMSLMMLSM 277
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
406-618 |
7.41e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPvlfSTT 485
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 486 IAENICYG-------RGNVTMDeikkavKEANAYEFIMKLPQkfdtlVGERGAQ-------LSGGQKQRIAIARALVRNP 551
Cdd:PRK15112 100 LNPRQRISqildfplRLNTDLE------PEQREKQIIETLRQ-----VGLLPDHasyyphmLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 552 KILLLDEATSALDTESEAE-VQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQlINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
143-335 |
1.03e-12 |
|
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: 70.19 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 143 GRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLV-IM 221
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLtAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 222 AISPILGLSAAV--WAKILSAFSDKELAAYAKAGAvaeEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANI 299
Cdd:cd18589 145 GLPLLLLVPKFVgkFQQSLAVQVQKSLARANQVAV---ETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 9961252 300 SM---GIAFLLIYASyalAFWYGSTLVISKEYTIGNAMT 335
Cdd:cd18589 222 SMwtsSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVT 257
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
987-1186 |
1.12e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQeakklnvqwLRaqLG 1066
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 IVSQEpILFDCSIAENIaygdnSRV------VSQDEIVSAAKAANIHPFIETLPHKyetrvgdkgtqLSGGQKQRIAIAR 1140
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961252 1141 ALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1186
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
415-629 |
1.18e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 415 LNLKVQSGQTVALVGSSGCGKSTtvqLIQRLYD--PDEGTINIDGQDIRNFNVNYLREIIGVVSQE-------PVLFSTT 485
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfamPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 486 IaenicYGRGNVTMDEIKKAVKE-ANAYEFIMKLPqkfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLD 557
Cdd:PRK03695 92 L-----HQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 558 EATSALDTESeaevQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELMKKE------GVYF 625
Cdd:PRK03695 159 EPMNSLDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEnlaqvfGVNF 234
|
....
gi 9961252 626 KLVN 629
Cdd:PRK03695 235 RRLD 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1006-1184 |
1.37e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1006 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKL------NVQWLRAQLGIVS----QEPILF 1075
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 DCSIAeniaygdnsRVVSQDEIVSAAKAANIHPFiETLPHKyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEAT 1155
Cdd:PRK13538 98 YQRLH---------GPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 9961252 1156 SALDTESEKVVQEALDK-AREGRTCIVIAH 1184
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
932-1205 |
2.05e-12 |
|
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: 71.37 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 932 AIVFGAVALGHASSFAPDYAKAKLSAAHL--FMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVP--VLQG 1007
Cdd:COG4615 271 VLLFLRGPLSQLVGALPTLSRANVALRKIeeLELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEgfTLGP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDcsiaeniaygd 1087
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD----------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1088 nsRVVSQDEIVSAAKAaniHPFIETL--PHKyeTRVGDKG---TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1162
Cdd:COG4615 420 --RLLGLDGEADPARA---RELLERLelDHK--VSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF 492
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9961252 1163 EKVVQEAL---DKAReGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1205
Cdd:COG4615 493 RRVFYTELlpeLKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
409-586 |
2.17e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIiGVV----SQ----EPV 480
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 481 LFSTTIAENIcYGrgnVTMDEIKKAVKEANAyefIMKLPQKFDTLVgeRgaQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:COG4586 114 IDSFRLLKAI-YR---IPDAEYKKRLDELVE---LLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180
....*....|....*....|....*..
gi 9961252 561 SALDTESEAEVQAALDK-AREGRTTIV 586
Cdd:COG4586 183 IGLDVVSKEAIREFLKEyNRERGTTIL 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1001-1208 |
2.36e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1001 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGTVLLDGQEAKKLNVQwLRAQLGI----------- 1067
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1068 -VSQEPILfdcsiaeNIAYgdNSRVVSQdeivsaaKAANIHP--FIETLPHKYETrVGDKGTQL--------SGGQKQRI 1136
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKFQ-------GLPELDPleFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1137 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVFQNGRVKEHGT 1208
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
414-589 |
3.03e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 414 GLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREII------GVvsqEPVLfstTIA 487
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 ENI---CYGRGNVTMDEIKKAvkeanayefimkLPQkfdtlVGERG------AQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK13538 93 ENLrfyQRLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|..
gi 9961252 559 ATSALDTESEAEVQAALDK-AREGRTTIVIAH 589
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
987-1189 |
3.35e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG 1066
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1067 iVSQE-----PILFDcSIAENIAYGDNS---RVVSQD-EIVSAAKAAnihpfIETLPHKYEtRVGdkgtQLSGGQKQRIA 1137
Cdd:PRK15056 85 -QSEEvdwsfPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1138 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1189
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
992-1215 |
3.52e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 992 VVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--LAGTVLLDGQE-----AKKLNVqwLRA 1063
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK--LRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1064 -QLGIVSQEP-----------------ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPfietlpHKYetrvgdkg 1125
Cdd:PRK09473 97 eQISMIFQDPmtslnpymrvgeqlmevLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYP------HEF-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1126 tqlSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGR 1202
Cdd:PRK09473 163 ---SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGR 239
|
250
....*....|...
gi 9961252 1203 VKEHGTHQQLLAQ 1215
Cdd:PRK09473 240 TMEYGNARDVFYQ 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
412-594 |
3.92e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfnvnYLRE-IIGVVSQEPVL---FSTTIA 487
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKnLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 ENICYGR-GNVTMDEIKKA-----VKEANAYEFIMKLPQKfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:PRK15056 99 DVVMMGRyGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 9961252 562 ALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV 594
Cdd:PRK15056 172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
398-591 |
4.06e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 398 DVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFNVN--YLREIIGVV 475
Cdd:PRK10982 3 NISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkeALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 476 SQE-PVLFSTTIAENICYGRgnvtmdEIKKA--VKEANAYEFIMKLPQKFDTLVG--ERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK10982 79 HQElNLVLQRSVMDNMWLGR------YPTKGmfVDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961252 551 PKILLLDEATSALdteSEAEVQ---AALDKARE-GRTTIVIAHRL 591
Cdd:PRK10982 153 AKIVIMDEPTSSL---TEKEVNhlfTIIRKLKErGCGIVYISHKM 194
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
987-1201 |
5.19e-12 |
|
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: 66.11 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLerfyDPLA---------GTVLLDGQEAKKL 1056
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LL----DVLAgrktagvitGEILINGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1057 nvqwLRAQLGIVSQEPILFDCS-IAENIAYGDNSRvvsqdeivsaakaanihpfietlphkyetrvgdkgtQLSGGQKQR 1135
Cdd:cd03232 77 ----FQRSTGYVEQQDVHSPNLtVREALRFSALLR------------------------------------GLSVEQRKR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1136 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVFQNG 1201
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
404-588 |
5.67e-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: 66.13 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 404 PSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFNVNYLREIIgVVSQEPV 480
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 481 LFST-TIAEnicygrgnvTMDeikkAVKEANAYEFImklpqkfdtlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:cd03233 94 HFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190
....*....|....*....|....*....|
gi 9961252 560 TSALDTESEAE-VQAALDKAREGRTTIVIA 588
Cdd:cd03233 146 TRGLDSSTALEiLKCIRTMADVLKTTTFVS 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1004-1218 |
6.07e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPilfdcSIAE 1081
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQ--DEIVSAAKAANIHPFIETLpHKYETRvGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALD 1159
Cdd:PRK10895 92 RLSVYDNLMAVLQirDDLSAEQREDRANELMEEF-HIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1160 TESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1218
Cdd:PRK10895 170 PISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
966-1187 |
6.84e-12 |
|
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: 69.78 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 966 RQPLIDSYSEEGLKPDKFEGN----ITFNEVVF-NYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1038
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRgiveYQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1039 YdPLAGTVLLDGQEAKklnvqwlraqLGIVSQEPILFDCSIAENIAYGDNS-----RVVSQDEIVsaAKAANIHpfietL 1113
Cdd:TIGR00954 502 W-PVYGGRLTKPAKGK----------LFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLE--QILDNVQ-----L 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1114 PHKYETRVG-----DKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1187
Cdd:TIGR00954 564 THILEREGGwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
125-331 |
7.08e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.53 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 125 AGVLVAAYIQVSFWTLAAGRQIRK--------IRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:cd18563 46 VLGLAGAYVLSALLGILRGRLLARlgeritadLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 197 QAVATFFAGFIVGFIRGWKLTLVIMAISPILG-LSAAVWAKILSAFSdKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 275
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVwGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKRE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 276 LERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 331
Cdd:cd18563 205 IKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG 260
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
414-612 |
8.58e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 414 GLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--------------RNF-NVNYLREIIGV---- 474
