|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-1314 |
1.65e-169 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 544.24 E-value: 1.65e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 29 DKKSRLQDKKKGEGARVGFFELFRFSSSKDNWLMFMGSVCALLHGMAQPGMIIVFGILTdifveydierqelsipekvcm 108
Cdd:PTZ00265 29 NKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIM--------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 109 nntivwinssfnQNMTNGTscglvDINSevIKFSgiyagvgvaVLILGYFQIRLWVITG------ARQIRKMRKFYFRRI 182
Cdd:PTZ00265 88 ------------KNMNLGE-----NVND--IIFS---------LVLIGIFQFILSFISSfcmdvvTTKILKTLKLEFLKS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 183 MRMEIGWFDCTSVG-ELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGL 261
Cdd:PTZ00265 140 VFYQDGQFHDNNPGsKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 262 SVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAF 341
Cdd:PTZ00265 220 KVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 342 WYGSRLVLDE-------GEYTPGTLIQIFLCVIIAAMNIGNASSCLEIFSTGCSAASSIFQTIDRQPVMDcMSGDGYKLD 414
Cdd:PTZ00265 300 WYGTRIIISDlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE-NNDDGKKLK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 415 RIKgEIEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTL-DGHDIRSLNIRW 493
Cdd:PTZ00265 379 DIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKW 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQEPVLFSTTIAENIR-------------------------------------------------------L 518
Cdd:PTZ00265 458 WRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnelieM 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 519 GREEATMED--IVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAK 596
Cdd:PTZ00265 538 RKNYQTIKDseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 597 VQGALNKIQHGH---TIIsVAHRLSTVRSADVI----------------------------------------------- 626
Cdd:PTZ00265 618 VQKTINNLKGNEnriTII-IAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnk 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 627 IGFEHGTAVERGTHEELLERK-GVYFMLVTLQSQEDNTHKETGiKGKDTTEGDTPERTFSRGSYQDSLRASIRQRSKSql 705
Cdd:PTZ00265 697 INNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNND-NDKDSDMKSSAYKDSERGYDPDEMNGNSKHENES-- 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 706 shLSHEPPLAIGDHKSSYEDRKDNDVLVEEV------EPAPVRRILKYNISEWPYILVGALCAAINGAVTPIYSLLFSQI 779
Cdd:PTZ00265 774 --ASNKKSCKMSDENASENNAGGKLPFLRNLfkrkpkAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKY 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 780 LKTFSLVDKEQQRSEIYSmcLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDDLKNNPGVLTT 859
Cdd:PTZ00265 852 VSTLFDFANLEANSNKYS--LYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSA 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 860 RLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVIS-VFFPF---------LALSGAVQTKML----TGF 925
Cdd:PTZ00265 930 HINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTgTYFIFmrvfairarLTANKDVEKKEInqpgTVF 1009
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 926 A-SQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGG 1004
Cdd:PTZ00265 1010 AyNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGS 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1005 YLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPIDVYSGAGEKWDN---FQGKIDFI 1081
Cdd:PTZ00265 1090 FLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIM 1169
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1082 DCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD------------------------------ 1131
Cdd:PTZ00265 1170 DVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqn 1249
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1132 ------------------------PDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYG--DNTKEiSV 1185
Cdd:PTZ00265 1250 vgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGkeDATRE-DV 1328
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1186 ERaiaAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLAL---- 1261
Cdd:PTZ00265 1329 KR---ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1405
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1262 DKAreGRTCIVIAHRLSTIQNSDIIAVMSQ-----GVVIEKGTHKKLMD-QKGAYYKLV 1314
Cdd:PTZ00265 1406 DKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSvQDGVYKKYV 1462
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
739-1314 |
6.16e-160 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 491.99 E-value: 6.16e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 739 APVRRILKYNISEWPYILVGALCAAINGAVTPIYSLLFSQILKTFSLvdkEQQRSEIYSMCLFFVILGCVSLFTQFLQGY 818
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLA---GGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 819 NFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNW 898
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 899 KLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKA 978
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 979 NVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLN-------FSYVFRVVSSIAMSATAVGrtfsytpSYAKAKISAARF 1051
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTvgdlvafILYLLRLFGPLRQLANVLN-------QLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1052 FQLLDRKPPIDVYSGAGEKwDNFQGKIDFIDCKFTYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD 1131
Cdd:COG1132 315 FELLDEPPEIPDPPGAVPL-PPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1132 PDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDntKEISVERAIAAAKQAQLHDFVMSLPEKYETN 1211
Cdd:COG1132 392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR--PDATDEEVEEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1212 VGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQ 1291
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
570 580
....*....|....*....|...
gi 1390249242 1292 GVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:COG1132 550 GRIVEQGTHEELLARGGLYARLY 572
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
136-661 |
3.38e-156 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 481.97 E-value: 3.38e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 136 SEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIAD 215
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 216 QMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFG 295
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 296 GENKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQIFLCVIIAAMNIGN 375
Cdd:COG1132 218 REERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-GSLTVGDLVAFILYLLRLFGPLRQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 376 ASSCLEIFSTGCSAASSIFQTIDRQPVMDCmSGDGYKLDRIKGEIEFHNVTFHYPsrPEVKILNNLSMVIKPGETTAFVG 455
Cdd:COG1132 297 LANVLNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 456 SSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDA 535
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 536 NAYNFIMALPQQFDTLVgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAH 615
Cdd:COG1132 454 QAHEFIEALPDGYDTVVgergvnlsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1390249242 616 RLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTLQSQED 661
Cdd:COG1132 534 RLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1078-1314 |
4.79e-138 |
|
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: 420.79 E-value: 4.79e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFDCSIMDNIKYGDNtkEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
420-657 |
5.04e-129 |
|
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: 396.91 E-value: 5.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKI 579
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTLQ 657
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
745-1061 |
1.26e-127 |
|
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: 396.05 E-value: 1.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 745 LKYNISEWPYILVGALCAAINGAVTPIYSLLFSQILKTFSLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSG 824
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 825 ELLTKRLRKFGFKAMLRQDIGWFDDLKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVI 904
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 905 SVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLC 984
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 985 YAFSQGISFLANSAAYRYGGYLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPI 1061
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
146-657 |
2.40e-125 |
|
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: 404.60 E-value: 2.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 146 AGVGVAVL---ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDdINKIDEAIADQMALFLQ 222
Cdd:COG2274 200 IGLLLALLfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 223 RLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVE 302
Cdd:COG2274 279 DLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 303 RYEK------NLMF-AQRWGIWKGMVMGFFTGymwclifFCYALAFWYGSRLVLDeGEYTPGTLI--QIFLCVIIAAMN- 372
Cdd:COG2274 359 RWENllakylNARFkLRRLSNLLSTLSGLLQQ-------LATVALLWLGAYLVID-GQLTLGQLIafNILSGRFLAPVAq 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 373 -IGNASSCLEIFStgcsAASSIFQTIDRQPvmDCMSGDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNNLSMVIKPGET 450
Cdd:COG2274 431 lIGLLQRFQDAKI----ALERLDDILDLPP--EREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGER 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 451 TAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQ 530
Cdd:COG2274 504 VAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 531 AAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTI 610
Cdd:COG2274 584 AARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV 663
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1390249242 611 ISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTLQ 657
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
734-1314 |
4.60e-120 |
|
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: 390.35 E-value: 4.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 734 EEVEPAPVRRILKYNISEWP---YILVGALCAAINGAVTPiyslLFSQILktfslVDK---EQQRSEIYSMCLFFVILGC 807
Cdd:COG2274 137 RGEKPFGLRWFLRLLRRYRRlllQVLLASLLINLLALATP----LFTQVV-----IDRvlpNQDLSTLWVLAIGLLLALL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 808 VSLFTQFLQGYNFAKSGELLTKRL-RKFgFKAMLRQDIGWFDdlKNNPGVLTTRLaTDASQVQGA-TGSQVGMMVNSFTn 885
Cdd:COG2274 208 FEGLLRLLRSYLLLRLGQRIDLRLsSRF-FRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFlTGSLLTALLDLLF- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 886 IFVAVLIAFLFNWKLSLVISVFFPFLALSGAVQTKMLtgfASQDKEILEKAGQITN---EALSNIRTVAGIGVEGRFIKA 962
Cdd:COG2274 283 VLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL---RRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 963 FEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLNF-------SYVFRVVSSIAmsatavgRTF 1035
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliafnILSGRFLAPVA-------QLI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1036 SYTPSYAKAKISAARFFQLLDRKPPIDVYSGAGEKwDNFQGKIDFIDCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSS 1115
Cdd:COG2274 433 GLLQRFQDAKIALERLDDILDLPPEREEGRSKLSL-PRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1116 GCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDntKEISVERAIAAAKQA 1195
Cdd:COG2274 511 GSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1196 QLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAH 1275
Cdd:COG2274 589 GLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
570 580 590
....*....|....*....|....*....|....*....
gi 1390249242 1276 RLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:COG2274 669 RLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
739-1314 |
1.09e-117 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 384.07 E-value: 1.09e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 739 APVRRILKYNISEWPYILVGAL---CAAINGAVTPIYSLLFSQILKTFSLVDKeqQRSEIYSMCLFFVilgcVSLFTQFL 815
Cdd:TIGR00958 147 DLLFRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYTGRVIDTLGGDKGPPA--LASAIFFMCLLSI----ASSVSAGL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 816 QGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFL 895
Cdd:TIGR00958 221 RGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 896 FNWKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAI 975
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 976 RKANVYGLCYAFSQGISFLANSAAYRYGGYLI----VYEDLNFSYVFrvvssIAMSATAVGRTFSYT-PSYAKAKISAAR 1050
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVltgkVSSGNLVSFLL-----YQEQLGEAVRVLSYVySGMMQAVGASEK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1051 FFQLLDRKPPIDvySGAGEKWDNFQGKIDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFY 1130
Cdd:TIGR00958 454 VFEYLDRKPNIP--LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1131 DPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTKEIsvERAIAAAKQAQLHDFVMSLPEKYET 1210
Cdd:TIGR00958 532 QPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPD--EEIMAAAKAANAHDFIMEFPNGYDT 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1211 NVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQlaLDKAREGRTCIVIAHRLSTIQNSDIIAVMS 1290
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ--ESRSRASRTVLLIAHRLSTVERADQILVLK 687
|
570 580
....*....|....*....|....
gi 1390249242 1291 QGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
130-657 |
7.35e-115 |
|
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: 371.73 E-value: 7.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 130 GLVDINSEVIKFSGIYAGVGVAVLILGYFqIRLWVIT--GARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDIN 207
Cdd:TIGR02204 48 GFSKDSSGLLNRYFAFLLVVALVLALGTA-ARFYLVTwlGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 208 KIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSS 287
Cdd:TIGR02204 127 LLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 288 IRTVAAFGGENKEVERY----EKNLMFA-QRWGIWKGMVMGFFTgymwcLIFFCYALAFWYGSRLVLdEGEYTPGTLIQI 362
Cdd:TIGR02204 207 IRTVQAFGHEDAERSRFggavEKAYEAArQRIRTRALLTAIVIV-----LVFGAIVGVLWVGAHDVI-AGKMSAGTLGQF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 363 FLCVIIAAMNIGNASSCLEIFSTGCSAASSIFQTIDRQPVMDCMSGDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNNLS 442
Cdd:TIGR02204 281 VFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 443 MVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREE 522
Cdd:TIGR02204 361 LTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 523 ATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALN 602
Cdd:TIGR02204 441 ATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALE 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 603 KIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTLQ 657
Cdd:TIGR02204 521 TLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
62-393 |
3.09e-110 |
|
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: 348.70 E-value: 3.09e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 62 MFMGSVCALLHGMAQPGMIIVFGILTDIFVEYDIERQELSipekvcmnntivwinssfnqnmtngtscglvDINSEVIKF 141
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPD-------------------------------EFLDDVNKY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 142 SGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFL 221
Cdd:cd18577 50 ALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 QRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEV 301
Cdd:cd18577 130 QSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 302 ERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQIFLCVIIAAMNIGNASSCLE 381
Cdd:cd18577 210 KRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRD-GEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
330
....*....|..
gi 1390249242 382 IFSTGCSAASSI 393
Cdd:cd18577 289 AFAKARAAAAKI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
165-654 |
1.06e-109 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 362.12 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 165 ITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLV 244
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 245 ILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLMFAQRWGIWKGMVMGF 324
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 325 FTGYMWCLIFFCYALAFWYGSRLVLdEGEYTPGTLIQiFLcviIAAMNIGNASSCL-EIFS---TGCSAASSIFQTIDRQ 400
Cdd:TIGR00958 387 YLWTTSVLGMLIQVLVLYYGGQLVL-TGKVSSGNLVS-FL---LYQEQLGEAVRVLsYVYSgmmQAVGASEKVFEYLDRK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 401 PvmdCMSGDG-YKLDRIKGEIEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMV 479
Cdd:TIGR00958 462 P---NIPLTGtLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 480 TLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQM 559
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 560 SGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGAlnKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGT 639
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGT 696
|
490
....*....|....*
gi 1390249242 640 HEELLERKGVYFMLV 654
Cdd:TIGR00958 697 HKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
752-1314 |
6.81e-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: 6.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 752 WPYI---LVGALCAAINGAVTPIYSLLFSQILKtfSLVDK---EQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGE 825
Cdd:TIGR02204 10 WPFVrpyRGRVLAALVALLITAAATLSLPYAVR--LMIDHgfsKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 826 LLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVIS 905
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 906 VFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCY 985
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 986 AFSQGISFLANSAAYRYGGYLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPIDVYS 1065
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1066 GAGEKWDNFQGKIDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSK 1145
Cdd:TIGR02204 326 HPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1146 KVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDntKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQ 1225
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGR--PDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
....*....
gi 1390249242 1306 QKGAYYKLV 1314
Cdd:TIGR02204 564 KGGLYARLA 572
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
742-1313 |
9.81e-101 |
|
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: 333.22 E-value: 9.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 742 RRILKYNISEWPYILVGALCAAINGAVTPIYSLLFSQIL-KTFSLVDkeqqRSEIYSMCLFFVILGCVSLFTQFLQGYNF 820
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRD----RSVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 821 AKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQG-ATGSQVGMMVNSFTNIFvavLIAFLF--N 897
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASaATDAFIVLVRETLTVIG---LFIVLLyyS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 898 WKLSLVISVFFPFLALSGAVQTKMltgFASQDKEILEKAGQITN---EALSNIRTVAGIGVEGRFIKAFEVELEKSYKTA 974
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKR---LRRISKEIQNSMGQVTTvaeETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 975 IRKANVYGLCYAFSQGISFLANSAAY------RYGGYLIVYEDLNFsyvfrVVSSIAM-----SATAVGRTFSytpsyaK 1043
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLfialfqAQAGSLTAGDFTAF-----ITAMIALirplkSLTNVNAPMQ------R 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1044 AKISAARFFQLLDRKPPIDvySGAGEKwDNFQGKIDFIDCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSI 1123
Cdd:TIGR02203 300 GLAAAESLFTLLDSPPEKD--TGTRAI-ERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1124 QLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDnTKEISVERAIAAAKQAQLHDFVMS 1203
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1204 LPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNS 1283
Cdd:TIGR02203 455 LPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKA 534
|
570 580 590
....*....|....*....|....*....|
gi 1390249242 1284 DIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:TIGR02203 535 DRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
148-660 |
1.72e-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: 332.45 E-value: 1.72e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 148 VGVAVL--ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLS 225
Cdd:TIGR02203 61 IGLAVLrgICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYE 305
Cdd:TIGR02203 141 TVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 306 knlmFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDE---GEYTPGTLIQIFLCVIIAAMNIGNASSCLEI 382
Cdd:TIGR02203 221 ----AVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQaqaGSLTAGDFTAFITAMIALIRPLKSLTNVNAP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 383 FSTGCSAASSIFQTIDRQPVMDcmsgDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGK 461
Cdd:TIGR02203 297 MQRGLAAAESLFTLLDSPPEKD----TGTRaIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGK 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 462 STALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGR-EEATMEDIVQAAKDANAYNF 540
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 541 IMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTV 620
Cdd:TIGR02203 452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTI 531
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1390249242 621 RSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTLQSQE 660
Cdd:TIGR02203 532 EKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1078-1313 |
9.15e-99 |
|
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: 314.94 E-value: 9.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFDCSIMDNIKYGdnTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1078-1313 |
1.51e-97 |
|
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: 311.47 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFDCSIMDNIKYGDNTkeISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1050-1313 |
3.83e-95 |
|
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: 318.69 E-value: 3.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1050 RFFQLLDRKPPIDVYSGAGE-KWDnfQGKIDFIDCKFTYpsRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLER 1128
Cdd:COG5265 331 RMFDLLDQPPEVADAPDAPPlVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1129 FYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNtkEISVERAIAAAKQAQLHDFVMSLPEKY 1208
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1209 ETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAV 1288
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260
....*....|....*....|....*
gi 1390249242 1289 MSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1076-1308 |
6.51e-94 |
|
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: 301.45 E-value: 6.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1076 GKIDFIDCKFTYpsRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSN 1155
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1156 IGIVSQEPVLFDCSIMDNIKYGDNTkeISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVR 1235
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKG 1308
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
420-653 |
1.16e-91 |
|
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: 295.29 E-value: 1.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEvKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKI 579
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFML 653
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
174-657 |
4.13e-90 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 303.86 E-value: 4.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 174 MRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIdeAIADQMALF-LQRLSTALSGLL-LGFYRGWKLTLVILAVSPL 251
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV--ASSSSGALItVVREGASIIGLFiMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 252 IGIgaaVIGLSVAKFTELELKAYAKAG---SIADEVLSSIRTVAAFGGENKEVERYEK--NLMFAQrwgiwkGMVMGFFT 326
Cdd:PRK11176 178 VSI---AIRVVSKRFRNISKNMQNTMGqvtTSAEQMLKGHKEVLIFGGQEVETKRFDKvsNRMRQQ------GMKMVSAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 327 GYMWCLIFF--CYALAF-WYGSRLVLDEGEYTPGTLIQIFlCVIIAAM----NIGNASScleIFSTGCSAASSIFQTIDR 399
Cdd:PRK11176 249 SISDPIIQLiaSLALAFvLYAASFPSVMDTLTAGTITVVF-SSMIALMrplkSLTNVNA---QFQRGMAACQTLFAILDL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 400 QPVMDcmsgDG-YKLDRIKGEIEFHNVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGM 478
Cdd:PRK11176 325 EQEKD----EGkRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 479 VTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEA-TMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGG 557
Cdd:PRK11176 400 ILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGV 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 558 QMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVER 637
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
490 500
....*....|....*....|
gi 1390249242 638 GTHEELLERKGVYFMLVTLQ 657
Cdd:PRK11176 560 GTHAELLAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
418-661 |
2.34e-89 |
|
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: 302.51 E-value: 2.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHY-PSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD 496
Cdd:COG5265 356 GEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVgegggqmsggqkqRVAIARALIRK 576
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVgerglklsggekqRVAIARTLLKN 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTL 656
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592
|
....*
gi 1390249242 657 QSQED 661
Cdd:COG5265 593 QQEEE 597
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
420-650 |
5.05e-84 |
|
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: 274.11 E-value: 5.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKI 579
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1047-1314 |
1.10e-83 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 286.09 E-value: 1.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1047 SAAR---FFQLLDRKPPIDVYSGAGEKwDNFQGKIDFIDCKFTYPSRPdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSI 1123
Cdd:PRK13657 302 AAPKleeFFEVEDAVPDVRDPPGAIDL-GRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1124 QLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYG--DNTKEisveRAIAAAKQAQLHDFV 1201
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrpDATDE----EMRAAAERAQAHDFI 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1202 MSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQ 1281
Cdd:PRK13657 455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVR 534
|
250 260 270
....*....|....*....|....*....|...
gi 1390249242 1282 NSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:PRK13657 535 NADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
143-648 |
5.78e-83 |
|
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: 283.19 E-value: 5.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDInkidEAIADQMALFL- 221
Cdd:COG4988 62 GLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV----EALDGYFARYLp 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 QRLSTALSGLLLG---FYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGEN 298
Cdd:COG4988 138 QLFLAALVPLLILvavFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 299 KEVERYEKN-----------LMFAQRwgiwKGMVMGFFT--GYMWCLIFFcyalafwyGSRLVldegeYTPGTLIQIFLC 365
Cdd:COG4988 218 AEAERIAEAsedfrkrtmkvLRVAFL----SSAVLEFFAslSIALVAVYI--------GFRLL-----GGSLTLFAALFV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 366 VIIAAmnignassclEIF-------------STGCSAASSIFQTIDrQPVMDCMSGDGYKLDRIKGEIEFHNVTFHYPSR 432
Cdd:COG4988 281 LLLAP----------EFFlplrdlgsfyharANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 433 PEVkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTI 512
Cdd:COG4988 350 RPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 513 AENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNE 592
Cdd:COG4988 428 RENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLgeggrglsggqaqRLALARALLRDAPLLLLDEPTAHLDAE 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 593 SEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKG 648
Cdd:COG4988 508 TEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
418-648 |
4.69e-82 |
|
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: 268.32 E-value: 4.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYpsRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ 497
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKP 577
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKG 648
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
827-1313 |
7.09e-80 |
|
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: 274.72 E-value: 7.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 827 LTKRLRKFGFKAMLRQDIGWFDDLKNnpGVLTTRLATDASQVQG--------ATgsqVGMMVnsftnIFVAVLIAFLFNW 898
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRS--GDLLNRLVADVDALDNlylrvllpLL---VALLV-----ILAAVAFLAFFSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 899 KLSLVIsvfFPFLALSGAVqtkMLTGFASQDKEILEKAGQITN-------EALSNIRTVAGIGVEGRFIKAFEvELEKSY 971
Cdd:COG4987 156 ALALVL---ALGLLLAGLL---LPLLAARLGRRAGRRLAAARAalrarltDLLQGAAELAAYGALDRALARLD-AAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 972 KTAIRKANVYGlcyAFSQGISFLANS----AAYRYGGYLIVYEDLNFSY----------VFRVVSSIAMSATAVGRTFSy 1037
Cdd:COG4987 229 AAAQRRLARLS---ALAQALLQLAAGlavvAVLWLAAPLVAAGALSGPLlallvlaalaLFEALAPLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1038 tpsyakakiSAARFFQLLDRKPPidVYSGAGEKWDNFQGKIDFIDCKFTYPSRPDiQVLNGLSVSVDPGQTLAFVGSSGC 1117
Cdd:COG4987 305 ---------AARRLNELLDAPPA--VTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1118 GKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNtkEISVERAIAAAKQAQL 1197
Cdd:COG4987 373 GKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1198 HDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRL 1277
Cdd:COG4987 451 GDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
490 500 510
....*....|....*....|....*....|....*.
gi 1390249242 1278 STIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
752-1313 |
2.53e-78 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 270.74 E-value: 2.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 752 WPYI------LVGALCAAINGAVTPIYSLlfsQILKtfSLVD---KEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFA- 821
Cdd:PRK11176 17 WPTIapfkagLIVAGVALILNAASDTFML---SLLK--PLLDdgfGKADRSVLKWMPLVVIGLMILRGITSFISSYCISw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 822 KSGELLTkRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLS 901
Cdd:PRK11176 92 VSGKVVM-TMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 902 LVISVFFPFLA------------LSGAVQTKM--LTGFASQ----DKEILEKAGQITNEAlsnirtvagigvegRFIKAF 963
Cdd:PRK11176 169 LILIVIAPIVSiairvvskrfrnISKNMQNTMgqVTTSAEQmlkgHKEVLIFGGQEVETK--------------RFDKVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 964 EVELEKSYKTAIRKANVYGLCyafsQGISFLANSAAYRYGGYLIVYEDLN---FSYVFRvvSSIAM-----SATAVGRTF 1035
Cdd:PRK11176 235 NRMRQQGMKMVSASSISDPII----QLIASLALAFVLYAASFPSVMDTLTagtITVVFS--SMIALmrplkSLTNVNAQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1036 SytpsyaKAKISAARFFQLLDRKPPIDvySGAGEKwDNFQGKIDFIDCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSS 1115
Cdd:PRK11176 309 Q------RGMAACQTLFAILDLEQEKD--EGKRVI-ERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1116 GCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGdNTKEISVERAIAAAKQA 1195
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA-RTEQYSREQIEEAARMA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1196 QLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAH 1275
Cdd:PRK11176 458 YAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
570 580 590
....*....|....*....|....*....|....*...
gi 1390249242 1276 RLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:PRK11176 538 RLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1042-1308 |
2.79e-78 |
|
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: 269.71 E-value: 2.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1042 AKAKISAARFFQLLDRKPPIDVYSGAGEKWDNfQGKIDFIDCKFTYPSRPdiQVLNGLSVSVDPGQTLAFVGSSGCGKST 1121
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1122 SIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDntKEISVERAIAAAKQAQLHDFV 1201
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1202 MSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQ 1281
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 1390249242 1282 NSDIIAVMSQGVVIEKGTHKKLMDQKG 1308
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
757-1321 |
4.80e-78 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 284.23 E-value: 4.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 757 VGALCAAINGAVTPIYSLLFSQILKTFSLVDkeqqrsEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGF 836
Cdd:PTZ00265 64 VSFVCATISGGTLPFFVSVFGVIMKNMNLGE------NVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 837 KAMLRQDiGWFDDlkNNPGV-LTTRLATDASQVQGATGSQVgMMVNSFTNIFVAVLIAFLF-NWKLSLVISVFFPFLALS 914
Cdd:PTZ00265 138 KSVFYQD-GQFHD--NNPGSkLTSDLDFYLEQVNAGIGTKF-ITIFTYASAFLGLYIWSLFkNARLTLCITCVFPLIYIC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 915 GAVQTKMLTgfASQDKEIL--EKAGQITNEALSNIRTVAGIGVEGRFIKAFEVElEKSYKTAIRKAN-VYGLCYAFSQGI 991
Cdd:PTZ00265 214 GVICNKKVK--INKKTSLLynNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLS-EKLYSKYILKANfMESLHIGMINGF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 992 SFLANSAAYRYGGYLIVYE--------DLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPIDv 1063
Cdd:PTZ00265 291 ILASYAFGFWYGTRIIISDlsnqqpnnDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1064 YSGAGEKWDNFQgKIDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMI-DGH 1142
Cdd:PTZ00265 370 NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSH 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1143 DSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYG--------------------------------------------- 1177
Cdd:PTZ00265 449 NLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnt 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1178 -DNTKEISVER---------AIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:PTZ00265 529 tDSNELIEMRKnyqtikdseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1248 ALDTESEKTVQLALD--KAREGRTCIVIAHRLSTIQNSDIIAVMSQ---------------------------------- 1291
Cdd:PTZ00265 609 SLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNrergstvdvdiigedptkdnkennnknnkddnnn 688
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1390249242 1292 -------------GVVIEKGTHKKLMDQKGAYYKLVITGAPIS 1321
Cdd:PTZ00265 689 nnnnnnnkinnagSYIIEQGTHDALMKNKNGIYYTMINNQKVS 731
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
62-393 |
5.23e-78 |
|
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: 260.29 E-value: 5.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 62 MFMGSVCALLHGMAQPGMIIVFGILTDIFVeydierqelsipekvcmNNTIVWINSSfnqNMTNGTSCGLVD-INSEVIK 140
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-----------------NGGMTNITGN---SSGLNSSAGPFEkLEEEMTL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 141 FSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALF 220
Cdd:cd18558 61 YAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 221 LQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKE 300
Cdd:cd18558 141 FQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 301 VERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDEgEYTPGTLIQIFLCVIIAAMNIGNASSCL 380
Cdd:cd18558 221 ETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQ-EYSIGEVLTVFFSVLIGAFSAGQQVPSI 299
|
330
....*....|...
gi 1390249242 381 EIFSTGCSAASSI 393
Cdd:cd18558 300 EAFANARGAAYHI 312
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
413-673 |
1.83e-77 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 268.37 E-value: 1.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 413 LDRIKGEIEFHNVTFHYP-SRPEVKilnNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNI 491
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 492 RWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIAR 571
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYF 651
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
250 260
....*....|....*....|....
gi 1390249242 652 MLVTLQS--QEDNTHKETGIKGKD 673
Cdd:PRK13657 565 ALLRAQGmlQEDERRKQPAAEGAN 588
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1072-1294 |
3.92e-77 |
|
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: 254.32 E-value: 3.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1072 DNFQGKIDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQF 1151
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQEPVLFDCSIMDNIKYGDNTKeiSVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIAR 1231
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSC--SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1232 AIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVV 1294
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1078-1314 |
9.22e-77 |
|
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: 253.95 E-value: 9.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYpsRPD-IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNI 1156
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1157 GIVSQEPVLFDCSIMDNIKYGDNTkeISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1237 PKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
420-657 |
1.31e-76 |
|
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: 253.18 E-value: 1.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHY-PSRPEvkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQI 498
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPK 578
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 579 ILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVTLQ 657
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
755-1050 |
1.18e-74 |
|
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: 250.08 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQILKTFS-----LVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTK 829
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 830 RLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFP 909
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 910 FLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQ 989
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 990 GISFLANSAAYRYGGYLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAAR 1050
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAK 299
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
872-1313 |
7.86e-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: 260.83 E-value: 7.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 872 TGSQVGMMVNS-FTNIFVAVLiaFLFNWKLSLVISVFFPFLAL-----SGAVQTKMLTGFASQdkeilEKAGQITNEALS 945
Cdd:TIGR01846 253 TGSALTVVLDLlFVVVFLAVM--FFYSPTLTGVVIGSLVCYALlsvfvGPILRKRVEDKFERS-----AAATSFLVESVT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 946 NIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCyafSQGISF---LANSAAYRYGGYLIVYEDLNfsyVFRVVS 1022
Cdd:TIGR01846 326 GIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIA---GQAIELiqkLTFAILLWFGAHLVIGGALS---PGQLVA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1023 sIAMSATAVG----RTFSYTPSYAKAKISAARFFQLLDRkpPIDVYSGAGEKWDNFQGKIDFIDCKFTYpsRPDI-QVLN 1097
Cdd:TIGR01846 400 -FNMLAGRVTqpvlRLAQLWQDFQQTGIALERLGDILNS--PTEPRSAGLAALPELRGAITFENIRFRY--APDSpEVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1098 GLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYG 1177
Cdd:TIGR01846 475 NLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1178 DntKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV 1257
Cdd:TIGR01846 555 N--PGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALI 632
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1258 QLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:TIGR01846 633 MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
53-401 |
1.91e-72 |
|
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: 244.67 E-value: 1.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 53 FSSSKDNW-LMFMGSVCALLHGMAQPGMIIVFGILTDIFveydierqelsipekvcmnntivwinssfnqnmtngTSCGL 131
Cdd:cd18578 1 LKLNKPEWpLLLLGLIGAIIAGAVFPVFAILFSKLISVF------------------------------------SLPDD 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 132 VDINSEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFD--CTSVGELNSRFSDDINKI 209
Cdd:cd18578 45 DELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 210 DEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIR 289
Cdd:cd18578 125 RGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 290 TVAAFGGENKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQIFLCVIIA 369
Cdd:cd18578 205 TVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVAN-GEYTFEQFFIVFMALIFG 283
|
330 340 350
....*....|....*....|....*....|..