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 475 VSQEPVLFSTTIAenicygrGNVTMDEIKKAvkEANAYEFIMKLPQKFDTL-VGERGA-QLSGGQKQRIAIARALVRNPK 552
Cdd:PRK11300 103 VAQHQQLKTGLFS-------GLLKTPAFRRA--ESEALDRAATWLERVGLLeHANRQAgNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 553 ILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfedgVIVEQG 612
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
411-598 |
8.70e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENi 490
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 CY-----GRGNVTMDEIKKavkeanayefIMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PRK13540 95 CLydihfSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 9961252 566 ESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNAD 598
Cdd:PRK13540 161 LSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-346 |
1.28e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 66.74 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 123 LGAGVLVAA--YIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVA 200
Cdd:cd18550 46 VAVAVASALlgVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 201 TFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGA--IRTVIAFGGQNKELER 278
Cdd:cd18550 126 TLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAAR 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 346
Cdd:cd18550 206 FARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTlvAFTALLGRLYGPLT 275
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
422-612 |
1.35e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 422 GQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREII---------GVVSQEP-------VLFSTT 485
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtewGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 486 IAENIC------YGR---------GNVTMDEIKkavkeanayefIMKLPQKFdtlvgergaqlSGGQKQRIAIARALVRN 550
Cdd:PRK11701 112 IGERLMavgarhYGDiratagdwlERVEIDAAR-----------IDDLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 551 PKILLLDEATSALDTeseaEVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:PRK11701 170 PRLVFMDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
709-928 |
1.74e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 66.82 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 709 PYFVVG-TVCAIANGglQPAFSVIFseiIAIFGPGDdaVKQQkcnifsliFLFLGIISFFTF-------FLQGFTFGKAG 780
Cdd:cd18565 18 PPLLIGvAIDAVFNG--EASFLPLV---PASLGPAD--PRGQ--------LWLLGGLTVAAFlleslfqYLSGVLWRRFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 781 EILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLL 860
Cdd:cd18565 83 QRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 861 LAVVPIIAVSGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVVSLTQERkFESMYVEKLYGPYR 928
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNArleNNLSGIAVIKAFTAED-FERERVADASEEYR 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
363-623 |
1.88e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 363 AAYVIFDIIdNNPKIDSFSERGHKPDSIKG--NLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQ 440
Cdd:PRK10522 291 SAQVAFNKL-NKLALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 441 LIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTtiaenicygrgnvTMDEIKKAVKEANAYEFI--MKL 518
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQ-------------LLGPEGKPANPALVEKWLerLKM 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 519 PQKFdTLVGERGA--QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLSTV 594
Cdd:PRK10522 435 AHKL-ELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYF 513
|
250 260 270
....*....|....*....|....*....|
gi 9961252 595 RNADVIAGFEDGVIVE-QGSHSELMKKEGV 623
Cdd:PRK10522 514 IHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1004-1226 |
2.07e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPLAGTVLLDGqeaKKLNVQWLRaQLGIVSQEPILF-DCSIA 1080
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1081 ENIAYGDNSRV---VSQDEIVSAAKAAnihpFIETLPHKYE-TRVGDKGTQ-LSGGQKQRIAIARALIRQPQILLLDEAT 1155
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVAESV----ISELGLTKCEnTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1156 SALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLLAqkgiYFSMVSVQ 1226
Cdd:PLN03211 235 SGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1014-1198 |
2.59e-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: 62.78 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1014 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVlldgqeakklnvqwlraqlgivsqepILFDCSIAENIAYGDNSrvvs 1093
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLL---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1094 qdeivsaakaanihpfietlphkyETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD-- 1171
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|..
gi 9961252 1172 -----KAREGRTCIVIAHRLSTIQNADLIVVF 1198
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
394-620 |
3.26e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDGQDIRNFN------- 464
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeerahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 465 -----VNYLREIIGVvsqepvlfsttiaENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDtLVGERGAQL------ 533
Cdd:CHL00131 85 giflaFQYPIEIPGV-------------SNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 534 --SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFEDGVI 608
Cdd:CHL00131 151 gfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
250
....*....|..
gi 9961252 609 VEQGShSELMKK 620
Cdd:CHL00131 231 IKTGD-AELAKE 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
403-616 |
5.26e-11 |
|
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: 64.35 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 403 YPSRANVKILKGLNLKVQSG-----QTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFNVNYLReiigvvsq 477
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIK-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 478 epVLFSTTIAEnicygrgnvTMDEIKKAVKEANAYEF-IMKlPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:cd03237 72 --ADYEGTVRD---------LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 557 DEATSALDTESEAEVQAALDKAREG--RTTIVIAHrlsTVRNADVIAgfeDGVIVEQGSHSE 616
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH---DIIMIDYLA---DRLIVFEGEPSV 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
394-620 |
5.38e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKST-TVQLIQRL-YDPDEGTINIDGQDIRNFN------- 464
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 465 -----VNYLREIIGVVSQepvLFSTTIAENICYGRGNVTMD--EIKKAVKEANAyefIMKLPQkfDTLVGERGAQLSGGQ 537
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDrfDFQDLMEEKIA---LLKMPE--DLLTRSVNVGFSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGSH 614
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
....*.
gi 9961252 615 SeLMKK 620
Cdd:PRK09580 231 T-LVKQ 235
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
113-331 |
5.85e-11 |
|
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: 64.80 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 113 MTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKV 192
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 193 GMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKI--------------LSAFsdkelaayakagavAEE 258
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRarkawqrvrkkisnLNAY--------------LHE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 259 ALGAIRTVIAFGGQNKELERYQKHLENAKEIGIkKAISANISMGIAFLLIYA-SYALAFWYGSTLVISKEYTIG 331
Cdd:cd18545 185 SISGIRVIQSFAREDENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG 257
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
711-922 |
9.18e-11 |
|
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: 64.35 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDavkQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRS 789
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIdALTAGTLT---ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 790 MAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18541 78 DLFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 870 SGIVEMKLLagnAKRDKKELEAAGKIATEAIEN---IRTVVSLTQE----RKFESM---YVEK 922
Cdd:cd18541 156 LVYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIKAFVQEeaeiERFDKLneeYVEK 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
410-589 |
9.61e-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: 66.11 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLyDPDegtinIDGQDIR--NFNVNYLreiigvvSQEPVLFST-TI 486
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKD-----FNGEARPqpGIKVGYL-------PQEPQLDPTkTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENICYGrgnvtMDEIKKAVKEANayEFIMKL---PQKFDTLVGERG--------------------------------- 530
Cdd:TIGR03719 86 RENVEEG-----VAEIKDALDRFN--EISAKYaepDADFDKLAAEQAelqeiidaadawdldsqleiamdalrcppwdad 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 531 -AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 589
Cdd:TIGR03719 159 vTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
407-592 |
1.31e-10 |
|
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: 65.54 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqdiRNFNVNYlreiigvVSQEPVLFSTTI 486
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFY-------VPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENICYGRGnvTMDEIKKAVKEANAYEFIMKLpqKFDTLVGERGA---------QLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:TIGR00954 532 RDQIIYPDS--SEDMKRRGLSDKDLEQILDNV--QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961252 558 EATSALDTESEaevQAALDKARE-GRTTIVIAHRLS 592
Cdd:TIGR00954 608 ECTSAVSVDVE---GYMYRLCREfGITLFSVSHRKS 640
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
411-625 |
1.47e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLydpDEGTINiDGQDIRNF---NVNYLReIIGVVSQEPV-LFSTT 485
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVIT-GGDRLVNGrplDSSFQR-SIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 486 IAENICYGRGNVTMDEIKKavKEANAY-EFIMKL---PQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL-LDEAT 560
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 561 SALDTESEAEVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFEDGVIVEQGShselmkkEGVYF 625
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFDRLLLLQKGG-------QTVYF 985
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
991-1193 |
1.82e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 991 EVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWlRAQLGIVSQ 1070
Cdd:PRK13540 6 ELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1071 EP-ILFDCSIAENIAYG--DNSRVVSQDEIVSaakaanihpfIETLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQ 1147
Cdd:PRK13540 82 RSgINPYLTLRENCLYDihFSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9961252 1148 ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1193
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
752-929 |
2.22e-10 |
|
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: 63.13 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 752 NIFSLIFLFLGIISFFTFFLQG-----FTFgkAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG 826
Cdd:cd18590 33 NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 827 AtgtrlalIAQNI----ANLG-TGIIISFIYG--WQLTLLLLAVVPIIAVSgiveMKLLAGNAKRDKKELE----AAGKI 895
Cdd:cd18590 109 S-------VALNAnvllRSLVkTLGMLGFMLSlsWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQdsiaKAGEL 177
|
170 180 190
....*....|....*....|....*....|....