gi 1390249242 370 AMNIGNASSCLEIFSTGCSAASSIFQTIDRQP 401
Cdd:cd18578 284 AQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
169-656 |
4.98e-72 |
|
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: 251.99 E-value: 4.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 169 RQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEaiadqmaLFLqR---------LSTALSGLLLGFYrGW 239
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDN-------LYL-RvllpllvalLVILAAVAFLAFF-SP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 240 KLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAY-AKAGSIADEVLSSIRTVAAFGGENKEVERY---EKNLMFAQR-- 313
Cdd:COG4987 156 ALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLdaaEARLAAAQRrl 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 314 --WGIWKGMVMGFFTGymwclifFCYALAFWYGSRLVLDEGeyTPGTLIQIFLCVIIAA----MNIGNAssCLEIFSTGc 387
Cdd:COG4987 236 arLSALAQALLQLAAG-------LAVVAVLWLAAPLVAAGA--LSGPLLALLVLAALALfealAPLPAA--AQHLGRVR- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 388 SAASSIFQTIDRQP-VMDcmSGDGYKLDRiKGEIEFHNVTFHYPSRPEvKILNNLSMVIKPGETTAFVGSSGAGKSTALQ 466
Cdd:COG4987 304 AAARRLNELLDAPPaVTE--PAEPAPAPG-GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 467 LIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQ 546
Cdd:COG4987 380 LLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPD 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 547 QFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVI 626
Cdd:COG4987 460 GLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRI 539
|
490 500 510
....*....|....*....|....*....|
gi 1390249242 627 IGFEHGTAVERGTHEELLERKGVYFMLVTL 656
Cdd:COG4987 540 LVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1078-1292 |
2.95e-69 |
|
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: 229.58 E-value: 2.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFDCSIMDNIkygdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqgsqLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQG 1292
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
420-632 |
3.52e-68 |
|
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: 226.50 E-value: 3.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEvKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREeatmedivqaakdanaynfimalpQQfdtlvgegggqmsggqkqRVAIARALIRKPKI 579
Cdd:cd03228 80 YVPQDPFLFSGTIRENILSGGQ------------------------RQ------------------RIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHG 632
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
755-1048 |
5.53e-68 |
|
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: 231.78 E-value: 5.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQILKTF-------------SLVDK----EQQRSEIYSMCLFFVILGCVSLFTQFLQG 817
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssGLNSSagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 818 YNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFN 897
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 898 WKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRK 977
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 978 ANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISA 1048
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAA 309
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
414-632 |
4.90e-67 |
|
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: 225.81 E-value: 4.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 414 DRIKGEIEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRW 493
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARAL 573
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHG 632
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
159-654 |
1.15e-66 |
|
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: 240.23 E-value: 1.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 159 QIRLWVITGARqirkmrkfYFRRIMRMEIGWFDCTSVGELNSRFSDDiNKIDEAIADQMAlflqrlSTALSGLLLGFYrg 238
Cdd:TIGR03796 222 EIKLAVGMSAR--------FLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLA------TTALDAVMLVFY-- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 239 wklTLVILAVSP---LIGIGAAVIGLSVAKF-----TELELKA---YAKAGSIADEVLSSIRTVAAFGGENKEVER---- 303
Cdd:TIGR03796 285 ---ALLMLLYDPvltLIGIAFAAINVLALQLvsrrrVDANRRLqqdAGKLTGVAISGLQSIETLKASGLESDFFSRwagy 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 304 YEKNLMFAQRWGI---WKGMVMGFFTGymwclifFCYALAFWYGSRLVLDeGEYTPGTLIqiflcviiAAMNIgnASSCL 380
Cdd:TIGR03796 362 QAKLLNAQQELGVltqILGVLPTLLTS-------LNSALILVVGGLRVME-GQLTIGMLV--------AFQSL--MSSFL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 381 EIFSTGCSAASSIfQTI----DR-QPVMDC-----------MSGDGYKLDRIKGEIEFHNVTFHYpSRPEVKILNNLSMV 444
Cdd:TIGR03796 424 EPVNNLVGFGGTL-QELegdlNRlDDVLRNpvdplleepegSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLT 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 445 IKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEAT 524
Cdd:TIGR03796 502 LQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIP 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 525 MEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNki 604
Cdd:TIGR03796 582 DADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR-- 659
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 605 QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLV 654
Cdd:TIGR03796 660 RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
753-1314 |
8.80e-66 |
|
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: 237.53 E-value: 8.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 753 PYILVGALCAAINGAVTPIysllFSQILKTFSLVDKEQQ--RSEIYSMCLFFVILGcvslFTQFLQGYNFAKsgeLLTKR 830
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPA----FSQIFVDEILVQGRQDwlRPLLLGMGLTALLQG----VLTWLQLYYLRR---LEIKL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 831 LRKFG---FKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIaFLFNWKLSLVISVF 907
Cdd:TIGR03796 226 AVGMSarfLWHILRLPVRFFA--QRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLM-LLYDPVLTLIGIAF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 908 FPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVE--------GRFIKAFEVELEKSYKTAIRKAn 979
Cdd:TIGR03796 303 AAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLEsdffsrwaGYQAKLLNAQQELGVLTQILGV- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 980 vyglcyaFSQGISFLANSAAYRYGGYLIVYEDLnfsyvfrvvsSIAMSATAVGRTFSYTPSYAKAKISAARFFQL---LD 1056
Cdd:TIGR03796 382 -------LPTLLTSLNSALILVVGGLRVMEGQL----------TIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELegdLN 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1057 R-----KPPIDVY-------SGAGEKWDNFQGKIDFIDCKFTYpSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQ 1124
Cdd:TIGR03796 445 RlddvlRNPVDPLleepegsAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1125 LLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTkeISVERAIAAAKQAQLHDFVMSL 1204
Cdd:TIGR03796 524 LVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSR 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1205 PEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALdkAREGRTCIVIAHRLSTIQNSD 1284
Cdd:TIGR03796 602 PGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCD 679
|
570 580 590
....*....|....*....|....*....|
gi 1390249242 1285 IIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:TIGR03796 680 EIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
882-1317 |
5.19e-64 |
|
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: 229.01 E-value: 5.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 882 SFTNIFVAVLIAFLFNWKLSLVISVF-FPFLALSGAVQTKMLTGFASQDKEILEKAGQITnEALSNIRTVAG---IGVEG 957
Cdd:TIGR01192 140 TFVALFLLIPTAFAMDWRLSIVLMVLgILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVS-DSISNVSVVHSynrIEAET 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 958 RFIKAFEVELEKSYKTAIrkaNVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLNfsyVFRVVSSIAMSATAVGR---- 1033
Cdd:TIGR01192 219 SALKQFTNNLLSAQYPVL---DWWALASGLNRMASTISMMCILVIGTVLVIKGELS---VGEVIAFIGFANLLIGRldqm 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1034 -TFSYTPSYAKAKISaaRFFQLLD----RKPPIDvysgAGEkWDNFQGKIDFIDCKFTYPSRPdiQVLNGLSVSVDPGQT 1108
Cdd:TIGR01192 293 sGFITQIFEARAKLE--DFFDLEDsvfqREEPAD----APE-LPNVKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1109 LAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTKeiSVERA 1188
Cdd:TIGR01192 364 VAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGA--TDEEV 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1189 IAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGR 1268
Cdd:TIGR01192 442 YEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNR 521
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1390249242 1269 TCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLVITG 1317
Cdd:TIGR01192 522 TTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
62-360 |
9.44e-62 |
|
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: 212.50 E-value: 9.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 62 MFMGSVCALLHGMAQPGMIIVFGILTDIFVEYdierqelsipekvcmnntivWINSSFNQNMtngtscglvdinsevikF 141
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPD--------------------GDPETQALNV-----------------Y 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 142 SGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFL 221
Cdd:pfam00664 44 SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 QRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEV 301
Cdd:pfam00664 124 QSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYEL 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 302 ERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:pfam00664 204 EKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVIS-GELSVGDLV 261
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
181-657 |
7.15e-61 |
|
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: 222.52 E-value: 7.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 181 RIMRMEIGWFDCTSVGELNSRfSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIG 260
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASR-AMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 261 LsvaKFTELELKAYAKAGSIADEVLSSIRTVAAF---GGENKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCY 337
Cdd:TIGR03797 297 L---LQVRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 338 ALAFWYGSRLvLDEGEYTPGTLIqiflcviiaAMNignasSCLEIFSTG----CSAASSIFQTI---DR-QPVMDCM-SG 408
Cdd:TIGR03797 374 AALFAAAISL-LGGAGLSLGSFL---------AFN-----TAFGSFSGAvtqlSNTLISILAVIplwERaKPILEALpEV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 409 DGYKLD--RIKGEIEFHNVTFHY-PSRPevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHD 485
Cdd:TIGR03797 439 DEAKTDpgKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 486 IRSLNIRWLRDQIGIVEQEPVLFSTTIAENIrLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQ 565
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 566 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQhgHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLE 645
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|..
gi 1390249242 646 RKGVYFMLVTLQ 657
Cdd:TIGR03797 674 REGLFAQLARRQ 685
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
143-650 |
5.27e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 214.19 E-value: 5.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQiRLWVITGARQIR-KMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEA-------IA 214
Cdd:PRK10789 40 GTMVLIAVVVYLLRYVW-RVLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAagegvltLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 215 DQMAL---FLQRLSTALSglllgfyrgWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTV 291
Cdd:PRK10789 119 DSLVMgcaVLIVMSTQIS---------WQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 292 AAFGGENKEVERYE--------KNLMFAQrwgiwkgmVMGFFTGYMWCLIFFCYALAFWYGSRLVLdEGEYTPGTL---- 359
Cdd:PRK10789 190 KAFGLEDRQSALFAadaedtgkKNMRVAR--------IDARFDPTIYIAIGMANLLAIGGGSWMVV-NGSLTLGQLtsfv 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 360 ----IQIFLCVIIAAMnignasscLEIFSTGCSAASSIFQTIDRQPVMDcmsgDGYK-LDRIKGEIEFHNVTFHYPSRpE 434
Cdd:PRK10789 261 mylgLMIWPMLALAWM--------FNIVERGSAAYSRIRAMLAEAPVVK----DGSEpVPEGRGELDVNIRQFTYPQT-D 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 435 VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAE 514
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVAN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 515 NIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESE 594
Cdd:PRK10789 408 NIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 595 AKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:PRK10789 488 HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1076-1299 |
7.44e-59 |
|
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: 201.95 E-value: 7.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1076 GKIDFIDCKFTYpsRPDIQ-VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRS 1154
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQEPVLFDCSIMDNIkygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIV 1234
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1235 RDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
193-1313 |
6.71e-58 |
|
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: 220.20 E-value: 6.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 193 TSVGELNSRFSDDINKIDEaiadqMALFLQRLSTALSGLLLGFYRGWkltlVILAVSPLIGIGAAVIGLSVAKFTELELK 272
Cdd:TIGR00957 412 STVGEIVNLMSVDAQRFMD-----LATYINMIWSAPLQVILALYFLW----LNLGPSVLAGVAVMVLMVPLNAVMAMKTK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 273 AYAKAG--------SIADEVLSSIRTVAAFGGE---NKEVERYEKNLMFAQRwgiwKGMVMGFFTGYMW-CLIFFCYALA 340
Cdd:TIGR00957 483 TYQVAHmkskdnriKLMNEILNGIKVLKLYAWElafLDKVEGIRQEELKVLK----KSAYLHAVGTFTWvCTPFLVALIT 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 341 FWY----GSRLVLD-EGEYTPGTLIQIF------LCVIIAamNIGNASSCLEIFSTGCSAASSIFQTIDRQPVMDcmsGD 409
Cdd:TIGR00957 559 FAVyvtvDENNILDaEKAFVSLALFNILrfplniLPMVIS--SIVQASVSLKRLRIFLSHEELEPDSIERRTIKP---GE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 410 GYKldrikgeIEFHNVTFHYpSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGhdirsl 489
Cdd:TIGR00957 634 GNS-------ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------ 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 490 nirwlrdQIGIVEQEPVLFSTTIAENIRLGReeATMEDIVQAAKDANAY-NFIMALPQQFDTLVGEGGGQMSGGQKQRVA 568
Cdd:TIGR00957 700 -------SVAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVS 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEA----KVQGALNKIQhGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:TIGR00957 771 LARAVYSNADIYLFDDPLSAVDAHVGKhifeHVIGPEGVLK-NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 645 ERKGVYF-MLVTLQSQEDNTHKETGIKGKDTTEGDTPERTFSRGSYQDSLRASIrQRSKSQLSHLSHEpplaIGDHKSSY 723
Cdd:TIGR00957 850 QRDGAFAeFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQL-QRQLSASSSDSGD----QSRHHGSS 924
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 724 E-----DRKDNDVLVEEVEPAPVRRIlKYNISeWPYILVGALCAA-------INGAVTPIYSLLFSQILKTFSLVDKEQQ 791
Cdd:TIGR00957 925 AelqkaEAKEETWKLMEADKAQTGQV-ELSVY-WDYMKAIGLFITflsiflfVCNHVSALASNYWLSLWTDDPMVNGTQN 1002
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 792 ----RSEIYSMclffviLGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQ 867
Cdd:TIGR00957 1003 ntslRLSVYGA------LGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDT 1074
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 868 VQGATGSQVGMMVNSFTNIFVAVLIAFLfnwkLSLVISVFFPFLALSGAVQTKMLTGFASQDKEiLEKAGQIT-----NE 942
Cdd:TIGR00957 1075 VDSMIPPVIKMFMGSLFNVIGALIVILL----ATPIAAVIIPPLGLLYFFVQRFYVASSRQLKR-LESVSRSPvyshfNE 1149
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 943 ALSNIRTVAGIGVEGRFIKAFEVELEKSYKTairkanvyglCYAfsqgiSFLAN---SAAYRYGGYLIVYedlnFSYVFR 1019
Cdd:TIGR00957 1150 TLLGVSVIRAFEEQERFIHQSDLKVDENQKA----------YYP-----SIVANrwlAVRLECVGNCIVL----FAALFA 1210
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1020 VVSSIAMSATAVGRTFSYT---------------------------PSYAKAKISAArfFQLLDRKPPidvysgagEKWD 1072
Cdd:TIGR00957 1211 VISRHSLSAGLVGLSVSYSlqvtfylnwlvrmssemetnivaverlKEYSETEKEAP--WQIQETAPP--------SGWP 1280
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1073 NfQGKIDFIDCKFTYpsRPDIQ-VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQF 1151
Cdd:TIGR00957 1281 P-RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD 1357
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQEPVLFDCSIMDNIkygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIAR 1231
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLAR 1434
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1232 AIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYY 1311
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
..
gi 1390249242 1312 KL 1313
Cdd:TIGR00957 1515 SM 1516
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1076-1298 |
1.73e-57 |
|
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: 198.20 E-value: 1.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1076 GKIDFIDCKFTYPSRPdIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSN 1155
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1156 IGIVSQEPVLFDCSIMDNIKYGDntKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVR 1235
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1043-1313 |
1.79e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 209.96 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1043 KAKISAARFFQLLDRkpPIDVYSGAGEKWDnfQGKIDFIDCKFTYpsRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTS 1122
Cdd:PRK10790 310 QAVVAGERVFELMDG--PRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1123 IQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGdntKEISVERAIAAAKQAQLHDFVM 1202
Cdd:PRK10790 384 ASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELAR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1203 SLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN 1282
Cdd:PRK10790 461 SLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
|
250 260 270
....*....|....*....|....*....|.
gi 1390249242 1283 SDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:PRK10790 541 ADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
135-627 |
7.59e-57 |
|
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: 206.75 E-value: 7.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 135 NSEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDInkidEAIA 214
Cdd:TIGR02857 40 LAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGV----EALD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 215 DQMALFL-QRLSTALSGLLLG---FYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRT 290
Cdd:TIGR02857 116 GYFARYLpQLVLAVIVPLAILaavFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 291 VAAFGGENKEV-------ERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIffcyalAFWYGSRLVldegeYTPGTLIQIF 363
Cdd:TIGR02857 196 LKLFGRAKAQAaairrssEEYRERTMRVLRIAFLSSAVLELFATLSVALV------AVYIGFRLL-----AGDLDLATGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 364 LCVIIAA---MNIGNASSCLEIFSTGCSAASSIFQTIDRQPVMdcMSGDGYKLDRIKGEIEFHNVTFHYPSRPEVkiLNN 440
Cdd:TIGR02857 265 FVLLLAPefyLPLRQLGAQYHARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 441 LSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGR 520
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 521 EEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGA 600
Cdd:TIGR02857 421 PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA 500
|
490 500
....*....|....*....|....*..
gi 1390249242 601 LNKIQHGHTIISVAHRLSTVRSADVII 627
Cdd:TIGR02857 501 LRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
165-656 |
1.50e-56 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 216.05 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 165 ITGARQIRKMRKFYFRRIMRMEIGWFD--CTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRgWKLT 242
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYF-CPIV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 243 LVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSI----------------ADEVLSSIRTVAAFGGENKEVERYEK 306
Cdd:PTZ00265 971 AAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 307 NLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVldegeyTPGT-LIQIFLCVIIAAMNIGNASSCLEIFST 385
Cdd:PTZ00265 1051 AIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLI------RRGTiLVDDFMKSLFTFLFTGSYAGKLMSLKG 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 386 GCSAASSIFQT----IDRQPVMDCMSGDGYKL---DRIKGEIEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSG 458
Cdd:PTZ00265 1125 DSENAKLSFEKyyplIIRKSNIDVRDNGGIRIknkNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETG 1204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 459 AGKSTALQLIQRFYD------------------------------------------------------PCEGMVTLDGH 484
Cdd:PTZ00265 1205 SGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGV 1284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 485 DIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQK 564
Cdd:PTZ00265 1285 DICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQK 1364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 565 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRSADVIIGFEH----GTAVE-R 637
Cdd:PTZ00265 1365 QRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaH 1444
|
570 580
....*....|....*....|
gi 1390249242 638 GTHEELLE-RKGVYFMLVTL 656
Cdd:PTZ00265 1445 GTHEELLSvQDGVYKKYVKL 1464
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1047-1313 |
2.99e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 203.13 E-value: 2.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1047 SAARFFQLLDRKPpiDVYSGAGEKWDNFQGKIDFIDCKFTYPSRPDiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL 1126
Cdd:PRK11160 310 SARRINEITEQKP--EVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1127 ERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTkeISVERAIAAAKQAQLHDFVMSlPE 1206
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1207 KYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDII 1286
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260
....*....|....*....|....*..
gi 1390249242 1287 AVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
418-639 |
1.80e-53 |
|
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: 186.55 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYpsRPEVK-ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD 496
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFSTTIAENIRLgREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRK 576
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDP-FGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGT 639
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1042-1289 |
2.00e-52 |
|
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: 193.66 E-value: 2.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1042 AKAKISAARFFQLLDRKPPIdVYSGAGEKWDNFQGkIDFIDCKFTYPSRPdiQVLNGLSVSVDPGQTLAFVGSSGCGKST 1121
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRP-LAGKAPVTAAPASS-LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1122 SIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGDntKEISVERAIAAAKQAQLHDFV 1201
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1202 MSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQ 1281
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*...
gi 1390249242 1282 NSDIIAVM 1289
Cdd:TIGR02857 522 LADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
755-1015 |
2.35e-52 |
|
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: 185.54 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQILKTFsLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKF 834
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 835 GFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALS 914
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 915 GAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFL 994
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260
....*....|....*....|.
gi 1390249242 995 ANSAAYRYGGYLIVYEDLNFS 1015
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVG 258
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
883-1294 |
6.80e-52 |
|
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: 192.66 E-value: 6.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 883 FTNIFVAVLiaFLFNWKLSLvisvffpfLALSGAVqtkMLTGFA-SQD---KEILEKAGQITNEA-------LSNIRTVA 951
Cdd:COG4618 142 WAPIFLAVL--FLFHPLLGL--------LALVGAL---VLVALAlLNErltRKPLKEANEAAIRAnafaeaaLRNAEVIE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 952 GIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLNFSYVFrvVSSIAMS---- 1027
Cdd:COG4618 209 AMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMI--AASILMGrala 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1028 ----ATAVGRTFSytpsyaKAKISAARFFQLLDRKPPIDvysgAGEKWDNFQGKIDFIDCKFTYP--SRPdiqVLNGLSV 1101
Cdd:COG4618 287 pieqAIGGWKQFV------SARQAYRRLNELLAAVPAEP----ERMPLPRPKGRLSVENLTVVPPgsKRP---ILRGVSF 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1102 SVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNI-KYGDnt 1180
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGD-- 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1181 keISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLA 1260
Cdd:COG4618 432 --ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509
|
410 420 430
....*....|....*....|....*....|....*
gi 1390249242 1261 LDKARE-GRTCIVIAHRLSTIQNSDIIAVMSQGVV 1294
Cdd:COG4618 510 IRALKArGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
418-638 |
1.98e-51 |
|
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: 180.48 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ 497
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKP 577
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERG 638
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
154-655 |
8.63e-50 |
|
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: 189.57 E-value: 8.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 154 ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDdINKIDEAIADQM-ALFLQRLSTALSGLL 232
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 233 LGfYRGWKLTLVILAVSPLIgigAAVIGLSVAKFTELELKAyAKAGSIAD----EVLSSIRTVAAFGGE----NKEVERY 304
Cdd:TIGR01193 290 LV-RQNMLLFLLSLLSIPVY---AVIIILFKRTFNKLNHDA-MQANAVLNssiiEDLNGIETIKSLTSEaerySKIDSEF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 305 EKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFcyalAFWYGSRLVLdEGEYTPGTLIQIFLCV---IIAAMNIGNASSCLE 381
Cdd:TIGR01193 365 GDYLNKSFKYQKADQGQQAIKAVTKLILNVV----ILWTGAYLVM-RGKLTLGQLITFNALLsyfLTPLENIINLQPKLQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 382 ifstgcsAASSIFQTIDRQPVMDCMSGDGYKLD---RIKGEIEFHNVTFHYPSRPEvkILNNLSMVIKPGETTAFVGSSG 458
Cdd:TIGR01193 440 -------AARVANNRLNEVYLVDSEFINKKKRTelnNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSG 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 459 AGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLG-REEATMEDIVQAAKDANA 537
Cdd:TIGR01193 511 SGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 538 YNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHgHTIISVAHRL 617
Cdd:TIGR01193 591 KDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRL 669
|
490 500 510
....*....|....*....|....*....|....*...
gi 1390249242 618 STVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLVT 655
Cdd:TIGR01193 670 SVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
827-1310 |
5.38e-49 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 184.53 E-value: 5.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 827 LTKRLRKFGFKAMLRQDIGWFddLKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTnIFVAVLIAF--LFNWKLSLVI 904
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLV-MGCAVLIVMstQISWQLTLLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 905 SVFFPFLALsgavqtkMLTGFASQDKEILEKA-------GQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRK 977
Cdd:PRK10789 144 LLPMPVMAI-------MIKRYGDQLHERFKLAqaafsslNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 978 ANVYGLcyaFSQGISF---LANSAAYRYGGYLIVYEDLNF----SYVFRVVSSI-AMSATA-----VGRTfsytpsyaka 1044
Cdd:PRK10789 217 ARIDAR---FDPTIYIaigMANLLAIGGGSWMVVNGSLTLgqltSFVMYLGLMIwPMLALAwmfniVERG---------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1045 kiSAA--RFFQLLDRKPPID-----VYSGAGEkwdnFQGKIDfidcKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSSGC 1117
Cdd:PRK10789 284 --SAAysRIRAMLAEAPVVKdgsepVPEGRGE----LDVNIR----QFTYPQT-DHPALENVNFTLKPGQMLGICGPTGS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1118 GKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYG--DNTKEiSVERAiaaAKQA 1195
Cdd:PRK10789 353 GKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGrpDATQQ-EIEHV---ARLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1196 QLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAH 1275
Cdd:PRK10789 429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
490 500 510
....*....|....*....|....*....|....*
gi 1390249242 1276 RLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAY 1310
Cdd:PRK10789 509 RLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
754-1299 |
1.73e-47 |
|
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: 179.47 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 754 YILVGALCAAIN--GAVTPIYSL-LFSQILKTFSLVdkeqqrseiysmCLFFVILGCVSLFT-----QFLQGYNFAKSGE 825
Cdd:TIGR01842 8 FIIVGLFSFVINilMLAPPLYMLqVYDRVLTSGSVP------------TLLMLTVLALGLYLflgllDALRSFVLVRIGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 826 LLTKRLRKFGFKAMLRQDIgwfddlkNNPGVLTTRLATDASQVQGATGSQVgmmVNSF-----TNIFVAVLiaFLFNwkl 900
Cdd:TIGR01842 76 KLDGALNQPIFAASFSATL-------RRGSGDGLQALRDLDQLRQFLTGPG---LFAFfdapwMPIYLLVC--FLLH--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 901 slvisVFFPFLALSGAV---QTKMLTGFASQDK-----EILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYK 972
Cdd:TIGR01842 141 -----PWIGILALGGAVvlvGLALLNNRATKKPlkeatEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 973 TAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLNfsyvfrvVSSIAMSATAVGRTFSytP---------SYAK 1043
Cdd:TIGR01842 216 AQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEIT-------PGMMIAGSILVGRALA--PidgaiggwkQFSG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1044 AKISAARFFQLLDRKPPIDvysgAGEKWDNFQGKIDfIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSI 1123
Cdd:TIGR01842 287 ARQAYKRLNELLANYPSRD----PAMPLPEPEGHLS-VENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1124 QLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNI-KYGDNTKEisvERAIAAAKQAQLHDFVM 1202
Cdd:TIGR01842 362 RLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGENADP---EKIIEAAKLAGVHELIL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1203 SLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAR-EGRTCIVIAHRLSTIQ 1281
Cdd:TIGR01842 439 RLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLG 518
|
570
....*....|....*...
gi 1390249242 1282 NSDIIAVMSQGVVIEKGT 1299
Cdd:TIGR01842 519 CVDKILVLQDGRIARFGE 536
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
855-1314 |
1.13e-46 |
|
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: 179.94 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 855 GVLTTRLaTDASQVQGATGSqvgMMVNSFTNIFVAVLIAFLF---NWKLSLVISVFFPFLALsgaVQTKMLTGFASQDKE 931
Cdd:TIGR01193 253 GEIVSRF-TDASSIIDALAS---TILSLFLDMWILVIVGLFLvrqNMLLFLLSLLSIPVYAV---IIILFKRTFNKLNHD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 932 ILEkAGQITN----EALSNIRTVAGIGVEG-RFIK---AFEVELEKSYKTAIRKAnvygLCYAFSQGISFLANSAAYRYG 1003
Cdd:TIGR01193 326 AMQ-ANAVLNssiiEDLNGIETIKSLTSEAeRYSKidsEFGDYLNKSFKYQKADQ----GQQAIKAVTKLILNVVILWTG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1004 GYLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQ--LLDRKppiDVYSGAGEKWDNFQGKIDFI 1081
Cdd:TIGR01193 401 AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSE---FINKKKRTELNNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1082 DCKFTYPSRPDIqvLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQ 1161
Cdd:TIGR01193 478 DVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 EPVLFDCSIMDNIKYGDNTKeISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKEN-VSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1242 LDEATSALDTESEKTVQLALDKAREgRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1091-1313 |
3.72e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 176.19 E-value: 3.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNG-LSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCS 1169
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGDntKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK11174 439 LRDNVLLGN--PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1250 DTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKL 1313
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
133-380 |
5.28e-46 |
|
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: 167.74 E-value: 5.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 133 DINSEVIKFSGIYAGVGVAVLILGYfqirLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEA 212
Cdd:cd18557 34 VLNELALILLAIYLLQSVFTFVRYY----LFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 213 IADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVA 292
Cdd:cd18557 110 VTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 293 AFGGENKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLdEGEYTPGTLIQIFLCVIIAAMN 372
Cdd:cd18557 190 SFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVL-SGQLTVGELTSFILYTIMVASS 268
|
....*...
gi 1390249242 373 IGNASSCL 380
Cdd:cd18557 269 VGGLSSLL 276
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
855-1277 |
1.08e-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: 173.70 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 855 GVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFfpfLALSGAVqTKMLTGFASQDKEILE 934
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAG---LLLAGFV-APLVSLRAARAAEQAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 935 KA--GQITNEALSNIRTVAGIGVEGR---FIKAFEvELEKSYkTAIRKANVYGLcyAFSQGISFLANSAAyryggylivy 1009
Cdd:TIGR02868 186 ARlrGELAAQLTDALDGAAELVASGAlpaALAQVE-EADREL-TRAERRAAAAT--ALGAALTLLAAGLA---------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1010 edlnfsyvfrVVSSIAMSATAV------GRTFS------------YTP------SYAKAKISAARFFQLLDRKPPIDVYS 1065
Cdd:TIGR02868 252 ----------VLGALWAGGPAVadgrlaPVTLAvlvllplaafeaFAAlpaaaqQLTRVRAAAERIVEVLDAAGPVAEGS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1066 GAGEKWDNFQG-KIDFIDCKFTYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDS 1144
Cdd:TIGR02868 322 APAAGAVGLGKpTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1145 KKVNVQFLRSNIGIVSQEPVLFDCSIMDNIKYGdnTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEK 1224
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA--RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGER 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1225 QRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRL 1277
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
420-1319 |
3.06e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 176.32 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLdghdirslnirwLRDQIG 499
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREEATMEdiVQAAKDANAYNFIMAL-PQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPK 578
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSDFESER--YWRAIDVTALQHDLDLlPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 579 ILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFMLV--- 654
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMena 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 655 --TLQSQEDNTHKETGIKGKDTTEGDTPERtfSRGSYQDSlrasirQRSKSQLSHlshepplaigdhkssyEDRKDNDVL 732
Cdd:PLN03232 841 gkMDATQEVNTNDENILKLGPTVTIDVSER--NLGSTKQG------KRGRSVLVK----------------QEERETGII 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 733 VEEVepapvrrILKYNISEWPYILVGALCAAIngAVTPIYSLLFSQILKTFSlvdkEQQRSEIYSMCLFFVILGCVSlFT 812
Cdd:PLN03232 897 SWNV-------LMRYNKAVGGLWVVMILLVCY--LTTEVLRVSSSTWLSIWT----DQSTPKSYSPGFYIVVYALLG-FG 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 813 Q----FLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQgatgSQVGMMVNSFTNIFV 888
Cdd:PLN03232 963 QvavtFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKDIGDID----RNVANLMNMFMNQLW 1036
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 889 AVLIAFLFNWKLSLV-ISVFFPFLAL---------SGAVQTKMLTGFASQdkEILEKAGQITNeALSNIRTVAGIG---- 954
Cdd:PLN03232 1037 QLLSTFALIGTVSTIsLWAIMPLLILfyaaylyyqSTSREVRRLDSVTRS--PIYAQFGEALN-GLSSIRAYKAYDrmak 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 955 VEGRF----IKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGY-----LIVYEDLN----FSYVFRVV 1021
Cdd:PLN03232 1114 INGKSmdnnIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFastmgLLLSYTLNittlLSGVLRQA 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1022 SSIAMSATAVGRTFSYT--PSYAKAKISAARffqlldrkPPIDVYSGagekwdnfqGKIDFIDCKFTYpsRPDIQ-VLNG 1098
Cdd:PLN03232 1194 SKAENSLNSVERVGNYIdlPSEATAIIENNR--------PVSGWPSR---------GSIKFEDVHLRY--RPGLPpVLHG 1254
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNIkygD 1178
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---D 1331
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1179 NTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQ 1258
Cdd:PLN03232 1332 PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1259 LALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKG-AYYKLVITGAP 1319
Cdd:PLN03232 1412 RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTGP 1473
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1076-1299 |
3.41e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 159.50 E-value: 3.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1076 GKIDFIDCKFTYpsRPDI-QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRS 1154
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQEPVLFDCSIMDNIkygDNTKEISVERAIAAAKqaqlhdfvmslpekyetnVGIQGSQLSRGEKQRIAIARAIV 1234
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1235 RDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
130-378 |
4.22e-44 |
|
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: 162.42 E-value: 4.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 130 GLVDINSEVIKFSGIYAGVGVAVLIlgyfqiRLWVIT--GARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDIN 207
Cdd:cd18780 37 ALRALNQAVLILLGVVLIGSIATFL------RSWLFTlaGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 208 KIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSS 287
Cdd:cd18780 111 VLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 288 IRTVAAFGGENKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQIFLCVI 367
Cdd:cd18780 191 IRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVID-GELTTGLLTSFLLYTL 269
|
250
....*....|.
gi 1390249242 368 IAAMNIGNASS 378
Cdd:cd18780 270 TVAMSFAFLSS 280
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
389-657 |
3.56e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 167.59 E-value: 3.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 389 AASSIFQTID--RQPVMDcmsgDGYKLDriKGEIEFHNVTFHYpsRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQ 466
Cdd:PRK10790 314 AGERVFELMDgpRQQYGN----DDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 467 LIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREeATMEDIVQAAKDANAYNFIMALPQ 546
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 547 QFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVI 626
Cdd:PRK10790 465 GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTI 544
|
250 260 270
....*....|....*....|....*....|.
gi 1390249242 627 IGFEHGTAVERGTHEELLERKGVYFMLVTLQ 657
Cdd:PRK10790 545 LVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1092-1303 |
1.07e-42 |
|
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: 155.80 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGTVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1164
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDCSIMDNIKYG------DNTKEISvERAIAAAKQAQLHDfvmslpekyETNVGIQGSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:cd03260 92 PFPGSIYDNVAYGlrlhgiKLKEELD-ERVEEALRKAALWD---------EVKDRLHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1239 ILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKL 1303
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
294-653 |
1.07e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 165.77 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 294 FGGENK---EVERYEKNLMFAQRwgiwkgmVMGFFTGYMWCLIFFCYALA----FWYGSRLVldEGEYTPGTLIQIFLCV 366
Cdd:PRK11160 216 FGAEDRyrqQLEQTEQQWLAAQR-------RQANLTGLSQALMILANGLTvvlmLWLAAGGV--GGNAQPGALIALFVFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 367 IIAA----MNIGNA----SSCLeifstgcSAASSIFQTIDRQPvmDCMSGDGYKLDRIKGEIEFHNVTFHYPSRPEvKIL 438
Cdd:PRK11160 287 ALAAfealMPVAGAfqhlGQVI-------ASARRINEITEQKP--EVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 439 NNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRL 518
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 519 GREEATMEDIVQAAKDANAYNFIMAlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQ 598
Cdd:PRK11160 437 AAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL 515
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 599 GALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFML 653
Cdd:PRK11160 516 ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
417-646 |
1.71e-42 |
|
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: 164.92 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 417 KGEIEFHNVTFHYPSRPEVkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD 496
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFSTTIAENI-RLGreEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIR 575
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 576 KPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLER 646
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
169-617 |
1.74e-42 |
|
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: 164.07 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 169 RQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDInkidEAIADQM---------ALFLQRLSTALSGLLLgfyrgW 239
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQDLYvrvivpagvALVVGAAAVAAIAVLS-----V 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 240 KLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAyaKAGSIADEVLSSIRTVA---AFGGEN---KEVERYEKNLMFAQR 313
Cdd:TIGR02868 154 PAALILAAGLLLAGFVAPLVSLRAARAAEQALAR--LRGELAAQLTDALDGAAelvASGALPaalAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 314 WGIWkgmVMGFFTGYMWCLIFFCYALAFWYGSRLVLDEGeyTPGTLIQIFLCVIIAAMNIGNA-SSCLEIFSTGCSAASS 392
Cdd:TIGR02868 232 RAAA---ATALGAALTLLAAGLAVLGALWAGGPAVADGR--LAPVTLAVLVLLPLAAFEAFAAlPAAAQQLTRVRAAAER 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 393 IFQTIDRQPVMDCMSGDGYKLDRIKG-EIEFHNVTFHYPSRPEVkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRF 471
Cdd:TIGR02868 307 IVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 472 YDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTL 551
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 552 VGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRL 617
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-660 |
9.08e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 163.09 E-value: 9.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 349 LDEGEY-TPGTLIQIFLCVIIA-----------------AMNIGNASSCLEIFSTGCSAASSIFQTI-DRQPVmdcmsgd 409
Cdd:PRK11174 276 LNFGHYgTGVTLFAGFFVLILApefyqplrdlgtfyhakAQAVGAAESLVTFLETPLAHPQQGEKELaSNDPV------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 410 gykldrikgEIEFHNVTFHypsRPEVKIL-NNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdPCEGMVTLDGHDIRS 488
Cdd:PRK11174 349 ---------TIEAEDLEIL---SPDGKTLaGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 489 LNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVA 568
Cdd:PRK11174 416 LDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLA 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKG 648
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575
|
330
....*....|..