gi 9961252 896 ATEAIENIRTVVSLTQERKFESMYVEKLYGPYRV 929
Cdd:cd18590 178 AREAVSSIRTVRSFKAEEEEACRYSEALERTYNL 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1003-1196 |
2.62e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVLLDG---QEAKKLNVQWL-----RAQLGIVsqepil 1074
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriIYEQDLIVARLqqdppRNVEGTV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FDcSIAENIA--------YGDNSRVVSQDEivSAAKAANIHPFIETLPH----KYETRVGD-----------KGTQLSGG 1131
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDP--SEKNLNELAKLQEQLDHhnlwQLENRINEvlaqlgldpdaALSSLSGG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1132 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIV 1196
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
999-1208 |
2.62e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 999 RANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPLA-------GTVLLDGQEAKKLNVQWL---RAQLGI 1067
Cdd:PRK13547 12 RHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1068 VSQEPILFdcsiaeniaygdnsrvvSQDEIVS-------AAKAANIHPFIETLPHKYE-----TRVGDKGTQLSGGQKQR 1135
Cdd:PRK13547 91 AAQPAFAF-----------------SAREIVLlgryphaRRAGALTHRDGEIAWQALAlagatALVGRDVTTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1136 IAIARAL---------IRQPQILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVFQNGRV 1203
Cdd:PRK13547 154 VQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAI 233
|
....*
gi 9961252 1204 KEHGT 1208
Cdd:PRK13547 234 VAHGA 238
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
711-916 |
3.61e-10 |
|
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: 62.42 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAVKQQKCNIFSLIFLFLGI--ISFFTFFLQGFTFGKAGEILTRRL 787
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 788 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPII 867
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961252 868 AVSgiveMKLLAGNAKRD-KKELEAAGKI---ATEAIENIRTVVSLTQERKFE 916
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAI 207
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
147-338 |
3.73e-10 |
|
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: 62.46 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 147 RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDdISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPI 226
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 227 LGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFL 306
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961252 307 LIYASYALAFWYGSTLVISKEYTIG-----NAMTVFF 338
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGqliafNALLGYF 270
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
756-917 |
4.14e-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: 62.53 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 756 LIFLFLGIISFftffLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALI 835
Cdd:cd18564 62 GIALLRGLASY----AGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 836 AQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIV---EMKLLAgnakRDKKELEAA-GKIATEAIENIRTVVSLTQ 911
Cdd:cd18564 136 LTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRfsrRIKEAS----REQRRREGAlASVAQESLSAIRVVQAFGR 211
|
....*.
gi 9961252 912 ERKFES 917
Cdd:cd18564 212 EEHEER 217
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
711-925 |
4.39e-10 |
|
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: 62.11 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEII--AIFGPGDDAVKqqkcnIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLR 788
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 789 SMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGtRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIA 868
Cdd:cd18543 76 TDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 869 VSGIVEMKLLAGNAKRDKkelEAAGKIATEAIEN---IRTVVSLTQER----KFESMyVEKLYG 925
Cdd:cd18543 153 LVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRERreldRFEAA-ARRLRA 212
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
756-929 |
5.05e-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: 62.10 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 756 LIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALI 835
Cdd:cd18589 40 TVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 836 AQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKF 915
Cdd:cd18589 118 MWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
|
170
....*....|....
gi 9961252 916 ESMYVEKLYGPYRV 929
Cdd:cd18589 198 AQRYRQRLQKTYRL 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1008-1214 |
5.35e-10 |
|
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: 63.31 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PLAGTVLLDGQEAKKLN-VQWLRAQLGIVSQEP----ILFDCSIAE 1081
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVSAAKAANIHPFIETLphKYETRVGDKG-TQLSGGQKQRIAIARALIRQPQILLLDEATSALDT 1160
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 1161 ESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK----EHG-THQQLLA 1214
Cdd:TIGR02633 437 GAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1005-1198 |
8.24e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1005 LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLldgqeaKKLNV----QWLRA-QLGIVSQepil 1074
Cdd:PRK13409 350 LGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKIsykpQYIKPdYDGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1075 FDCSIAENIaygDNSRVvsQDEIvsaakaanIHPFieTLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:PRK13409 420 LLRSITDDL---GSSYY--KSEI--------IKPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9961252 1155 TSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVF 1198
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVF 527
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
990-1187 |
1.09e-09 |
|
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: 60.46 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 990 NEVVFNYPtrANVPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDP---------LAGTVL----- 1047
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPpdwdeildeFRGSELqnyft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1048 --LDGQEAKKLNVQWlraqlgiVSQEPILFDCSIAENIAYGDNSRVvsQDEIVsaaKAANIHPFIETlphkyetrvgdKG 1125
Cdd:cd03236 81 klLEGDVKVIVKPQY-------VDLIPKAVKGKVGELLKKKDERGK--LDELV---DQLELRHVLDR-----------NI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1126 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1187
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1008-1208 |
1.23e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.30 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLR----AQLGIVSQEPI--LFDC 1077
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1078 -----SIAENIAY--GDNSRVVSQD--EIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQI 1148
Cdd:PRK11022 106 ytvgfQIMEAIKVhqGGNKKTRRQRaiDLLNQVGIPDPASRLDVYPH-----------QLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1149 LLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGT 1208
Cdd:PRK11022 175 LIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1003-1215 |
1.50e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFDcs 1078
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVEIP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 iaeniayGDNSRVVSQDEIVSAAKAANIHP--------FIE------TLPHKYETRVGDKGtqLSGGQKQRIAIARALIR 1144
Cdd:PRK09580 92 -------GVSNQFFLQTALNAVRSYRGQEPldrfdfqdLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGTH---QQLLAQ 1215
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
996-1208 |
1.76e-09 |
|
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: 59.73 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 996 YPTRANVPVLQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydplAGTVLLDGQEAKKLNVQwlraqlgiVSQ 1070
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1071 EPilfdcsiaENIAYGDNSRVvsQDEIVSAAKAANIHPFIET---LPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQ 1147
Cdd:cd03237 66 KP--------QYIKADYEGTV--RDLLSSITKDFYTHPYFKTeiaKPLQIEQILDREVPELSGGELQRVAIAACLSKDAD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1148 ILLLDEATSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVFQnGRVKEHGT 1208
Cdd:cd03237 136 IYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
756-916 |
1.78e-09 |
|
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: 60.49 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 756 LIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA--TGTRLA 833
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 834 LIAqnIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQE- 912
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
....*..
gi 9961252 913 ---RKFE 916
Cdd:cd18548 199 yeeERFD 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
991-1214 |
1.91e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 991 EVVF---NY----PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLA--GTVLLDGQEAKKLN-VQW 1060
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKIRNpQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1061 LRAQLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKY---ETRVGdkgtQLSGGQK 1133
Cdd:PRK13549 336 IAQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTaspELAIA----RLSGGNQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1134 QRIAIARALIRQPQILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK---- 1204
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdli 488
|
250
....*....|.
gi 9961252 1205 -EHGTHQQLLA 1214
Cdd:PRK13549 489 nHNLTQEQVME 499
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
711-928 |
2.50e-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: 59.86 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGddavKQQKCNIFSLIFLFLG--IISFFTFFLQGFTFGKAGEILTRRLR 788
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIG----SKSLGLLLGLALLLLGayLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 789 SMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQgatgtRLAL--IAQNIANLGTGIIIS---FIYGWQLTLLLLAV 863
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTLVGVAiilFSINPKLALLTLIP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 864 VPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKfESMYVEKLYGPYR 928
Cdd:cd18778 150 IPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE-EAKRFEALSRRYR 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1002-1202 |
2.55e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1002 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAK-KLNVQWLRAQLGIVSQE-PILFDCSI 1079
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYGDNSR---VVSQDEIVSAAKAANIHPFIETLPHkyetrvgDKGTQLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:PRK10982 91 MDNMWLGRYPTkgmFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1157 ALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVFQNGR 1202
Cdd:PRK10982 164 SL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1008-1213 |
2.56e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1008 LSLEVKKGQTLALVGSSGCGKSTvvqLLERFYD--PLAGTVLLDGQ-----EAKKLNVQwlRAQLgiVSQEPILF----- 1075
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQpleawSAAELARH--RAYL--SQQQTPPFampvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1076 ---DCSIAENIAYGDNSRVVsqDEIVSAAKaanihpfietLPHKYETRVGdkgtQLSGGQKQRIAIArALIRQ------P 1146
Cdd:PRK03695 88 qylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwpdinP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 1147 --QILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1213
Cdd:PRK03695 151 agQLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
419-592 |
2.63e-09 |
|
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: 59.30 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 419 VQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTI--NIDGQDIrnfnvnyLREIIGVVSQEpvLFSTTIAENICYGRGN 496
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddPPDWDEI-------LDEFRGSELQN--YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 497 VTMDEIKKAVKeANAYEFIMKLPQ--KFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:cd03236 94 QYVDLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 9961252 566 ESEAEVQAALDK-AREGRTTIVIAHRLS 592
Cdd:cd03236 173 KQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
125-345 |
2.75e-09 |
|
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: 59.77 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 125 AGVLVAAYI-------QVSFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISE----GIGDkv 192
Cdd:cd18549 45 GAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 193 gmFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 272
Cdd:cd18549 123 --LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANE 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 273 NKELERYQK---HLENAKEIGIKkaISANISMGIAFL--LIYASyALAFwyGSTLVISKEYTIGNAMTvfFSILIGAF 345
Cdd:cd18549 201 EYEIEKFDEgndRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FLLYVNVF 271
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
405-613 |
3.31e-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: 59.17 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQ------LIQRLYDPDEGTINIDGQDirnfNVNYLREIIgVVSQE 478
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHLKKEQPGNHDRIE----GLEHIDKVI-VIDQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 479 PV-------------LFsTTIAE---NICYG-RGNVTMDEIK---KAVKE------ANAYEFIMKLPQ---KFDTLV--- 526
Cdd:cd03271 79 PIgrtprsnpatytgVF-DEIRElfcEVCKGkRYNRETLEVRykgKSIADvldmtvEEALEFFENIPKiarKLQTLCdvg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 527 ------GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN 596
Cdd:cd03271 158 lgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|...