gi 1390249242 649 VYFMLVTLQSQE 660
Cdd:PRK11174 576 LFATLLAHRQEE 587
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
420-643 |
1.55e-41 |
|
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: 152.33 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-----PCEGMVTLDGHDIRSLNIR-- 492
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 493 WLRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIVQ-----AAKDANAYNFIMALP-----QQfdtlvgegg 556
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEealrkAALWDEVKDRLHALGlsggqQQ--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHGTAV 635
Cdd:cd03260 149 ---------RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLV 219
|
....*...
gi 1390249242 636 ERGTHEEL 643
Cdd:cd03260 220 EFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1096-1247 |
6.60e-41 |
|
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: 147.79 E-value: 6.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLF-DCSIMDNI 1174
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1175 KYGDNTKEISveraiAAAKQAQLHDFV--MSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:pfam00005 81 RLGLLLKGLS-----KREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
144-360 |
1.90e-40 |
|
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: 151.54 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 144 IYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQR 223
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 224 LSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVER 303
Cdd:cd18572 121 LVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 304 YEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLdEGEYTPGTLI 360
Cdd:cd18572 201 YERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVL-SGRMSAGQLV 256
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1085-1294 |
6.30e-40 |
|
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: 145.82 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYP--SRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQE 1162
Cdd:cd03246 8 FRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 PVLFDCSIMDNIkygdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqgsqLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1243 DEATSALDTESEKTVQLALDKARE-GRTCIVIAHRLSTIQNSDIIAVMSQGVV 1294
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1092-1299 |
8.79e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.83 E-value: 8.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERfydPDQGTVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 -DCSIMDNIKYGD-NTKEISVERAIAAAkqaqlhdfvMSLPEKyetnVGIQG------SQLSRGEKQRIAIARAIVRDPK 1238
Cdd:COG1126 90 pHLTVLENVTLAPiKVKKMSKAEAEERA---------MELLER----VGLADkadaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1239 ILLLDEATSALDTESEKTVqLAL--DKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:COG1126 157 VMLFDEPTSALDPELVGEV-LDVmrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
420-647 |
1.04e-39 |
|
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: 147.48 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPV--LFSTTIAENI-----RLGREEATMEDIVQAA---------KDANAYNfimaLP---QQfdtlvgegggqms 560
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVafgpeNLGLPREEIRERVEEAlelvglehlADRPPHE----LSggqKQ------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 561 ggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTV-RSADVIIGFEHGTAVERG 638
Cdd:COG1122 142 -----RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADG 216
|
....*....
gi 1390249242 639 THEELLERK 647
Cdd:COG1122 217 TPREVFSDY 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1095-1275 |
1.12e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNI 1174
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 KYGDNTKEISV--ERAIAAAKQAQLHDFVMslpekyETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:COG4619 95 PFPFQLRERKFdrERALELLERLGLPPDIL------DKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180
....*....|....*....|....*
gi 1390249242 1253 SEKTVQLALDK--AREGRTCIVIAH 1275
Cdd:COG4619 165 NTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1078-1298 |
1.13e-39 |
|
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: 145.15 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQfLRSNIG 1157
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFDCSIMDNIkygdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1092-1306 |
1.06e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQfLRSNIGIVSQEPVLF-DCSI 1170
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGDNTKEISVERAIAAAKQAqLHDFvmSLPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1251 TESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:COG1131 164 PEARRELwELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1084-1306 |
1.43e-38 |
|
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: 151.98 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1084 KFTYPSRP--DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD---SKKVNVQFLRSNIGI 1158
Cdd:COG1123 267 SKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1159 VSQEPVL-FDC--SIMDNI-----KYGDNTKEISVERAIAAAKQAQLH-DFVMSLPekyetnvgiqgSQLSRGEKQRIAI 1229
Cdd:COG1123 347 VFQDPYSsLNPrmTVGDIIaeplrLHGLLSRAERRERVAELLERVGLPpDLADRYP-----------HELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1230 ARAIVRDPKILLLDEATSALDTesekTVQLA-LD-----KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKK 1302
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDV----SVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
....
gi 1390249242 1303 LMDQ 1306
Cdd:COG1123 492 VFAN 495
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1078-1299 |
4.30e-38 |
|
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: 142.72 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQ---LLERfydPDQGTVMIDGHDSKKVN---VQ 1150
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1151 FLRSNIGIVSQEPVLFDC-SIMDNIKYgdnTKEI-SVERAIAAAKQAQLHDFVmSLPEKYEtnvgIQGSQLSRGEKQRIA 1228
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVAL---PLEIaGVPKAEIEERVLELLELV-GLEDKAD----AYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESEKTV-QLALDKARE-GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSIlALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1078-1307 |
7.82e-38 |
|
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: 142.09 E-value: 7.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPV--LFDCSIMDNIKYG----DNTKEISVERAIAAAKQaqlhdfvmslpekyetnVGIQG------SQLSRGEKQ 1225
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlGLPREEIRERVEEALEL-----------------VGLEHladrppHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
....
gi 1390249242 1304 MDQK 1307
Cdd:COG1122 222 FSDY 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1086-1296 |
9.56e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 9.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPS-RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGTVMIDGHD----SKKVNVQFLRSNIG 1157
Cdd:COG1136 13 SYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDisslSERELARLRRRHIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFDC-SIMDNI----KYGDNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARA 1232
Cdd:COG1136 90 FVFQFFNLLPElTALENValplLLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1233 IVRDPKILLLDEATSALDTESEKTV-QLALDKARE-GRTCIVIAHRLSTIQNSDIIAVMSQGVVIE 1296
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVlELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
420-634 |
1.74e-37 |
|
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: 138.89 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREeatmediVQaakdanaynfimalpqqfdtlvgegggqmsggqkqRVAIARALIRKPKI 579
Cdd:cd03246 80 YLPQDDELFSGSIAENILSGGQ-------RQ-----------------------------------RLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVRSADVIIGFEHGTA 634
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1092-1298 |
5.64e-37 |
|
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: 138.81 E-value: 5.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLFD-CSI 1170
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYG-----DNTKEISvERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:cd03259 90 AENIAFGlklrgVPKAEIR-ARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1246 TSALDTESEKTVQLALDK--AREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03259 158 LSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
146-374 |
7.38e-37 |
|
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: 141.08 E-value: 7.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 146 AGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLS 225
Cdd:cd18576 43 LGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYE 305
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 306 KNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQIFLCVIIAAMNIG 374
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLA-GELTAGDLVAFLLYTLFIAGSIG 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
420-1318 |
1.51e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.43 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEgmvtlDGHDIrslnirwLRDQIG 499
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-----DASVV-------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGreeatmedivqAAKDANAYNF---IMALPQQFDTL-------VGEGGGQMSGGQKQRVAI 569
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFG-----------SPFDPERYERaidVTALQHDLDLLpggdlteIGERGVNISGGQKQRVSM 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKV-QGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKG 648
Cdd:PLN03130 752 ARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 649 VYFMLVTLQSQEDNTHKETGIKGKDTTEGDTPERTfsrgsyqdslRASIRQRSKSQLSHlshepplaigdhkssyeDRKD 728
Cdd:PLN03130 832 LFQKLMENAGKMEEYVEENGEEEDDQTSSKPVANG----------NANNLKKDSSSKKK-----------------SKEG 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 729 NDVLV--EEVEPAPV--RRILKYNISEWPYILVGALCAAIngAVTPIYSLLFSQILKTFSlvdkEQQRSEIYSMCLFFVI 804
Cdd:PLN03130 885 KSVLIkqEERETGVVswKVLERYKNALGGAWVVMILFLCY--VLTEVFRVSSSTWLSEWT----DQGTPKTHGPLFYNLI 958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 805 LGCVSlFTQ----FLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFddlKNNP-GVLTTRLATDASQVQGATGSQVGMM 879
Cdd:PLN03130 959 YALLS-FGQvlvtLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFF---HTNPlGRIINRFAKDLGDIDRNVAVFVNMF 1034
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 880 VNSFTNIFVA-VLIAFLFNWKLSLVISVFFPFLAL-----SGAVQTKMLTGFASQdkEILEKAGQITNeALSNIRT---- 949
Cdd:PLN03130 1035 LGQIFQLLSTfVLIGIVSTISLWAIMPLLVLFYGAylyyqSTAREVKRLDSITRS--PVYAQFGEALN-GLSTIRAykay 1111
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 950 --VAGIgvEGRF----IKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYG------GYLIVYEdLN---- 1013
Cdd:PLN03130 1112 drMAEI--NGRSmdnnIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAafastmGLLLSYA-LNitsl 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1014 FSYVFRVVSSIAMSATAVGRTFSYT--PSYAKAKISaarffqllDRKPPidvysgagEKWDNfQGKIDFIDCKFTYpsRP 1091
Cdd:PLN03130 1189 LTAVLRLASLAENSLNAVERVGTYIdlPSEAPLVIE--------NNRPP--------PGWPS-SGSIKFEDVVLRY--RP 1249
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQ-VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSI 1170
Cdd:PLN03130 1250 ELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTV 1329
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIkygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:PLN03130 1330 RFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1251 TESEKTVQLALDKarEGRTC--IVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKL-MDQKGAYYKLV-ITGA 1318
Cdd:PLN03130 1407 VRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVqSTGA 1476
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
138-360 |
1.66e-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: 139.99 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 138 VIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQM 217
Cdd:cd07346 38 LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 218 ALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGE 297
Cdd:cd07346 118 LQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 298 NKEVERYEKNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd07346 198 EREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQ-GSLTIGELV 259
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
758-1051 |
3.36e-36 |
|
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: 139.23 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 758 GALCAAINGAVTPIYSLLFSQILKTFSlvdKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFK 837
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTII---KGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 838 AMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAV 917
Cdd:cd18557 78 SLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 918 QTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKAnvygLCYAFSQGISFLANS 997
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKA----LANALFQGITSLLIY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 998 AA----YRYGGYLIVYEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARF 1051
Cdd:cd18557 232 LSlllvLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1086-1298 |
4.71e-36 |
|
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: 136.87 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRPD-IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFL---RSNIGIVSQ 1161
Cdd:cd03257 10 SFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 E------PVLfdcSIMDNIK------YGDNTKEISVERAIAAAKQAQLHDFVM-SLPekyetnvgiqgSQLSRGEKQRIA 1228
Cdd:cd03257 90 DpmsslnPRM---TIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLPEEVLnRYP-----------HELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESEKTVQLALDKARE--GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
418-639 |
8.39e-36 |
|
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: 135.23 E-value: 8.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHY-PSRPEVkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD 496
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFSTTIAENIRLgREEATMEDIVQAAKDANAYNFIMALPQQFdtlvgegggqmsggqkqrVAIARALIRK 576
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALRVSEGGLNLSQGQRQL------------------LCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGT 639
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1089-1292 |
3.78e-35 |
|
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: 132.31 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDG--HDSKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 -DCSIMDNIKYGdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqgsqLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1246 TSALDTESEKTVQLALD--KAREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1086-1290 |
3.99e-35 |
|
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: 133.75 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSR-PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflrsnIGIVSQEPV 1164
Cdd:cd03293 9 TYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----RGYVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFD-CSIMDNIKYGDNTKEISV----ERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03293 84 LLPwLTVLDNVALGLELQGVPKaearERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1240 LLLDEATSALDTESEKTVQLALDK--AREGRTCIVIAHRLS-TIQNSDIIAVMS 1290
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLS 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
420-615 |
4.93e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.02 E-value: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENI----RLGREEATMEDIVQAAKDANAYNFIMALP--------QQfdtlvgegggqmsggqkqRV 567
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPverlsggeRQ------------------RL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAH 615
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSH 189
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1095-1316 |
8.44e-35 |
|
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: 134.27 E-value: 8.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNI 1174
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 kygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1254
Cdd:cd03288 116 ---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1255 KTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQK-GAYYKLVIT 1316
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1080-1292 |
9.52e-35 |
|
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: 130.44 E-value: 9.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1080 FIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIV 1159
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQepvlfdcsimdnikygdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqgsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1240 LLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
420-646 |
1.44e-34 |
|
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: 140.04 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP--EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWL 494
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 RDQIGIVEQEPV--LF-STTIAENI-------RLGREEATMEDIVQA-------AKDANAYnfimalPQQFdtlvgeggg 557
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIaeplrlhGLLSRAERRERVAELlervglpPDLADRY------PHELsgg------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 558 qmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGTA 634
Cdd:COG1123 409 -----qrqRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|..
gi 1390249242 635 VERGTHEELLER 646
Cdd:COG1123 484 VEDGPTEEVFAN 495
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
420-638 |
1.45e-34 |
|
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: 130.51 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEvKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNiRWLRDQIG 499
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENirLGREEATMEdivqaakdanaynfimalpQQfdtlvgegggqmsggqkqRVAIARALIRKPKI 579
Cdd:cd03247 79 VLNQRPYLFDTTLRNN--LGRRFSGGE-------------------RQ------------------RLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERG 638
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1092-1299 |
1.97e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCSI 1170
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFpHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGdntkeISVERAIAAAKQAQLHDfVMSLpekyetnVGIQG------SQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:COG3842 95 AENVAFG-----LRMRGVPKAEIRARVAE-LLEL-------VGLEGladrypHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1245 ATSALDTESEKTVQLALDK--AREGRTCIVIAHRLS---TIqnSDIIAVMSQGVVIEKGT 1299
Cdd:COG3842 162 PLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1082-1292 |
2.22e-34 |
|
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: 131.44 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1082 DCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQ 1161
Cdd:cd03225 4 NLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 EP--VLFDCSIMDNIKYG-DN---TKEISVERAIAAAKQaqlhdfvmslpekyetnVGIQG------SQLSRGEKQRIAI 1229
Cdd:cd03225 83 NPddQFFGPTVEEEVAFGlENlglPEEEIEERVEEALEL-----------------VGLEGlrdrspFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1230 ARAIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1086-1305 |
5.26e-34 |
|
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: 131.46 E-value: 5.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPv 1164
Cdd:COG1124 10 SYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 lfdcsimdnikYGD-NTKEiSVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGS-------QLSRGEKQRIAIARAIVRD 1236
Cdd:COG1124 89 -----------YASlHPRH-TVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfldryphQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1237 PKILLLDEATSALDTesekTVQ---LAL--D-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:COG1124 157 PELLLLDEPTSALDV----SVQaeiLNLlkDlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1078-1299 |
5.35e-34 |
|
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: 138.11 E-value: 5.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGTVMIDGHDSKKVNVQFLRS 1154
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQEP--VLFDCSIMDNI----KYGDNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIA 1228
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIaealENLGLSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESEKTVQLALDK--AREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGT 1299
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1078-1294 |
7.44e-34 |
|
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: 128.28 E-value: 7.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKvNVQFLRSNIG 1157
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLF-DCSIMDNIKYgdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqgsqlSRGEKQRIAIARAIVRD 1236
Cdd:cd03230 77 YLPEEPSLYeNLTVRENLKL-------------------------------------------SGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1237 PKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVV 1294
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFwELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
421-633 |
9.77e-34 |
|
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: 129.51 E-value: 9.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPSRPEvKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGI 500
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 501 VEQEP--VLFSTTIAENI-----RLGREEATMEDIV-QAAKDANAYNFIMALP-------QQfdtlvgegggqmsggqkq 565
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVafgleNLGLPEEEIEERVeEALELVGLEGLRDRSPftlsggqKQ------------------ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 566 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRS-ADVIIGFEHGT 633
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1078-1298 |
1.20e-33 |
|
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: 129.45 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDS---KKVNVQFLRS 1154
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQE-PVLFDCSIMDNIKY-----GDNTKEISvERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIA 1228
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIR-KRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAhrlstIQNSDIIAVMSQGV-VIEKG 1298
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA-----THAKELVDTTRHRViALERG 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
438-587 |
1.34e-33 |
|
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: 126.99 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFS-TTIAENI 516
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 517 RLGREeatMEDIVQAAKDANAYNFIMALPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATS 587
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1078-1308 |
1.39e-33 |
|
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: 129.98 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFlRSNIG 1157
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLFD-CSIMDNIKYGDNTKEISVERAIAAAKQ-AQLhdfvMSLPEKYETNVGiqgsQLSRGEKQRIAIARAIVR 1235
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEElIEL----LGLEEFLDRRVG----ELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIA-HRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQKG 1308
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
140-359 |
1.39e-33 |
|
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: 131.87 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 140 KFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMAL 219
Cdd:cd18573 42 TFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 220 FLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENK 299
Cdd:cd18573 122 GLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 300 EVERYEK--NLMF--AQRWGIWKGMVMG--FFTGYMwclIFFCyalAFWYGSRLVLdEGEYTPGTL 359
Cdd:cd18573 202 EVERYAKkvDEVFdlAKKEALASGLFFGstGFSGNL---SLLS---VLYYGGSLVA-SGELTVGDL 260
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1092-1294 |
1.80e-33 |
|
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: 128.80 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERfydPDQGTVMIDGH--DSKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 -DCSIMDNIKYGDNT-----KEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:cd03262 89 pHLTVLENITLAPIKvkgmsKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1241 LLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVV 1294
Cdd:cd03262 158 LFDEPTSALDPELVGEVlDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
113-651 |
2.01e-33 |
|
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: 140.85 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 113 VWINSSFNQNMTNGTScglvdiNSEVIKFsGIYAGVGV--AVLILGYFQIRlwVITGARQIRKMRKFYFRRIMRMEIGWF 190
Cdd:TIGR00957 986 YWLSLWTDDPMVNGTQ------NNTSLRL-SVYGALGIlqGFAVFGYSMAV--SIGGIQASRVLHQDLLHNKLRSPMSFF 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 191 DCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLlgfyrgwkltlVILAVSPLIGIGAAVIGL--------- 261
Cdd:TIGR00957 1057 ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALI-----------VILLATPIAAVIIPPLGLlyffvqrfy 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 262 --SVAKFTELELKAYAKAGSIADEVLSSIRTVAAFggenKEVERYEKN--------------LMFAQRWgiwkgMVMGF- 324
Cdd:TIGR00957 1126 vaSSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIHQsdlkvdenqkayypSIVANRW-----LAVRLe 1196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 325 FTGYmwCLIFFcyALAFWYGSRLVLDEGeyTPGTLIQIFLCVIIAAMNIGNASSCLEIFSTGCSAASSIFQTIDRQP--V 402
Cdd:TIGR00957 1197 CVGN--CIVLF--AALFAVISRHSLSAG--LVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqI 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 403 MDCMSGDGYKLdriKGEIEFHNVTFHYpsRPEVK-ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTL 481
Cdd:TIGR00957 1271 QETAPPSGWPP---RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 482 DGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRlGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSG 561
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 562 GQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHE 641
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPS 1504
|
570
....*....|
gi 1390249242 642 ELLERKGVYF 651
Cdd:TIGR00957 1505 NLLQQRGIFY 1514
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1078-1298 |
3.12e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.25 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN---VQFLRS 1154
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQE-PVLFDCSIMDNIKY-----GDNTKEISvERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIA 1228
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIR-RRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTE-SEKTVQLaLDKAREGRTCIVIA-HrlstiqNSDIIAVMSQGVV-IEKG 1298
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtH------DLELVDRMPKRVLeLEDG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1086-1299 |
3.42e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 131.74 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERfydPDQGTVMIDGHDSKKVNVQFL---RSNIGI 1158
Cdd:COG1135 10 TFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELraaRRKIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1159 VSQEPVLFD-CSIMDNIKY-----GDNTKEIsveraiaAAKQAQLHDFVmslpekyetnvGIQG------SQLSRGEKQR 1226
Cdd:COG1135 87 IFQHFNLLSsRTVAENVALpleiaGVPKAEI-------RKRVAELLELV-----------GLSDkadaypSQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1227 IAIARAIVRDPKILLLDEATSALDTESEKTVqLAL-DKARE--GRTCIVIAHRLSTIQnsDI---IAVMSQGVVIEKGT 1299
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSI-LDLlKDINRelGLTIVLITHEMDVVR--RIcdrVAVLENGRIVEQGP 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1093-1294 |
3.54e-33 |
|
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: 127.99 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERfydPDQGTVMIDGHDSKKVN----VQFLRSNIGIVSQE--- 1162
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSekelAAFRRRHIGFVFQSfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 -PVLfdcSIMDNIKY-----GDNTKEIsVERAIAAAKQaqlhdfvMSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRD 1236
Cdd:cd03255 94 lPDL---TALENVELplllaGVPKKER-RERAEELLER-------VGLGDRLNHYP----SELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1237 PKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIA-HRLSTIQNSDIIAVMSQGVV 1294
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVmELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1077-1292 |
6.23e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.67 E-value: 6.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1077 KIDFIDCKFTYPSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQFLRSN 1155
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1156 IGIVSQEPVLFD-CSIMDNIKYG----DNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIA 1230
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlelrGVPKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1231 RAIVRDPKILLLDEATSALDTESEKTVQLALDK--AREGRTCIVIAH------RLstiqnSDIIAVMSQG 1292
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
420-633 |
7.85e-33 |
|
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: 125.76 E-value: 7.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN--IRWLRDQ 497
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFST-TIAENIRLGreeatmedivqaakdanaynfimaLP---QQfdtlvgegggqmsggqkqRVAIARAL 573
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG------------------------LSggqQQ------------------RVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTV-RSADVIIGFEHGT 633
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1078-1299 |
8.38e-33 |
|
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: 127.62 E-value: 8.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRpdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNV---QFLRS 1154
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQEPVLFDC-SIMDNI-----KYGDNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIA 1228
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVafplrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1229 IARAIVRDPKILLLDEATSALD-TESEKTVQLALD-KAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
755-1008 |
2.22e-32 |
|
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: 128.05 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQIlktFSLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKF 834
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLL---IDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 835 GFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALS 914
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 915 GAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFL 994
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....
gi 1390249242 995 ANSAAYRYGGYLIV 1008
Cdd:cd07346 236 GTALVLLYGGYLVL 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1092-1303 |
3.22e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.69 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD--PDQ---GTVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1164
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDCSIMDNIKYG---------DNTKEIsVERAIaaaKQA--------QLHDfvmslpekyetnvgiQGSQLSRGEKQRI 1227
Cdd:COG1117 103 PFPKSIYDNVAYGlrlhgikskSELDEI-VEESL---RKAalwdevkdRLKK---------------SALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREgRTCIVI-------AHRLstiqnSDIIAVMSQGVVIEKGTH 1300
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARV-----SDYTAFFYLGELVEFGPT 237
|
...
gi 1390249242 1301 KKL 1303
Cdd:COG1117 238 EQI 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
421-633 |
3.49e-32 |
|
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: 123.12 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGI 500
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 501 VEQepvlFSttiaenirlGREeatmedivqaakdanaynfimalpQQfdtlvgegggqmsggqkqRVAIARALIRKPKIL 580
Cdd:cd00267 78 VPQ----LS---------GGQ------------------------RQ------------------RVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 581 LLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHGT 633
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
420-615 |
5.89e-32 |
|
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: 124.51 E-value: 5.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSR-PEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNirwlrDQI 498
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFS-TTIAENIRLG----------REEATME--DIVQAAKDANAYnfimalP-------QQfdtlvgegggq 558
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvpkaeARERAEEllELVGLSGFENAY------PhqlsggmRQ----------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 559 msggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAH 615
Cdd:cd03293 139 -------RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTH 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1092-1306 |
6.06e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 125.04 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSkkVNVQFLRSNIGIVSQEPVLF-DCSI 1170
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGDNTKEIS---VERAIAAA-KQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03300 90 FENIAFGLRLKKLPkaeIKERVAEAlDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1247 SALDTESEKTVQLALDK--AREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:cd03300 159 GALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
420-646 |
1.17e-31 |
|
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: 131.18 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDP---CEGMVTLDGHDIRSLNIRWLRD 496
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEP--VLFSTTIAENI-------RLGREEATmEDIVQAAKDANAYNFIMALPQQFdtlvgegggqmSGGQKQRV 567
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIaealenlGLSRAEAR-ARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELL 644
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
..
gi 1390249242 645 ER 646
Cdd:COG1123 232 AA 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1094-1299 |
1.28e-31 |
|
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: 124.32 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNV---QFLRSNIGIVSQEPVLFDC-S 1169
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNI-----KYGDNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:COG1127 99 VFENVafplrEHTDLSEAEIRELVLEKLELVGLPGAADKMP-----------SELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1245 ATSALD--TeSEKTVQLALD-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:COG1127 168 PTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
420-636 |
1.62e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.61 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPS-RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLI---QRfydPCEGMVTLDGHDIRSLNI---- 491
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 492 RWLRDQIGIVEQEPVLFST-TIAENIRL-------GREEATmEDIVQAAKDANAYNFIMALP-------QQfdtlvgegg 556
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALplllagvSRKERR-ERARELLERVGLGDRLDHRPsqlsggqQQ--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRSADVIIGFEHGTA 634
Cdd:COG1136 152 ---------RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
..
gi 1390249242 635 VE 636
Cdd:COG1136 223 VS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
420-644 |
2.25e-31 |
|
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: 123.46 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLR 495
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQIGIVEQEPVLFST-TIAENIRLGREEATMEDIVQAAK------------DANAYnfimalPQQFdtlvgegggqmSGG 562
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERvlellelvgledKADAY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 563 QKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGT 639
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....*
gi 1390249242 640 HEELL 644
Cdd:cd03258 225 VEEVF 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1085-1299 |
3.91e-31 |
|
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: 123.23 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPV 1164
Cdd:COG1120 9 VGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 L-FDCSIMDNIKYG------------DNTKEIsVERAIAAakqaqlhdfvmslpekyetnVGIQG------SQLSRGEKQ 1225
Cdd:COG1120 86 ApFGLTVRELVALGryphlglfgrpsAEDREA-VEEALER--------------------TGLEHladrpvDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALDtesektV--QLAL-----DKARE-GRTCIVIAHRLS-TIQNSDIIAVMSQGVVIE 1296
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLD------LahQLEVlellrRLARErGRTVVMVLHDLNlAARYADRLVLLKDGRIVA 218
|
...
gi 1390249242 1297 KGT 1299
Cdd:COG1120 219 QGP 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
420-644 |
3.99e-31 |
|
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: 123.23 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVL-FSTTIAENIRLGR---------EEATMEDIVQAA-KDANAYNFIMalpQQFDTLvgegggqmsggqkqRVA 568
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHLAD---RPVDELsgg--------erqRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
420-644 |
4.13e-31 |
|
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: 122.79 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLgreEATMEDIVQAAKDANAYNFI--MALPQQfdTLVGEGGGQMSGGQKQRVAIARALIRK 576
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIAL---VPKLLKWPKEKIRERADELLalVGLDPA--EFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRL-STVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
154-651 |
4.16e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.56 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 154 ILGYFQIRL------WVITGA-RQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLST 226
Cdd:PLN03232 958 LLGFGQVAVtftnsfWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQ 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 227 ALSGLLLgfyRGWKLTLVILAVSPL-IGIGAAVIglsVAKFTELELK---------AYAKAGSiADEVLSSIRTVAAFGG 296
Cdd:PLN03232 1038 LLSTFAL---IGTVSTISLWAIMPLlILFYAAYL---YYQSTSREVRrldsvtrspIYAQFGE-ALNGLSSIRAYKAYDR 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 297 ENKEVERY-EKNLMF------AQRWGIWKGMVMGfftGYM-WCLIFFCY--------ALAFWYGSRLVLdegEYTPgTLI 360
Cdd:PLN03232 1111 MAKINGKSmDNNIRFtlantsSNRWLTIRLETLG---GVMiWLTATFAVlrngnaenQAGFASTMGLLL---SYTL-NIT 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 361 QIFLCVIIAAMNIGNASSCLEIFSTGC---SAASSIFQtiDRQPVMDCMSGdgykldrikGEIEFHNVTFHYpsRPEVK- 436
Cdd:PLN03232 1184 TLLSGVLRQASKAENSLNSVERVGNYIdlpSEATAIIE--NNRPVSGWPSR---------GSIKFEDVHLRY--RPGLPp 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENI 516
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 517 RLGREEATmEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAK 596
Cdd:PLN03232 1331 DPFSEHND-ADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 597 VQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYF 651
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
420-638 |
7.11e-31 |
|
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: 121.84 E-value: 7.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD-- 496
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 -QIGIVEQEPvlFST-----TIAENI---------------RLGREEATMEDIVQAAKDANAYnfimalPQQFdtlvgeg 555
Cdd:cd03257 82 kEIQMVFQDP--MSSlnprmTIGEQIaeplrihgklskkeaRKEAVLLLLVGVGLPEEVLNRY------PHELsgg---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHG 632
Cdd:cd03257 150 -------qrqRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
....*.
gi 1390249242 633 TAVERG 638
Cdd:cd03257 223 KIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
420-632 |
7.91e-31 |
|
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: 121.44 E-value: 7.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPE-VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN----IRWL 494
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 RDQIGIVEQEPVLFST-TIAENIRLG----------REEATME--DIVQAAKDANAYnfimalP-------QQfdtlvge 554
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPlllagvpkkeRRERAEEllERVGLGDRLNHY------PselsggqQQ------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 555 gggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRSADVIIGFEHG 632
Cdd:cd03255 148 -----------RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1096-1299 |
1.23e-30 |
|
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: 122.37 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN---VQFLRSN-IGIVSQEPVLF-DCSI 1170
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYG----DNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03294 120 LENVAFGlevqGVPRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1247 SALDTESEKTVQ---LALdKAREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03294 189 SALDPLIRREMQdelLRL-QAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGT 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1078-1304 |
1.93e-30 |
|
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: 120.87 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVLF-DCSIMDNIkyGDNTKEISVERAIAAAKQAQLHDFVMSLPEKYetnVGIQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:cd03295 79 YVIQQIGLFpHMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 1237 PKILLLDEATSALDTESEKTVQLALDKARE--GRTCIVIAHRL-STIQNSDIIAVMSQGVVIEKGTHKKLM 1304
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
141-651 |
3.01e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 130.63 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 141 FSGIYAGVG---VAVLILGYFqirlWVITGA-RQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQ 216
Cdd:PLN03130 955 YNLIYALLSfgqVLVTLLNSY----WLIMSSlYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 217 MALFLQRLSTALSG-LLLGFYRgwklTLVILAVSPLIgigaavIGLSVA----KFTELELK---------AYAKAGSiAD 282
Cdd:PLN03130 1031 VNMFLGQIFQLLSTfVLIGIVS----TISLWAIMPLL------VLFYGAylyyQSTAREVKrldsitrspVYAQFGE-AL 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 283 EVLSSIRT------VAAFGGENKEVE-RYEKNLMFAQRWgiwKGMVMGFFTGYMwclIFFCYALAFWYGSRlVLDEGEYT 355
Cdd:PLN03130 1100 NGLSTIRAykaydrMAEINGRSMDNNiRFTLVNMSSNRW---LAIRLETLGGLM---IWLTASFAVMQNGR-AENQAAFA 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 356 P--GTLIQIflcviiaAMNIGNA-SSCLEIfstgCSAASSIFQTIDR-----------QPVM-DCMSGDGYKLdriKGEI 420
Cdd:PLN03130 1173 StmGLLLSY-------ALNITSLlTAVLRL----ASLAENSLNAVERvgtyidlpseaPLVIeNNRPPPGWPS---SGSI 1238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYpsRPEVK-ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PLN03130 1239 KFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAENIRLGREEATMeDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKI 579
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDPFNEHNDA-DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYF 651
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
420-636 |
6.97e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.62 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrPEVKILNNLSMVIKPGEttaFV---GSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRW 493
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGE---FVfltGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQE-PVLFSTTIAENIRL-----GREEATMEDIVQAAKD-----ANAYNFIMALP---QQfdtlvgegggqm 559
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDlvglsDKAKALPHELSggeQQ------------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 560 sggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADV-IIGFEHGTAVE 636
Cdd:COG2884 145 ------RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1072-1307 |
7.16e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1072 DNFQGKIDFIDCKFTYPSRpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQF 1151
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQEP--VLFDCSIMDNIKYGDNTKEISVE--RAI--AAAKQAQLHDFVMSLPEKyetnvgiqgsqLSRGEKQ 1225
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENKKVPPKkmKDIidDLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGR--TCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
....