gi 9961252 597 ADVI------AGFEDGVIVEQGS 613
Cdd:cd03271 238 ADWIidlgpeGGDGGGQVVASGT 260
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
711-869 |
8.21e-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: 58.26 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFsvIFSEIIaifgpgDDAVKQQKCNIFSLIFLFL---GIISFFTFFLQGFTFGKAGEILTRRL 787
Cdd:cd18550 3 LVLLLILLSALLGLLPPL--LLREII------DDALPQGDLGLLVLLALGMvavAVASALLGVVQTYLSARIGQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 788 RSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPII 867
Cdd:cd18550 75 RVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLF 152
|
..
gi 9961252 868 AV 869
Cdd:cd18550 153 VL 154
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
411-593 |
8.52e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQ-RLYDPD-EGTINIDGqdiRNFNVNYLREIiGVVSQEPVLFS-TTIA 487
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 488 ENICYGRGNVTMDEIKKAVKEANAYEFI--MKLPQKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|..
gi 9961252 563 LD-TESEAEVQAALDKAREGRTTIVIAHRLST 593
Cdd:PLN03211 237 LDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
998-1196 |
9.36e-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: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLG---IVSQEPI- 1073
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 ------------LFD------CSIAENIAYgdNSRVV-------SQDEIV--SAAKAANIHPFIETLPHKYET------- 1119
Cdd:cd03271 82 rtprsnpatytgVFDeirelfCEVCKGKRY--NRETLevrykgkSIADVLdmTVEEALEFFENIPKIARKLQTlcdvglg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1120 --RVGDKGTQLSGGQKQRIAIARALIRQ---PQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNAD 1193
Cdd:cd03271 160 yiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCAD 239
|
...
gi 9961252 1194 LIV 1196
Cdd:cd03271 240 WII 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
997-1203 |
1.10e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 997 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRaQLGIV----SQep 1072
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1073 ILFDCSIAENIA-----YGdnsrvVSQDEIvsaakAANIHPFIETLphkyetRVGDKGT----QLSGGQKQRIAIARALI 1143
Cdd:COG4586 107 LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELL------DLGELLDtpvrQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1144 RQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1203
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
394-616 |
1.34e-08 |
|
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: 59.18 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIdGQDIRNFNVNYLREIIg 473
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 vvsqEPvlfSTTIAENICYGrgnvtMDEIKKAVKEAN--AY--EFIMKLP--QKfdtLVGergaQLSGGQKQRIAIARAL 547
Cdd:TIGR03719 398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSdqQK---KVG----QLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 548 VRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH-RLSTVRNADVIAGFEDGVIVE--QGSHSE 616
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
395-566 |
1.47e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ-DIRNFNvNYlREIIg 473
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFD-QH-RAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 vvsqEPvlfSTTIAENICYGRGNVTMDEIKKAVKeanAY--EFIMKlPQKFDTLVgergAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*
gi 9961252 552 KILLLDEATSALDTE 566
Cdd:PRK11147 460 NLLILDEPTNDLDVE 474
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
755-869 |
1.69e-08 |
|
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: 57.50 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 755 SLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 834
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110
....*....|....*....|....*....|....*
gi 9961252 835 IAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL 154
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
752-915 |
1.90e-08 |
|
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: 57.07 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGA-TGT 830
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREAiSST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 831 RLALIAQNIANLGTGIIIsFIYGWQLTLLLLAVVPIIAVSGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVV 907
Cdd:cd18570 119 TISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPF---KKKNREVMESNAELNSyliESLKGIETIK 194
|
....*...
gi 9961252 908 SLTQERKF 915
Cdd:cd18570 195 SLNAEEQF 202
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
753-868 |
2.10e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 57.13 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 753 IFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTR 831
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLSDGL 121
|
90 100 110
....*....|....*....|....*....|....*..
gi 9961252 832 LALIAQNIANLGTGIIIsFIYGWQLTLLLLAVVPIIA 868
Cdd:cd18563 122 PDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVV 157
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
99-347 |
2.20e-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: 57.19 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 99 SLSLLNPGKILEEEMTRYAYYYSGL--GAGVL--VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELN 174
Cdd:cd18565 35 SFLPLVPASLGPADPRGQLWLLGGLtvAAFLLesLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 175 TRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGA 254
Cdd:cd18565 115 SVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 255 VAEEALGAIRTVIAFGGQNKELERYQKHLENAKEigikKAISAnISMGIAF-----LLIYASYALAFWYGSTLVISKEYT 329
Cdd:cd18565 195 RLENNLSGIAVIKAFTAEDFERERVADASEEYRD----ANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPL 269
|
250
....*....|....*...
gi 9961252 330 IGNAMTVffsiliGAFSV 347
Cdd:cd18565 270 FTGTLTV------GTLVT 281
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
394-623 |
2.24e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInidgQDIRNFNVNY------ 467
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENANIGYyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 468 --------LREIIGVVSQ----EPVLFSTtiaenicYGRGNVTMDEIKKAVKeanayefimklpqkfdtlvgergaQLSG 535
Cdd:PRK15064 393 ydfendltLFDWMSQWRQegddEQAVRGT-------LGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 536 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFEDGVIV 609
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 9961252 610 EQGSHSELMKKEGV 623
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1011-1208 |
3.00e-08 |
|
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: 57.87 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1011 EVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVLLDGQEA-KKLNV----QWLRAQLGIVSQEpILFDcSIAENIay 1085
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYISPDYDGTVEE-FLRS-ANTDDF-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1086 gDNSRVvsQDEIvsaakaanIHPFieTLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKV 1165
Cdd:COG1245 431 -GSSYY--KTEI--------IKPL--GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961252 1166 VQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFqNGRVKEHGT 1208
Cdd:COG1245 494 VAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVF-EGEPGVHGH 538
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
379-589 |
3.32e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 379 SFSERGHKPDSikgnleFNDVHFSYPSRanVKILKGLNLKVQSGQ-----TVALVGSSGCGKSTTVQLIQRLYDPDEGTI 453
Cdd:PRK13409 325 EFEERPPRDES------ERETLVEYPDL--TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 454 NIDgqdIRnfnVNYLREIIGVVSQEPV-LFSTTIAENIcygRGNVTMDEIKKAvkeanayefiMKLPQKFDTLVGErgaq 532
Cdd:PRK13409 397 DPE---LK---ISYKPQYIKPDYDGTVeDLLRSITDDL---GSSYYKSEIIKP----------LQLERLLDKNVKD---- 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAH 589
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
394-572 |
3.86e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInidgqdIRNFNVNylreiIG 473
Cdd:PLN03073 509 ISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 474 VVSQEPV----LFSTTIaenicygrgnVTMDEIKKAVKEanayefimklpQKFDTLVGERGAQ----------LSGGQKQ 539
Cdd:PLN03073 576 VFSQHHVdgldLSSNPL----------LYMMRCFPGVPE-----------QKLRAHLGSFGVTgnlalqpmytLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 9961252 540 RIAIARALVRNPKILLLDEATSALDTES-EAEVQ 572
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
410-567 |
4.61e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLyDPDegtinIDGQDIR--NFNVNYLreiigvvSQEPVLFST-TI 486
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKE-----FEGEARPapGIKVGYL-------PQEPQLDPEkTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENICYGrgnvtMDEIKKAVKEANAYEFIMKLPQ-KFDTLVGERG----------------------------------A 531
Cdd:PRK11819 88 RENVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvT 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961252 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
123-341 |
5.07e-08 |
|
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: 55.95 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 123 LGAGVLVAAYIQVSFWT---LAAGRQIRkIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGdKVGMFFQAV 199
Cdd:cd18543 46 LALGVAEAVLSFLRRYLagrLSLGVEHD-LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 200 ATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERY 279
Cdd:cd18543 124 LTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRF 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 280 QKHLENAKEIGIKKA-ISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 341
Cdd:cd18543 204 EAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLG-TLVAFSAYL 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1009-1215 |
7.00e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1009 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG--------TVLLDGQEAKKL-NVQWLRAQLGIVSQEPILFDCSI 1079
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIaygdnsrvvsQDEIVSAAK----AANIHpfIETL---PHKYetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLD 1152
Cdd:PRK10938 103 AEII----------QDEVKDPARceqlAQQFG--ITALldrRFKY----------LSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1153 EATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1215
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
385-609 |
8.20e-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: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 385 HKPDSIKGN-LEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD-EGTINIDGQ--DI 460
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 461 RN---------FNVNYLREIIGVVSQEPVLFSTTIAENICY-GRGNVT----MDEIKKAVKEANAYEFIMKLPQkfdtlv 526
Cdd:TIGR02633 328 RNpaqairagiAMVPEDRKRHGIVPILGVGKNITLSVLKSFcFKMRIDaaaeLQIIGSAIQRLKVKTASPFLPI------ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 527 gergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVrnadviAGFED 605
Cdd:TIGR02633 402 ----GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV------LGLSD 471
|
....