gi 1390249242 1304 MDQK 1307
Cdd:PRK13632 230 LNNK 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
420-647 |
8.73e-30 |
|
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: 119.84 E-value: 8.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRW-LRDQI 498
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEP--VLFSTT----IA---ENIRLGREEatMEDIVQ-AAKDANAYNFIMALPQ-------Qfdtlvgegggqmsg 561
Cdd:TIGR04520 80 GMVFQNPdnQFVGATveddVAfglENLGVPREE--MRKRVDeALKLVGMEDFRDREPHllsggqkQ-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 562 gqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGT 639
Cdd:TIGR04520 144 ----RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*...
gi 1390249242 640 HEELLERK 647
Cdd:TIGR04520 220 PREIFSQV 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1094-1299 |
8.75e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.18 E-value: 8.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGTVMIDGHDSKkVNVQFLRSNIGIVSQEPVLF-DCS 1169
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLF-TNLPPRERRVGFVFQHYALFpHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGdntkeISVERAIAAAKQAQlhdfVMSLPEKyetnVGIQG------SQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:COG1118 92 VAENIAFG-----LRVRPPSKAEIRAR----VEELLEL----VQLEGladrypSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1244 EATSALDTESEKTVQLALdkaRE-----GRTCIVIAH------RLstiqnSDIIAVMSQGVVIEKGT 1299
Cdd:COG1118 159 EPFGALDAKVRKELRRWL---RRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-646 |
1.29e-29 |
|
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: 118.75 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPE-VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQI 498
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVL-----FS--TTIAENIRLGREEATMEDIVQAAKDanaynfiMALP---------------QQfdtlvgegg 556
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQ-------VGLPpsfldryphqlsggqRQ--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTV-RSADVIIGFEHGT 633
Cdd:COG1124 146 ---------RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVaHLCDRVAVMQNGR 216
|
250
....*....|...
gi 1390249242 634 AVERGTHEELLER 646
Cdd:COG1124 217 IVEELTVADLLAG 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
418-654 |
4.67e-29 |
|
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: 117.70 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYPS--RPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLR 495
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQIGIVEQEPVLFSTTIAENIRLGREeATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIR 575
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 576 KPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERK-GVYFMLV 654
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1078-1292 |
4.72e-29 |
|
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: 115.64 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDIQ--VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL--ErfYDPDQGTVmidghdskkvnvqFLR 1153
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1154 SNIGIVSQEPVLFDCSIMDNIKYGdntKEISVERAIAAAKQAQLH-DFVMsLPEKYETNVGIQGSQLSRGEKQRIAIARA 1232
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFG---KPFDEERYEKVIKACALEpDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1233 IVRDPKILLLDEATSALDTESEKTV--QLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQG 1292
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
420-645 |
5.55e-29 |
|
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: 116.62 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRD 496
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFST-TIAENIRLG-RE-----EATMEDIVQAAKDA----NAYNFI-------MAlpqqfdtlvgegggq 558
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtdlsEAEIRELVLEKLELvglpGAADKMpselsggMR--------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 559 msggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTAV 635
Cdd:COG1127 148 ------KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|
gi 1390249242 636 ERGTHEELLE 645
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1092-1299 |
5.79e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.79 E-value: 5.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLFD-CSI 1170
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYPhMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYG-----DNTKEISvERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:COG3839 93 YENIAFPlklrkVPKAEID-RRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1246 TSALD------TESE-KTVQlaldkAREGRTCIVIAHRLS---TIqnSDIIAVMSQGVVIEKGT 1299
Cdd:COG3839 161 LSNLDaklrveMRAEiKRLH-----RRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
420-648 |
6.06e-29 |
|
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: 116.88 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNiRWLRDQIG 499
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENIRLgreEATMEDIVQAAKDANAYNFI--MALPQQFDTLVgeggGQMSGGQKQRVAIARALIRK 576
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRV----GELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERKG 648
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
420-643 |
8.59e-29 |
|
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: 116.13 E-value: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSL---NIRWLRD 496
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFS-TTIAENI---RLGREEA--------TMEDIVQAAK-------DANAYNFIMALP---QQfdtlvge 554
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVlsgRLGRRSTwrslfglfPKEEKQRALAalervglLDKAYQRADQLSggqQQ------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 555 gggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEH 631
Cdd:cd03256 152 -----------RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKD 220
|
250
....*....|..
gi 1390249242 632 GTAVERGTHEEL 643
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
781-1007 |
9.50e-29 |
|
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: 117.64 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 781 KTFSLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTR 860
Cdd:cd18572 21 AVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 861 LATDASQVqgatGSQVGMMVNSFTNIFVAVL--IAFLFN--WKLSLVISVFFPFLALS----GAVQTKMltgfASQDKEI 932
Cdd:cd18572 99 LTSDCQKV----SDPLSTNLNVFLRNLVQLVggLAFMFSlsWRLTLLAFITVPVIALItkvyGRYYRKL----SKEIQDA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 933 LEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLI 1007
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLV 245
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
787-1013 |
1.10e-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: 117.35 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 787 DKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDAS 866
Cdd:cd18780 33 GGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 867 QVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSN 946
Cdd:cd18780 111 VLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISN 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 947 IRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLN 1013
Cdd:cd18780 191 IRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELT 257
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1091-1306 |
1.13e-28 |
|
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: 115.90 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCS 1169
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGDNTKEISvERAIAAAKQAQLHDFVM-----SLPEKYEtnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLKlvqldWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1245 ATSALDTESEKTVQLALDKARE--GRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1092-1299 |
1.13e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCSI 1170
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGDNTK-----EISvERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PRK09452 104 FENVAFGLRMQktpaaEIT-PRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1246 TSALDTESEKTVQLALdKA--RE-GRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK09452 172 LSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
420-638 |
1.52e-28 |
|
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: 114.54 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwLRDqIG 499
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENI-----RLGREEATMEDIV-QAAKDANAYNFIMALP-------QQfdtlvgegggqmsggqkq 565
Cdd:cd03259 76 MVFQDYALFPHlTVAENIafglkLRGVPKAEIRARVrELLELVGLEGLLNRYPhelsggqQQ------------------ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 566 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLS-TVRSADVIIGFEHGTAVERG 638
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
420-615 |
1.53e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 115.96 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlrdqI 498
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFS-TTIAENIRLG----------REEATME--DIVQAAKDANAYnfimalP-------QQfdtlvgegggq 558
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgvpkaeRRERAREllELVGLAGFEDAY------PhqlsggmRQ----------- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 559 msggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAH 615
Cdd:COG1116 146 -------RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1077-1303 |
2.15e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1077 KIDFIDCKFTYPSRPDiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNI 1156
Cdd:PRK13635 5 IIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1157 GIVSQEPvlfD-----CSIMDNIKYG-DNT---KEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRI 1227
Cdd:PRK13635 84 GMVFQNP---DnqfvgATVQDDVAFGlENIgvpREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALD----TESEKTVQLAldKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDprgrREVLETVRQL--KEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1086-1307 |
3.01e-28 |
|
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: 114.59 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD---SKKVNVQFLRSNIGIVSQE 1162
Cdd:cd03256 9 TYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 PVLFD-CSIMDNIKYG------------DNTKEISVERAIAAAKQAQLHDFVMslpekyetnvgIQGSQLSRGEKQRIAI 1229
Cdd:cd03256 87 FNLIErLSVLENVLSGrlgrrstwrslfGLFPKEEKQRALAALERVGLLDKAY-----------QRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1230 ARAIVRDPKILLLDEATSALDTESEKTV-QLALDKARE-GRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVmDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAELTDE 235
|
.
gi 1390249242 1307 K 1307
Cdd:cd03256 236 V 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
420-646 |
3.83e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 114.32 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI--RSLNIRWLRDQ 497
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFS-TTIAENIRLG--------REEAT---ME--DIVQAAKDANAYnfimalP-------QQfdtlvgegg 556
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeraMEllERVGLADKADAY------PaqlsggqQQ--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVqgaLNKIQH----GHTIISVAHRLSTVRS-ADVIIGFEH 631
Cdd:COG1126 144 ---------RVAIARALAMEPKVMLFDEPTSALDPELVGEV---LDVMRDlakeGMTMVVVTHEMGFAREvADRVVFMDG 211
|
250
....*....|....*
gi 1390249242 632 GTAVERGTHEELLER 646
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1095-1299 |
5.06e-28 |
|
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: 113.97 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCSIMDN 1173
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYGDNTKEIsveraiaaaKQAQLHDFVMSLPEKyetnVGI------QGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:cd03299 92 IAYGLKKRKV---------DKKEIERKVLEIAEM----LGIdhllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1248 ALDTESEKTVQLALDKARE--GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1086-1306 |
5.39e-28 |
|
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: 116.31 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDP---DQGTVMIDGHD----SKKVNVQFLRSNIG 1157
Cdd:COG0444 10 YFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklSEKELRKIRGREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEP---------VLFdcSIMDNIKY-GDNTKEISVERAIAAAKQAQLHDfvmslPEKYEtnvgiqGS---QLSRGEK 1224
Cdd:COG0444 90 MIFQDPmtslnpvmtVGD--QIAEPLRIhGGLSKAEARERAIELLERVGLPD-----PERRL------DRyphELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1225 QRIAIARAIVRDPKILLLDEATSALDTesekTVQ---LAL--D-KAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEK 1297
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDV----TIQaqiLNLlkDlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEE 232
|
....*....
gi 1390249242 1298 GTHKKLMDQ 1306
Cdd:COG0444 233 GPVEELFEN 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
420-643 |
7.00e-28 |
|
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: 113.37 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRD 496
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLF-STTIAENIRLG-RE-----EATMEDIVQAAKDAnaynfiMALPQQFDTLVgeggGQMSGGQKQRVAI 569
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPlREhtrlsEEEIREIVLEKLEA------VGLRGAEDLYP----AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEEL 643
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1093-1299 |
7.30e-28 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 113.30 E-value: 7.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQfLRSNIGIVS--QEPVLF-DCS 1169
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNI--------KYGDNTKEISVERAIAAAKQAQLHDFVmSLPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:cd03219 92 VLENVmvaaqartGSGLLLARARREEREARERAEELLERV-GLADLADRPAG----ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1242 LDEATSAL-DTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1086-1303 |
7.38e-28 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 112.98 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRPDIqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKvNVQFLRSNIGIVSQEPVL 1165
Cdd:cd03263 9 TYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1166 FD-CSIMDNIKY-----GDNTKEISVEraiaaakQAQLHDfVMSLPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03263 87 FDeLTVREHLRFyarlkGLPKSEIKEE-------VELLLR-VLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1240 LLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKL 1303
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
406-646 |
8.96e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.59 E-value: 8.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 406 MSGDGYKLDRIkgeIEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD--P---CEGMVT 480
Cdd:COG1117 1 MTAPASTLEPK---IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 481 LDGHDI--RSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIV-----QAA-----KD---ANAyn 539
Cdd:COG1117 75 LDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVeeslrKAAlwdevKDrlkKSA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 540 fiMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHR 616
Cdd:COG1117 153 --LGLSggqQQ------------------RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|.
gi 1390249242 617 LS-TVRSADVIIGFEHGTAVERGTHEELLER 646
Cdd:COG1117 213 MQqAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
420-632 |
1.20e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 113.23 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRD 496
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFS-TTIAENI---RLGREEA--------TMEDIVQAAKdanaynfimALP------------------- 545
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTSTwrsllglfPPEDRERALE---------ALErvgladkayqradqlsggq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 546 QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS- 622
Cdd:COG3638 152 QQ------------------RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRy 213
|
250
....*....|
gi 1390249242 623 ADVIIGFEHG 632
Cdd:COG3638 214 ADRIIGLRDG 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
420-646 |
1.36e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.97 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRDQIG 499
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLG----------REEATME--DIVQAAKDANAYnfIMALP---QQfdtlvgegggqmsggq 563
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrmrgvpkaeIRARVAEllELVGLEGLADRY--PHQLSggqQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 564 kqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLS---TVrsADVIIGFEHGTAVERG 638
Cdd:COG3842 143 --RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
....*...
gi 1390249242 639 THEELLER 646
Cdd:COG3842 219 TPEEIYER 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1085-1298 |
1.37e-27 |
|
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: 110.60 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQepv 1164
Cdd:cd03214 7 VGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 lfdcsimdnikygdntkeisveraiaAAKQAQLHDFVmslpekyETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03214 81 --------------------------ALELLGLAHLA-------DRPF----NELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1245 ATSALDTESEKTV-QLALDKARE-GRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03214 124 PTSHLDIAHQIELlELLRRLARErGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1091-1295 |
1.46e-27 |
|
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: 109.83 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdskkvnvqflrsnigivsqEPVLFDcsi 1170
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFA--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 mdnikygdntkeiSVERAIAAakqaqlhdfvmslpekyetnvGIQG-SQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:cd03216 68 -------------SPRDARRA---------------------GIAMvYQLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1390249242 1250 -DTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVI 1295
Cdd:cd03216 114 tPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
429-1320 |
1.70e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 121.81 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 429 YPSRPEVkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVtldghdirslnirWLRDQIGIVEQEPVLF 508
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 STTIAENIRLGREE--ATMEDIVQAAK-DANaynfIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMA 585
Cdd:PTZ00243 734 NATVRGNILFFDEEdaARLADAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 586 TSALDNE-SEAKVQ----GALnkiqHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKgvyfMLVTLQSQE 660
Cdd:PTZ00243 810 LSALDAHvGERVVEecflGAL----AGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS----LYATLAAEL 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 661 -DNTHKETGIKGKDTTEGDTPERTFSrgsyqdslrasirqrsksqlshlSHEPPLAIGDHKSSYEDRKDNDV----LVEE 735
Cdd:PTZ00243 882 kENKDSKEGDADAEVAEVDAAPGGAV-----------------------DHEPPVAKQEGNAEGGDGAALDAaagrLMTR 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 736 VEPA----PVRRILKYnisewpYILVGALCAA----INGAVTPIYSLLFSQILKTFSlVDKEQQRSEIY-SMCLFFVILG 806
Cdd:PTZ00243 939 EEKAsgsvPWSTYVAY------LRFCGGLHAAgfvlATFAVTELVTVSSGVWLSMWS-TRSFKLSAATYlYVYLGIVLLG 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 807 CVSLFTQFLQGYNFAKSGellTKRLRKFGFKAMLRQDIGWFDdlkNNP-GVLTTRLATDASQVQGATGSQVGMMVNSFTN 885
Cdd:PTZ00243 1012 TFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFD---TTPlGRILNRFSRDIDILDNTLPMSYLYLLQCLFS 1085
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 886 IFVAVLIAFlFNWKLSLVIsvffpfLALSGAVQTKMLTGFASQDKEI-----LEKAGQIT--NEALSNIRTVAGIG---- 954
Cdd:PTZ00243 1086 ICSSILVTS-ASQPFVLVA------LVPCGYLYYRLMQFYNSANREIrriksVAKSPVFTllEEALQGSATITAYGkahl 1158
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 955 --------------------VEGRFIkAFEVE-LEKSYKTAIRKANVYGLC-YAFSQGISFLANSAAYRyggyLIVYEDL 1012
Cdd:PTZ00243 1159 vmqealrrldvvyscsylenVANRWL-GVRVEfLSNIVVTVIALIGVIGTMlRATSQEIGLVSLSLTMA----MQTTATL 1233
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1013 NfsYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAAR-FFQLLDRKP--PIDVY--------SGAGEKWDNFQ-GKIDF 1080
Cdd:PTZ00243 1234 N--WLVRQVATVEADMNSVERLLYYTDEVPHEDMPELDeEVDALERRTgmAADVTgtvviepaSPTSAAPHPVQaGSLVF 1311
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1081 IDCKFTYpsRPDIQ-VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIV 1159
Cdd:PTZ00243 1312 EGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMI 1389
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQEPVLFDCSIMDNIkygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIV-RDPK 1238
Cdd:PTZ00243 1390 PQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSG 1466
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1239 ILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKL-MDQKGAYYKLVITG 1317
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEAL 1546
|
...