gi 9961252 606 GVIV 609
Cdd:TIGR02633 472 RVLV 475
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1003-1218 |
9.40e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVlldgqeakklnvQWL-RAQLGIVSQEP--------I 1073
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1074 LFDCsIAENIAYGDNSRVV---------SQDEIVSAAKAanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIR 1144
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVKV------------------------LSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1145 QPQILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVFQNGRVKEHGTHQQLLAQKGI 1218
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
409-588 |
1.18e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVG--SSGCG---KSTTVQLIQRLYDpDEGTINIDGQDIRNFNVNYLREIIgVVSQEPVLF- 482
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGrpGSGCStllKTIASNTDGFHIG-VEGVITYDGITPEEIKKHYRGDVV-YNAETDVHFp 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 483 STTIAENI-----CYGRGNVTM--DEIKKAVKEANAYEFIMKLPQKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPK 552
Cdd:TIGR00956 152 HLTVGETLdfaarCKTPQNRPDgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAK 229
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961252 553 ILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA 588
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
711-917 |
1.87e-07 |
|
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: 54.38 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQKCN---IFSLIFLFLGIISFF-TFFLQGFtfgkaGEIL--- 783
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYII------DDLLPSKNLRlilIIGAILLALYILRTLlNYFVTYW-----GHVMgar 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 784 -TRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVqgatgTRLA-------LIAqnIANLGTGIIISFIYGWQ 855
Cdd:cd18549 73 iETDMRRDLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 856 LTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELeaaGKI---ATEAIENIRTVVSLTQE----RKFES 917
Cdd:cd18549 144 LTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEInaqLEDSLSGIRVVKAFANEeyeiEKFDE 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1126-1162 |
1.93e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.93e-07
10 20 30
....*....|....*....|....*....|....*..
gi 9961252 1126 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1162
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
417-567 |
1.99e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 417 LKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgQDI----------RNF--NV-NYLREiiGVVSQEPVL-- 481
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivarlqqdppRNVegTVyDFVAE--GIEEQAEYLkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 ---FSTTIAENicYGRGNVT-MDEIKKAVKEANAYEF-------IMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRN 550
Cdd:PRK11147 101 yhdISHLVETD--PSEKNLNeLAKLQEQLDHHNLWQLenrinevLAQLGLDPDAALSS----LSGGWLRKAALGRALVSN 174
|
170
....*....|....*..
gi 9961252 551 PKILLLDEATSALDTES 567
Cdd:PRK11147 175 PDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
708-914 |
2.22e-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: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 708 WPYFVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAvkqqkcNIFSLIFLFLGIISFFTFFLQGFTF--GKAGEILT 784
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIdHFITPGTLD------GLTGFILLYLGLILIQALSVFLFIRlaGKIEMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 785 RRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVV 864
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961252 865 PIIA-VSGIVEMKLLAGNAKRDKKELEAAGKIaTEAIENIRTVVSLTQERK 914
Cdd:cd18540 153 PVLAvVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEK 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
985-1171 |
2.23e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 985 GNITF--NEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVlldgQEAKKLNVQWL- 1061
Cdd:PRK11147 316 GKIVFemENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 --RAQLgivsqEPilfDCSIAENIAYGD-----NSR---VVS--QDEIVSAAKAANihpfietlPHKyetrvgdkgtQLS 1129
Cdd:PRK11147 389 qhRAEL-----DP---EKTVMDNLAEGKqevmvNGRprhVLGylQDFLFHPKRAMT--------PVK----------ALS 442
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961252 1130 GGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD 1171
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1009-1213 |
2.33e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1009 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGqeaKKLNV----QWLRAqlGIV------SQEPILFDCS 1078
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIrsprDAIRA--GIMlcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1079 IAENIAYGDNSRVVSQDEIVSAAK-AANIHPFIETLphKYETRVGD-KGTQLSGGQKQRIAIARALIRQPQILLLDEATS 1156
Cdd:PRK11288 348 VADNINISARRHHLRAGCLINNRWeAENADRFIRSL--NIKTPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 1157 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLL 1213
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
404-594 |
2.48e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 404 PSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD--EGTINIDGQ--DIRN------FNVNYL---RE 470
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDGKpvKIRNpqqaiaQGIAMVpedRK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIAENICYGRGNVtmdeIKKAVKEANAYEFIMKLPQKFDTLVgERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK13549 349 RDGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961252 551 PKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV 594
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEV 468
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
419-591 |
2.85e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 419 VQSGQTVALVGSSGCGKSTTVQLIQrlydpdegtinidGQDIRNFNvNYLREiigvVSQEPVL--FSTTIAENicYGR-- 494
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNLG-DYEEE----PSWDEVLkrFRGTELQN--YFKkl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 495 --GNVT-------MDEIKKAVKeANAYEFIMKLPQ--KFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK13409 156 ynGEIKvvhkpqyVDLIPKVFK-GKVRELLKKVDErgKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961252 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 591
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1126-1162 |
3.02e-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: 54.56 E-value: 3.02e-07
10 20 30
....*....|....*....|....*....|....*..
gi 9961252 1126 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1162
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
125-345 |
3.51e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 53.31 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 125 AGVLVAAYIQVSFWT--------LAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:cd18778 43 ALLLLGAYLLRALLNflriylnhVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 197 QAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 276
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 277 ERYQKHLENAKeigiKKAISANISMGIAFLLIY----ASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAF 345
Cdd:cd18778 203 KRFEALSRRYR----KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGD--LVAFLLYLGLF 269
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
405-612 |
3.55e-07 |
|
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: 51.55 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIqrLYDPDEGTINIDGQdirnfnvNYLREIIGVVSQepvlFST 484
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKARLISFLP-------KFSRNKLIFIDQ----LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 485 TIAENICYgrgnvtmdeikkavkeanayefiMKLPQKFDTLvgergaqlSGGQKQRIAIARALVRNPK--ILLLDEATSA 562
Cdd:cd03238 71 LIDVGLGY-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 563 LDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQG 612
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
123-343 |
3.55e-07 |
|
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: 53.37 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 123 LGAGVLVAAYIQVSF-------WTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLtDDISKISEGIGDKVGMF 195
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 196 FQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAfggQNKE 275
Cdd:cd18782 123 LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 276 L-------ERYQKHLENAKEIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGNAMTvfFSILIG 343
Cdd:cd18782 200 LkarwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
511-617 |
3.56e-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: 54.63 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 511 AYEFIMKLP---QKFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAE----V 571
Cdd:TIGR00630 796 AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKllevL 875
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 572 QAALDKareGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSEL 617
Cdd:TIGR00630 876 QRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
420-593 |
3.59e-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: 54.41 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 420 QSGQTVALVGSSGCGKSTTVQLIQrlydpdegtinidGQDIRNFNvNYLREiigvVSQEPVL--FSTTIAENicYGRgNV 497
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNLG-DYDEE----PSWDEVLkrFRGTELQD--YFK-KL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 498 TMDEIKKAVKEanayEFIMKLPQKFDTLVG-------ERGA-------------------QLSGGQKQRIAIARALVRNP 551
Cdd:COG1245 156 ANGEIKVAHKP----QYVDLIPKVFKGTVRellekvdERGKldelaeklglenildrdisELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9961252 552 KILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLST 593
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1120-1196 |
4.15e-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: 54.63 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1120 RVGDKGTQLSGGQKQRIAIARALIRQ---PQILLLDEATSALDTESEK----VVQEALDKareGRTCIVIAHRLSTIQNA 1192
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTA 898
|
....
gi 9961252 1193 DLIV 1196
Cdd:TIGR00630 899 DYII 902
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
154-343 |
4.60e-07 |
|
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: 52.97 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 154 FHAILRQEIGWFDINDTTELNTRLTDdISKISEgigdkvgmFF--QAVATF----FAG--FIVGFIRGWKLTLVIMAISP 225
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpFVLifLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 226 ILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAF 305
Cdd:cd18566 153 LFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQ 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961252 306 LLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIG 343
Cdd:cd18566 233 LFSQVSMVAVVAFGALLVINGDLTVG--ALIACTMLSG 268
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
401-589 |
5.23e-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: 54.02 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 401 FSYPSRanVKILKGLNLKVQSGQ-----TVALVGSSGCGKSTTVQLIQRLYDPDEGTINidgQDIRnfnVNYLREIIGVV 475
Cdd:COG1245 342 VEYPDL--TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK---ISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 476 SQEPV--LFSTTIAENIcygRGNVTMDEIKKAvkeanayefiMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKI 553
Cdd:COG1245 414 YDGTVeeFLRSANTDDF---GSSYYKTEIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADL 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961252 554 LLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAH 589
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
965-1217 |
5.27e-07 |
|
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: 54.63 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 965 ERQPLIDSyseeGLKPDKFEgnitFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErfydplAG 1044
Cdd:TIGR01257 1924 ERQRIISG----GNKTDILR----LNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT------GD 1988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1045 TVLLDGQeakklnvqwlraqlGIVSQEPILFDCS-IAENIAYGDNSRVVsqDEIVSAAKAANIHPFIETLPHKYETRVGD 1123
Cdd:TIGR01257 1989 TTVTSGD--------------ATVAGKSILTNISdVHQNMGYCPQFDAI--DDLLTGREHLYLYARLRGVPAEEIEKVAN 2052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1124 KGTQ--------------LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLST 1188
Cdd:TIGR01257 2053 WSIQslglslyadrlagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEE 2132
|
250 260 270
....*....|....*....|....*....|
gi 9961252 1189 IQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1217
Cdd:TIGR01257 2133 CEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
416-618 |
5.93e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG---------VVSQEPVLFSTTI 486
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 487 AENIcygrgnvtMDEIKKAvkeanayEFIMKLPQKF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PRK10938 103 AEII--------QDEVKDP-------ARCEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961252 565 TESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:PRK10938 168 VASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
412-648 |
6.15e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnVNYLREIIGVVSQepvlfsTTIAENI- 490
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------VSVIAISAGLSGQ------LTGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 491 ----CYGrgnVTMDEIKKAVKEANAY----EFIMKLPQKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK13546 108 fkmlCMG---FKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 563 LDtesEAEVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKegvYFKLVNMQTSGSQI 637
Cdd:PRK13546 174 GD---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKA 247
|
250
....*....|...
gi 9961252 638 QSEEF--ELNDEK 648
Cdd:PRK13546 248 EQKEFrnKLDESR 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
404-616 |
9.07e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 404 PSRANVKILKG------LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRnfnVNYLREII--GVV 475
Cdd:PRK11288 255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIraGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 476 ------SQEPVLFSTTIAENICYG--RGNVTMDEIKKAVKEA-NAYEFIMKLPQKF---DTLVGergaQLSGGQKQRIAI 543
Cdd:PRK11288 332 lcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAIL 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 544 ARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSE 616
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1003-1214 |
9.85e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1003 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQlGIV------SQEPILFD 1076
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1077 CSIAENI---AYGDNSRVVSQdeIVSAAKAANIHPFIETLPHKYETRVGDKGTqLSGGQKQRIAIARALIRQPQILLLDE 1153
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 1154 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLLA 1214
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
752-914 |
1.06e-06 |
|
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: 51.70 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA-TGT 830
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 831 RLALIAQNIANLGTgIIISFIYGWQLTLLLLAVVPIIAVSgiveMKLLAGNAKRDKKELEAagKIAT------EAIENIR 904
Cdd:cd18545 118 LINLIPDLLTLVGI-VIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARKAWQRVRK--KISNlnaylhESISGIR 190
|
170
....*....|
gi 9961252 905 TVVSLTQERK 914
Cdd:cd18545 191 VIQSFAREDE 200
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
119-345 |
1.19e-06 |
|
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: 51.74 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 119 YYSGLGAGVLVAAYIQVSFwTLAAGRQIRKIR--------QKFFHAILRQEIGWFDINDTTELNTRLtDDISKISEGIGD 190
Cdd:cd18555 40 LLNVLGIGILILFLLYGLF-SFLRGYIIIKLQtkldkslmSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18555 118 QVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLG 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF 345
Cdd:cd18555 198 SEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLG--ELIAFSSLAGSF 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
987-1210 |
1.21e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPtraNVPVL-QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLldgQEAKklnvqwlrAQL 1065
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAK--------VRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GIVSQEPilfdcsiaeniaygdnsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQ----------LSGGQKQR 1135
Cdd:PLN03073 575 AVFSQHH-------------------VDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1136 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVFQNGRVKE-HGTHQ 1210
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
405-600 |
1.28e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTV---------QLIQRLYDP----DEGTI--------NIDGQDIRNF 463
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSnlsiQWGAIsrlvhitrDLPGRSQRSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 464 NVNYLR---EIIGVVSQEP-----------VLFSTTIAENI-CYGRGNVT-MD--------------------EIKKAVK 507
Cdd:PRK00635 684 PLTYIKafdDLRELFAEQPrskrlgltkshFSFNTPLGACAeCQGLGSITtTDnrtsipcpsclgkrflpqvlEVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 508 ------EANAYE---FIMKLP---QKFDTL---------VGERGAQLSGGQKQRIAIARAL---VRNPKILLLDEATSAL 563
Cdd:PRK00635 764 niadilEMTAYEaekFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL 843
|
250 260 270
....*....|....*....|....*....|....*...
gi 9961252 564 DTES-EAEVQAALDKAREGRTTIVIAHRLSTVRNADVI 600
Cdd:PRK00635 844 HTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
409-614 |
1.54e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.93 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDG-----------------QDIRNFNVN--- 466
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSPQVTvre 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 467 ------YLREIIGVVSQEPVLFSTTIAENicygrgnVTMDEIKKAvkeanayefIMKLPqkfdtlvGERGaqLSGGQKQR 540
Cdd:PLN03140 973 sliysaFLRLPKEVSKEEKMMFVDEVMEL-------VELDNLKDA---------IVGLP-------GVTG--LSTEQRKR 1027
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQGSH 614
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1012-1197 |
1.81e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1012 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydplAGTVLLDgqEAKKLNVQWLRAQLGI--V 1068
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1069 SQEPILFDCSIAENIAYGDNSRVVsqDEIVsaaKAANIHPFIetlphkyetrvgDKG-TQLSGGQKQRIAIARALIRQPQ 1147
Cdd:PRK13409 170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENIL------------DRDiSELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1148 ILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVV 1197
Cdd:PRK13409 233 FYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHI 283
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1127-1198 |
1.84e-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: 1.84e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961252 1127 QLSGGQKQRIAIARALIRQPQILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVF 1198
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
429-564 |
2.13e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 429 GSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFNVnylREIIGVVSQEpvlFSTtiaenicYG----RGN------ 496
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---RRRVGYMSQA---FSL-------YGeltvRQNlelhar 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 497 ---VTMDEIKKAVKEanayefimkLPQKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:NF033858 366 lfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
987-1193 |
4.44e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 987 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE----RFYdplAGTVLLDGQEAKKLNVQW-L 1061
Cdd:PRK10938 261 IVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGRRRGSGETIWdI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 RAQLGIVS-------------QEPIL---FDcSIAENIAYGDNSRVVSQD--EIVSAAKAANIHPFietlpHkyetrvgd 1123
Cdd:PRK10938 335 KKHIGYVSsslhldyrvstsvRNVILsgfFD-SIGIYQAVSDRQQKLAQQwlDILGIDKRTADAPF-----H-------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1124 kgtQLSGGQkQRIA-IARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLS 1187
Cdd:PRK10938 401 ---SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLE 474
|
....*.
gi 9961252 1188 TIQNAD 1193
Cdd:PRK10938 475 FVPDGD 480
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
754-923 |
5.40e-06 |
|
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: 49.84 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 754 FSLIFLFLGII-SFFTFFlQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 832
Cdd:cd18605 44 FLTVYGFLAGLnSLFTLL-RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTIDDSLPFIL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 833 ALIAQNIANL-GTGIIISFIYGWqltlLLLAVVPIIAVSGIVEMKLLAGNakRDKKELEAA--GKIAT---EAIENIRTV 906
Cdd:cd18605 121 NILLAQLFGLlGYLVVICYQLPW----LLLLLLPLAFIYYRIQRYYRATS--RELKRLNSVnlSPLYThfsETLKGLVTI 194
|
170
....*....|....*..
gi 9961252 907 VSLTQERKFESMYVEKL 923
Cdd:cd18605 195 RAFRKQERFLKEYLEKL 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
384-591 |
5.63e-06 |
|
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: 51.17 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 384 GHKPDSIKGNlEFNDVHFSYPSRANVKILKGlnlkVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNf 463
Cdd:TIGR01257 1932 GNKTDILRLN-ELTKVYSGTSSPAVDRLCVG----VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 464 NVNYLREIIGVVSQ-EPVLFSTTIAENI-CYGR-GNVTMDEIKKAvkeANAYEFIMKLPQKFDTLVGergaQLSGGQKQR 540
Cdd:TIGR01257 2006 NISDVHQNMGYCPQfDAIDDLLTGREHLyLYARlRGVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961252 541 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRL 591
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
429-600 |
6.31e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 429 GSSGCGKSTTVQLIQRLYDPDEGTINIdgqdiRNFNVNYLreiigvvsQEPvlFSTTIAENICYGRGNVTMDEIKKAVKE 508
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNI--------AKP--YCTYIGHNLGLKLEMTVFENLKFWSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 509 ANAYEFIMKLPQ--KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD-KAREGRTTI 585
Cdd:PRK13541 98 YNSAETLYAAIHyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
|
170
....*....|....*
gi 9961252 586 VIAHRLSTVRNADVI 600
Cdd:PRK13541 178 LSSHLESSIKSAQIL 192
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
419-604 |
6.39e-06 |
|
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: 47.95 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 419 VQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdirnfnvnylreiigvvsqepvlfsttiaenicygrgnvt 498
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 499 mdeIKKAVKeanayefimklPQKFDtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 578
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 9961252 579 RE--GRTTIVIAHRLSTVRN-ADVIAGFE 604
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
375-598 |
8.33e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 375 PKIDSFSERGHKPDSIKgNLEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRlyDPDEGTIN 454
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGYSN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 455 ---IDGQ---------DIRNFnvnylreiIGVVSQEPVL---FSTTIAENICYGrgnvTMDEIK--KAVKEANayefiMK 517
Cdd:PRK10938 317 dltLFGRrrgsgetiwDIKKH--------IGYVSSSLHLdyrVSTSVRNVILSG----FFDSIGiyQAVSDRQ-----QK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 518 LPQKFDTLVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-- 586
Cdd:PRK10938 380 LAQQWLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfv 458
|
250 260
....*....|....*....|..
gi 9961252 587 ----------IAHRLSTVRNAD 598
Cdd:PRK10938 459 shhaedapacITHRLEFVPDGD 480
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
121-338 |
8.59e-06 |
|
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: 49.02 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 121 SGLGAGVLVAAYIQVSFWTLAAGRQ----IRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 197 QAVATFFAGFIVGFIRGWKLTLVIMAISPILGLsAAVW----------------AKILSAFSdkelaayakagavaeEAL 260
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWfrrrssrayrrareriAAVNADLQ---------------ETL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 261 GAIRTVIAFGGQNKELERYQKHLENAKEIGIKkaisANISMGIAF----LLIYASYALAFWYGSTLVISKEYTIGnAMTV 336
Cdd:cd18546 186 AGIRVVQAFRRERRNAERFAELSDDYRDARLR----AQRLVAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTVG-VLVA 260
|
..
gi 9961252 337 FF 338
Cdd:cd18546 261 FL 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
998-1205 |
9.04e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPLA-GTVLLDGQEAK-KLNVQWLRAQLGIVSQ--- 1070
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1071 EPILF-DCSIAENIAygdnsrvvsqdeIVSAAKAANIHPFIETLPHKYETRVGDKG---------------TQLSGGQKQ 1134
Cdd:PRK09700 349 DNGFFpNFSIAQNMA------------ISRSLKDGGYKGAMGLFHEVDEQRTAENQrellalkchsvnqniTELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961252 1135 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGRVKE 1205
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1088-1202 |
9.53e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1088 NSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGD---KGtqLSGGQKQRIAIARALIRQPQILLLDEATSALDTESek 1164
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 9961252 1165 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVFQNGR 1202
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1128-1199 |
9.95e-06 |
|
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: 47.57 E-value: 9.95e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1128 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQ 1199
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
114-233 |
1.05e-05 |
|
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: 48.65 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 114 TRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKV 192
Cdd:cd18580 38 GYYLGVYAALLVLASVLLVLLRWLLFVLAGLRAsRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLAL 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 9961252 193 GMFFQAVATFFAGFIvgfirgwkltlVIMAISPILGLSAAV 233
Cdd:cd18580 118 LDFLQSLFSVLGSLI-----------VIAIVSPYFLIVLPP 147
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1004-1188 |
1.05e-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: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLdGQEAKklnvqwlraqLGIVSQ--EPILFDCSIAE 1081
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1082 NIAYGDNSRVVSQDEIVSAAkaanihpfietlphkYETRVGDKGT-------QLSGGQKQRIAIARALIRQPQILLLDEA 1154
Cdd:TIGR03719 406 EISGGLDIIKLGKREIPSRA---------------YVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9961252 1155 TSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1188
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
113-345 |
1.35e-05 |
|
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: 48.63 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 113 MTRYA-------------YYYSGLGAGVLVAAYIQVSFWTLAAGRQ----IRKIRQKFFHAILRQEIGWFDINDTTELNT 175
Cdd:cd18540 24 LTKYAidhfitpgtldglTGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 176 RLTDDISKISE----GIGDkvgmFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLsAAVW----------------A 235
Cdd:cd18540 104 RVTSDTQRLGEiiswGLVD----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV-VSIYfqkkilkayrkvrkinS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 236 KILSAFSdkelaayakagavaeEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALA 315
Cdd:cd18540 179 RITGAFN---------------EGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALV 243
|
250 260 270
....*....|....*....|....*....|
gi 9961252 316 FWYGSTLVISKEYTIGnAMTVFFSILIGAF 345
Cdd:cd18540 244 LWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
206-346 |
1.51e-05 |
|
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: 48.26 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 206 FIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 285
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961252 286 AKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS 346
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIG--QLIAFNMLAGQVS 271
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1000-1198 |
2.21e-05 |
|
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: 46.16 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1000 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQllERFYdplagtvlldgQEAKKLNVQWLRAqlgiVSQEPILFDCSI 1079
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY-----------ASGKARLISFLPK----FSRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1080 AENIAYGdnsrvvsqdeivsaakaanihpfIETLPhkyetrVGDKGTQLSGGQKQRIAIARALIRQPQ--ILLLDEATSA 1157
Cdd:cd03238 69 QFLIDVG-----------------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961252 1158 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVF 1198
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1022-1195 |
2.33e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1022 GSSGCGKSTVVQLLERFYDPLAGTVL---LDGQEAKKLNVQWLRAQLGIVSqepilfDCSIAENIAYGdnSRVVSQDEIV 1098
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYCTYIGHNLGLKL------EMTVFENLKFW--SEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1099 SAAkaanIHPFietlphKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD-KAREGR 1177
Cdd:PRK13541 105 YAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 9961252 1178 TCIVIAHRLSTIQNADLI 1195
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1004-1170 |
2.88e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1004 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLdgqeAKKLnvqwlraQLGIVSQEpilfdcsiaeni 1083
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLGYFAQH------------ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1084 aygdnsrvvsQDEIVSAAKAANIHpFIETLPHKYETRV----------GDKGT----QLSGGQKQRIAIARALIRQPQIL 1149
Cdd:PRK10636 384 ----------QLEFLRADESPLQH-LARLAPQELEQKLrdylggfgfqGDKVTeetrRFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 9961252 1150 LLDEATSALDTESEKVVQEAL 1170
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
405-621 |
3.79e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSttvQLIQRLYDPD---EGTINIDGQDIR-NFNVNYLREIIGVVSQ--- 477
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDkraGGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 478 EPVLFST-TIAENICYGR--------GNVTMDEIKKAVKEANAYEFIMKLpqKFDTlVGERGAQLSGGQKQRIAIARALV 548
Cdd:PRK09700 349 DNGFFPNfSIAQNMAISRslkdggykGAMGLFHEVDEQRTAENQRELLAL--KCHS-VNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 549 RNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
412-588 |
4.61e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN-----------VNYLREIIGVVSQEPV 480
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 481 LFSTTIAeNICYGRGNVTMDEIKKAVKEANAYEFIM--KLPQKfDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK10982 344 GFNSLIS-NIRNYKNKVGLLDNSRMKSDTQWVIDSMrvKTPGH-RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190
....*....|....*....|....*....|.
gi 9961252 559 ATSALDTESEAEV-QAALDKAREGRTTIVIA 588
Cdd:PRK10982 418 PTRGIDVGAKFEIyQLIAELAKKDKGIIIIS 448
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
409-610 |
4.84e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVqLIQRLYDPDEGTinidgqdiRNF-------NVNYLREIIGVvsQEPVL 481
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWrf*twcaNRRALRRTIG*--HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 482 FSTTIAENicyGRGNVTMD----EIKKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:NF000106 95 *GRRESFS---GRENLYMIgr*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961252 558 EATSALDTESEAEV-QAALDKAREGRTTIV----------IAHRLSTVRNADVIAgfeDGVIVE 610
Cdd:NF000106 170 EPTTGLDPRTRNEVwDEVRSMVRDGATVLLttqymeeaeqLAHELTVIDRGRVIA---DGKVDE 230
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
199-345 |
5.51e-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: 46.40 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 199 VATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 278
Cdd:cd18568 126 LLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWR 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 345
Cdd:cd18568 206 WENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQlvAFNMLFGSVINPL 274
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
533-571 |
5.63e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 5.63e-05
10 20 30
....*....|....*....|....*....|....*....
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 571
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1127-1219 |
5.94e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1127 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARegRTCIVIAHRLStiqnadlivvFQNGRVKE- 1205
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHARE----------FLNTVVTDi 411
|
90
....*....|....*
gi 9961252 1206 -HGTHQQLLAQKGIY 1219
Cdd:PLN03073 412 lHLHGQKLVTYKGDY 426
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
757-869 |
6.48e-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: 46.31 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 757 IFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIA 836
Cdd:cd18606 40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD--TTPLGRILNRFSKDTDVLDNELPDSLRMFL 117
|
90 100 110
....*....|....*....|....*....|...
gi 9961252 837 QNIANLGTGIIISFIYgwqLTLLLLAVVPIIAV 869
Cdd:cd18606 118 YTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1120-1196 |
7.15e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1120 RVGDKGTQLSGGQKQRIAIARALIRQPQ---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1192
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 9961252 1193 DLIV 1196
Cdd:PRK00349 900 DWII 903
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
986-1159 |
7.94e-05 |
|
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: 44.95 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 986 NITFNEvvfnYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPlAGTVLLDGQEAKKLNVQWL 1061
Cdd:cd03233 8 NISFTT----GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1062 RaqlgivsqepilfdcsiaeNIAYgdnsrvVSQDEIvsaakaaniHPFIETLPHKYETRVGDKGTQ----LSGGQKQRIA 1137
Cdd:cd03233 83 G-------------------EIIY------VSEEDV---------HFPTLTVRETLDFALRCKGNEfvrgISGGERKRVS 128
|
170 180
....*....|....*....|..
gi 9961252 1138 IARALIRQPQILLLDEATSALD 1159
Cdd:cd03233 129 IAEALVSRASVLCWDNSTRGLD 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
532-589 |
1.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARegRTTIVIAH 589
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1122-1217 |
1.39e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1122 GDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQ 1199
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 9961252 1200 NGRVKEHGTHQQLLAQKG 1217
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
117-233 |
1.42e-04 |
|
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: 45.15 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 117 AYY---YSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVG 193
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLS 122
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 9961252 194 MFFQAVATFFAGFIvgfirgwkltlVIMAISPILGLSAAV 233
Cdd:cd18604 123 SLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
532-603 |
1.67e-04 |
|
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: 43.50 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 532 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTEseaEVQAALDKARE----GRTTIVIAHRLSTVRNADVIAGF 603
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
716-946 |
2.57e-04 |
|
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: 44.51 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 716 VCAIANGGLQPAFSVIFSEIIaifgpgdDAVKQQKcNIFSLIFLFLGIISFFTF-----FLQGFTFGKAGEILTRRLRSM 790
Cdd:cd18782 9 ALSFVVQLLGLANPLLFQVII-------DKVLVQQ-DLATLYVIGVVMLVAALLeavltALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 791 AFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQG-ATGTRLALIAQNIANLGTgIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18782 81 IIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 870 SGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVVSLTQERKFESMYvEKLYGPY--RVFSAIVFGAvALGHAS 944
Cdd:cd18782 157 LTFLFGPIL---RRQIRRRAEASAKTQSylvESLTGIQTVKAQNAELKARWRW-QNRYARSlgEGFKLTVLGT-TSGSLS 231
|
..
gi 9961252 945 SF 946
Cdd:cd18782 232 QF 233
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
752-915 |
3.48e-04 |
|
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: 44.04 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRlATDAAQVQGATGTR 831
Cdd:cd18555 42 NVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQILSNQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 832 LALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLagnAKRDKKELEAAGK---IATEAIENIRTVVS 908
Cdd:cd18555 119 VISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKI---KKLNQEEIVAQTKvqsYLTETLYGIETIKS 195
|
....*..
gi 9961252 909 LTQERKF 915
Cdd:cd18555 196 LGSEKNI 202
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1127-1196 |
3.60e-04 |
|
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: 42.35 E-value: 3.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1127 QLSGGQKQRIAIARAL----IRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1196
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1127-1214 |
3.94e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1127 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1203
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 9961252 1204 KEHGTHQQLLA 1214
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
533-612 |
4.62e-04 |
|
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: 43.02 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 533 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGF 603
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGV 217
|
....*....
gi 9961252 604 EDGVIVEQG 612
Cdd:cd03270 218 HGGEIVAQG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
404-587 |
4.65e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 404 PSRANVKILKGLNLKVQSGQTVALVGSSGCGKS-TTVQLIQRLYDPD-EGTINIDGQDIRNFNVN--------YL---RE 470
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVDVSTVSdaidaglaYVtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 471 IIGVVSQEPVLFSTTIA--ENICygRGNVtMDEIKKaVKEANAYEFIM--KLPQkfdtlVGERGAQLSGGQKQRIAIARA 546
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlGKVS--RRGV-IDENEE-IKVAEEYRKKMniKTPS-----VFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961252 547 LVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVI 587
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVI 460
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
761-946 |
6.78e-04 |
|
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: 43.34 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 761 LGIISFFTFFLQGF---TFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQGATGTRLALIAQ 837
Cdd:cd18566 48 VVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 838 NIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQE----R 913
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEpqmlR 204
|
170 180 190
....*....|....*....|....*....|...
gi 9961252 914 KFESMYVEKLYGPYRVfsaIVFGAVALGHASSF 946
Cdd:cd18566 205 RYERLQANAAYAGFKV---AKINAVAQTLGQLF 234
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
511-624 |
7.94e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 511 AYEF---IMKLPQKFDTLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA---EV- 571
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRkllEVl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 572 QAALDKareGRTTIVIAHRLSTVRNADVIA--GFEDGV----IVEQGSHSELMKKEGVY 624
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIIdlGPEGGDgggeIVATGTPEEVAKVEASY 932
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
998-1217 |
8.77e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 998 TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGtvlldgqeAKKL---NVQWL---------RAQL 1065
Cdd:NF033858 14 TVA----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AG--------ARKIqqgRVEVLggdmadarhRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1066 GivsqeP-ILF-----------DCSIAENIAY-GdnsRVVSQDE------IVSAAKAANIHPFIEtlphkyetRVGDKgt 1126
Cdd:NF033858 75 C-----PrIAYmpqglgknlypTLSVFENLDFfG---RLFGQDAaerrrrIDELLRATGLAPFAD--------RPAGK-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 1127 qLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---DLIV 1196
Cdd:NF033858 137 -LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfDWLV 208
|
250 260
....*....|....*....|.
gi 9961252 1197 VFQNGRVKEHGTHQQLLAQKG 1217
Cdd:NF033858 209 AMDAGRVLATGTPAELLARTG 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
532-618 |
1.12e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 9961252 609 VEQGSHSELM 618
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1121-1187 |
1.14e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 1121 VGDKG-TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLS 1187
Cdd:PLN03140 1012 VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
754-883 |
1.17e-03 |
|
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: 42.49 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 754 FSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLA 833
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD--TTPSGRILNRFSKDIGLIDEELPLALL 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 834 LIAQNIANLGTGIIISFIYGWqltLLLLAVVPIIAVSGIV---------EMKLLAGNAK 883
Cdd:cd18580 119 DFLQSLFSVLGSLIVIAIVSP---YFLIVLPPLLVVYYLLqryylrtsrQLRRLESESR 174
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
504-600 |
1.61e-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: 41.05 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 504 KAVKEANAYEFIMKLPQ-KFDTLVGERGAQLSGGQKQ------RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD 576
Cdd:cd03240 86 TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEII 165
|
90 100
....*....|....*....|....*..
gi 9961252 577 KAREG---RTTIVIAHRLSTVRNADVI 600
Cdd:cd03240 166 EERKSqknFQLIVITHDEELVDAADHI 192
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1126-1196 |
1.74e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961252 1126 TQLSGGQKQRIAIARALIRQPQ---ILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1196
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
533-608 |
2.67e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 2.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961252 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
419-439 |
3.90e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 3.90e-03
10 20
....*....|....*....|.
gi 9961252 419 VQSGQTVALVGSSGCGKSTTV 439
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLV 212
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1005-1035 |
3.97e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 3.97e-03
10 20 30
....*....|....*....|....*....|..
gi 9961252 1005 LQGLSLEVKKGQTLALVGSSGCGKSTVV-QLL 1035
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
496-621 |
5.12e-03 |
|
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: 41.15 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961252 496 NVTMDEIKKAVKEANAYEFIMKLpqKFDTLVG------ERGAQ-LSGGQKQRIAIARAL------VrnpkILLLDEATSA 562
Cdd:TIGR00630 447 QLTLTPEEKKIAEEVLKEIRERL--GFLIDVGldylslSRAAGtLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIG 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961252 563 L---DTESEAEVqaaLDKARE-GRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSELMKKE 621
Cdd:TIGR00630 521 LhqrDNRRLINT---LKRLRDlGNTLIVVEHDEDTIRAADYVidigpgAGEHGGEVVASGTPEEILANP 586
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1128-1196 |
6.90e-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: 6.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961252 1128 LSGGQKQRIAIARALIRQPQ--ILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1196
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| |