gi 1390249242 1318 API 1320
Cdd:PTZ00243 1547 GRS 1549
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1078-1303 |
1.83e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEP--VLFDCSIMDNIKYGDNTKEIS----VERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIAR 1231
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPheemKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1232 AIVRDPKILLLDEATSALDTESEKTVQLALDKARE--GRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1082-1294 |
2.10e-27 |
|
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: 111.47 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1082 DCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVnvqflRSNIGIVSQ 1161
Cdd:cd03235 4 DLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 EPVL---FDCSIMDNIKYGDNTKEISVERAIAAAKQA--QLHDFV-MSlpEKYETNVGiqgsQLSRGEKQRIAIARAIVR 1235
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKvdEALERVgLS--ELADRQIG----ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQNS-DIIAVMSQGVV 1294
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
420-646 |
2.32e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.08 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRdQIG 499
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENIRL-----GREEATMEDIVQAAKDA-----NAYNFIMALP---QQfdtlvgegggqmsggqkq 565
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfarlyGLPRKEARERIDELLELfgltdAADRKVGTLSggmKQ------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 566 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEEL 643
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDEL 218
|
...
gi 1390249242 644 LER 646
Cdd:COG1131 219 KAR 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
129-377 |
3.84e-27 |
|
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: 112.96 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 129 CGLVDINSEVIKFSGIYAGVGVAVLILGYFqIRLWVIT--GARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDI 206
Cdd:cd18575 25 QGFAAGNTALLNRAFLLLLAVALVLALASA-LRFYLVSwlGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 207 NKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLS 286
Cdd:cd18575 104 TLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 287 SIRTVAAFGGENKEVERY----EKNLMFAQRWGIWKgmvmGFFTGYMWCLIFFCYALAFWYGSRLVLdEGEYTPGTLIQI 362
Cdd:cd18575 184 AIKTVQAFTREDAERQRFatavEAAFAAALRRIRAR----ALLTALVIFLVFGAIVFVLWLGAHDVL-AGRMSAGELSQF 258
|
250
....*....|....*
gi 1390249242 363 FLCVIIAAMNIGNAS 377
Cdd:cd18575 259 VFYAVLAAGSVGALS 273
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
420-647 |
4.26e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.39 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEP---VLFSTT---IA---ENIRLGREEatMEDIV-QAAKDANAYNFIMALPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:PRK13632 87 IIFQNPdnqFIGATVeddIAfglENKKVPPKK--MKDIIdDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
110-364 |
5.80e-27 |
|
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: 112.40 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 110 NTIVwINSSFNQNMTNGTSCGLVDINSEVikFSGIYAGvgvavlilgyfqirLWVITGARQIRKMRKFYFRRIMRMEIGW 189
Cdd:cd18784 24 DGIV-IEKSQDKFSRAIIIMGLLAIASSV--AAGIRGG--------------LFTLAMARLNIRIRNLLFRSIVSQEIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 190 FDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTEL 269
Cdd:cd18784 87 FDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 270 ELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLMFAQRWGIWKGMVMGfftGYMWCLIFFCYALA---FWYGSR 346
Cdd:cd18784 167 VQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG---GYVWSNELTELALTvstLYYGGH 243
|
250
....*....|....*...
gi 1390249242 347 LVLdEGEYTPGTLIQIFL 364
Cdd:cd18784 244 LVI-TGQISGGNLISFIL 260
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
148-371 |
6.14e-27 |
|
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: 112.52 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 148 VGVAVL--ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLS 225
Cdd:cd18552 46 IGLFLLrgLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERY- 304
Cdd:cd18552 126 TVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFr 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 305 ---EKNLMFAQRWGIWKGM---VMGFFTGymwclifFCYALAFWYGSRLVLDeGEYTPGTLIqiflcVIIAAM 371
Cdd:cd18552 206 kanERLRRLSMKIARARALsspLMELLGA-------IAIALVLWYGGYQVIS-GELTPGEFI-----SFITAL 265
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1078-1299 |
7.63e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.36 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYP-SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERfydPDQGTVMIDGHDSKKVNVQFLR 1153
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1154 S---NIGIVSQEpvlFDC----SIMDNIKY-----GDNTKEIsveraiaAAKQAQLHDFVmSLPEKYETnvgiQGSQLSR 1221
Cdd:PRK11153 79 KarrQIGMIFQH---FNLlssrTVFDNVALplelaGTPKAEI-------KARVTELLELV-GLSDKADR----YPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1222 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVqLALDKA--RE-GRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEK 1297
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSI-LELLKDinRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQ 222
|
..
gi 1390249242 1298 GT 1299
Cdd:PRK11153 223 GT 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1096-1306 |
9.26e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.90 E-value: 9.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD----SKKVNVQfLRSNIGIVSQEPvlfdcsim 1171
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglSGRELRP-LRRRMQMVFQDP-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1172 dnikYGD-NTKeISVERAIAA-------AKQAQLHDFVMSLPEKyetnVGIQGSQLSR-------GEKQRIAIARAIVRD 1236
Cdd:COG4608 105 ----YASlNPR-MTVGDIIAEplrihglASKAERRERVAELLEL----VGLRPEHADRyphefsgGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1237 PKILLLDEATSALDteseKTVQ-----LALD-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:COG4608 176 PKLIVCDEPVSALD----VSIQaqvlnLLEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
420-644 |
1.24e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.48 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD-- 496
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 -QIGIVEQEPVLFST-TIAENIRL-----GREEATMEDIVQ--------AAKdANAYnfimalP-------QQfdtlvge 554
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENVALpleiaGVPKAEIRKRVAellelvglSDK-ADAY------PsqlsggqKQ------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 555 gggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-AD---VIig 628
Cdd:COG1135 148 -----------RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRiCDrvaVL-- 214
|
250
....*....|....*.
gi 1390249242 629 fEHGTAVERGTHEELL 644
Cdd:COG1135 215 -ENGRIVEQGPVLDVF 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
420-643 |
1.36e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 110.08 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRD 496
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFS-TTIAENI---RLGREEA--------TMEDIVQAAKDANAYNFIMALPQQFDTLvgegggqmSGGQK 564
Cdd:TIGR02315 80 RIGMIFQHYNLIErLTVLENVlhgRLGYKPTwrsllgrfSEEDKERALSALERVGLADKAYQRADQL--------SGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 565 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHE 641
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPS 231
|
..
gi 1390249242 642 EL 643
Cdd:TIGR02315 232 EL 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1094-1317 |
1.57e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGTVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DCSIMDNIKYGDNTKEI--------SVERAIaaaKQAQLHDFVMSlpEKYETNVGiqgsqLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIkdkqvldeAVEKSL---KGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1239 ILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRL---STIqnSDIIAVMSQGVVIEKG-THKKLMDQKGAYYKLV 1314
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNdTKQMFMNPKHKETEDY 246
|
...
gi 1390249242 1315 ITG 1317
Cdd:PRK14239 247 ISG 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1089-1288 |
4.17e-26 |
|
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: 107.18 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFlRSNIGIVSQEPVLF-D 1167
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 CSIMDNIK-----YGDNTKEISVERAIAAakqaqlhdfvmslpekyetnVGIQG------SQLSRGEKQRIAIARAIVRD 1236
Cdd:COG4133 90 LTVRENLRfwaalYGLRADREAIDEALEA--------------------VGLAGladlpvRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1237 PKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQNSDIIAV 1288
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLaELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1085-1294 |
5.75e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVnvqflRSNIGIVSQEpV 1164
Cdd:COG1121 14 VSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVPQR-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDCSIMdnikygdntkeISVERAIAAAKQAQL----------HDFVMSLPEKyetnVGIQG------SQLSRGEKQRIA 1228
Cdd:COG1121 85 EVDWDFP-----------ITVRDVVLMGRYGRRglfrrpsradREAVDEALER----VGLEDladrpiGELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTI-QNSDIIAVMSQGVV 1294
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1093-1303 |
6.86e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.05 E-value: 6.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN---VQFLRSNIGIVSQEPVlfdCS 1169
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNPY---GS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGD--------NTKEISVERaiaAAKQAQLHDFVMSLPEKYetnvGIQGSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK11308 105 LNPRKKVGQileeplliNTSLSAAER---REKALAMMAKVGLRPEHY----DRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1242 LDEATSALDTESEKTV-QLALDKAREGRTCIV-IAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK11308 178 ADEPVSALDVSVQAQVlNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1095-1298 |
1.94e-25 |
|
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: 105.80 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkVN-VQFLRSNIGIVSQEPVLF-DCSIMD 1172
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD---VTdLPPKDRDIAMVFQNYALYpHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYG----DNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:cd03301 92 NIAFGlklrKVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1249 LDTESEKTVQLALDK--AREGRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03301 161 LDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1088-1298 |
2.06e-25 |
|
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: 105.91 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1088 PSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFD 1167
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 -CSIMDNIKY-GDntkeisveraIAAAKQAQLHDFVMSLPEKYETN--VGIQGSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:cd03266 92 rLTARENLEYfAG----------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1244 EATSALDTESEKTVQLALDKAREGRTCIVIA-HRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1081-1275 |
2.09e-25 |
|
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: 105.42 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1081 IDCKFTYPSRPDIqvLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsKKVNVQFLRSNIGIVS 1160
Cdd:cd03226 3 ENISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1161 QEP--VLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPK 1238
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390249242 1239 ILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAH 1275
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVgELIRELAAQGKAVIVITH 184
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
420-632 |
2.50e-25 |
|
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: 105.30 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI--RSLNIRWLRDQ 497
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFS-TTIAENIRLG--------REEAT---ME--DIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggq 563
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkgmsKAEAEeraLEllEKVGLADKADAYPAQLSGGQQ---------------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 564 kQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRS-ADVIIGFEHG 632
Cdd:cd03262 142 -QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
420-627 |
3.75e-25 |
|
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: 103.63 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIG 499
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENIRL--GreeatMedivqaakdanaynfimalpQQfdtlvgegggqmsggqkqRVAIARALIRK 576
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKLsgG-----M--------------------KQ------------------RLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVII 627
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVA 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1093-1306 |
4.00e-25 |
|
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: 111.31 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFyDPDQGTVMIDGHD----SKKVNvQFLRSNIGIVSQEPvlfdc 1168
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldglSRRAL-RPLRRRMQVVFQDP----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 simdnikYGDNTKEISVERAIA--------AAKQAQLHDFVMSLPEKyetnVGIQGSQLSR-------GEKQRIAIARAI 1233
Cdd:COG4172 372 -------FGSLSPRMTVGQIIAeglrvhgpGLSAAERRARVAEALEE----VGLDPAARHRyphefsgGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1234 VRDPKILLLDEATSALDteseKTVQ---LALDK---AREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:COG4172 441 ILEPKLLVLDEPTSALD----VSVQaqiLDLLRdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1085-1303 |
4.35e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.72 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEP- 1163
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 -VLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEKyetnvgiQGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK13642 92 nQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1243 DEATSALDTESEKTVQLALDKAREGR--TCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
148-361 |
4.46e-25 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 106.75 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 148 VGVAVL--ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLS 225
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAK-FTELElKAYAKAGSIADEVLSSIRTVAAFGGENKEVERY 304
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPaFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 305 EK-NLMFAQRWgIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQ 361
Cdd:cd18542 205 DKeNEEYRDLN-IKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN-GEITLGELVA 260
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
421-620 |
4.74e-25 |
|
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: 104.54 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGhdirsLNIRWLRDQIGI 500
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 501 VEQEPVL---FSTTIAENIRLGRE----------EATMEDIVQAAKDANAYNFImalPQQFDTLvgegggqmSGGQKQRV 567
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYghkglfrrlsKADKAKVDEALERVGLSELA---DRQIGEL--------SGGQQQRV 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV 620
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLV 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1092-1305 |
5.55e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.17 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF-DC 1168
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYGdntkeisvERAIAAAKQAQLHDFVMSLPEKyetnVGIQG------SQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK09493 93 TALENVMFG--------PLRVRGASKEEAEKQARELLAK----VGLAErahhypSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1243 DEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN--SDIIaVMSQGVVIEKGTHKKLMD 1305
Cdd:PRK09493 161 DEPTSALDPELRHEVlKVMQDLAEEGMTMVIVTHEIGFAEKvaSRLI-FIDKGRIAEDGDPQVLIK 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
755-1012 |
8.47e-25 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 105.97 E-value: 8.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQILKTfslVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKF 834
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDD---IFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 835 GFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALS 914
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 915 GAVQTKMLTGFAsqdKEILEKAGQITN---EALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGI 991
Cdd:cd18552 156 IRRIGKRLRKIS---RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260
....*....|....*....|.
gi 1390249242 992 SFLANSAAYRYGGYLIVYEDL 1012
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGEL 253
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1099-1298 |
8.84e-25 |
|
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: 103.91 E-value: 8.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVD-PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDG---HDS-KKVNVQFLRSNIGIVSQEPVLF-DCSIMD 1172
Cdd:cd03297 15 LKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYGDNTKEISVERaIAAAKQAQLHDfVMSLPEKYEtnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:cd03297 95 NLAFGLKRKRNREDR-ISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249242 1253 SEKTVQLALDK--AREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:cd03297 166 LRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1094-1303 |
1.30e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERfydPDQGTV-----MIDGHDS---KKVNVQFLRSNIGIVSQE 1162
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIrvgdiTIDTARSlsqQKGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 PVLFDC-SIMDNIKYGDN-TKEISVERAIAAAKQaqlhdfvmsLPEKyetnVGIQGSQ------LSRGEKQRIAIARAIV 1234
Cdd:PRK11264 94 FNLFPHrTVLENIIEGPViVKGEPKEEATARARE---------LLAK----VGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 1235 RDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
136-361 |
1.63e-24 |
|
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: 105.19 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 136 SEVIKFSGIYAGVGVAVLILGYFQiRLWVITGARQI-RKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIA 214
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 215 DQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAF 294
Cdd:cd18541 116 PGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAF 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 295 GGENKEVER--------YEKNLMFAQrwgiwkgmVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIQ 361
Cdd:cd18541 196 VQEEAEIERfdklneeyVEKNLRLAR--------VDALFFPLIGLLIGLSFLIVLWYGGRLVIR-GTITLGDLVA 261
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1085-1319 |
1.75e-24 |
|
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: 111.96 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYpSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdskkvnvqflrsNIGIVSQEPV 1164
Cdd:TIGR00957 644 FTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDCSIMDNIKYGDNTKEISVERAIAAAkqAQLHDFVMsLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:TIGR00957 710 IQNDSLRENILFGKALNEKYYQQVLEAC--ALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1245 ATSALDTESEKTV---QLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLVITGAP 1319
Cdd:TIGR00957 787 PLSAVDAHVGKHIfehVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1091-1296 |
3.72e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQF------LRSNIGIVSQEPV 1164
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-----VRFrsprdaQAAGIAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LF-DCSIMDNIKYGDNTKE---ISVERAIAAAKQAqLHDFVMSLPEkyETNVGiqgsQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:COG1129 90 LVpNLSVAENIFLGREPRRgglIDWRAMRRRAREL-LARLGLDIDP--DTPVG----DLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1241 LLDEATSAL-DTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIE 1296
Cdd:COG1129 163 ILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
420-639 |
7.53e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 7.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYP-SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLR 495
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQIGIVEQE-PVLFSTTIAENIRL-----GREEATME-------DIVQAAKDANAYnfimalPQQFdtlvgegggqmSGG 562
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALplelaGTPKAEIKarvtellELVGLSDKADRY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 563 QKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-AD---VIigfEHGTAVE 636
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDrvaVI---DAGRLVE 221
|
...
gi 1390249242 637 RGT 639
Cdd:PRK11153 222 QGT 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-646 |
7.97e-24 |
|
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: 103.98 E-value: 7.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPC---EGMVTLDGHDIRSLN---IR 492
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 493 WLR-DQIGIVEQEPvlFS---------TTIAENIR----LGREEAT------MED--IVQAAKDANAYnfimalPQQFdt 550
Cdd:COG0444 82 KIRgREIQMIFQDP--MTslnpvmtvgDQIAEPLRihggLSKAEAReraielLERvgLPDPERRLDRY------PHELsg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 551 lvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVII 627
Cdd:COG0444 154 g-----------mrqRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVAEiADRVA 222
|
250
....*....|....*....
gi 1390249242 628 GFEHGTAVERGTHEELLER 646
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
421-638 |
8.74e-24 |
|
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: 99.82 E-value: 8.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGI 500
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 501 VEqepvlfsttiaenirlgreeatmedivQAAKDANAYNFIMalpQQFDTLvgegggqmsggqkqRVAIARALIRKPKIL 580
Cdd:cd03214 78 VP---------------------------QALELLGLAHLAD---RPFNELsgg--------erqRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 581 LLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERG 638
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1094-1300 |
1.05e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD---SKKVN---VQFLRSNIGIVSQE----P 1163
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSdkaIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 VLfdcSIMDN-----IKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK11124 96 HL---TVQQNlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1239 ILLLDEATSALDTE-SEKTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAV-MSQGVVIEKGTH 1300
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVEQGDA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1092-1298 |
1.43e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 99.98 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdSKKVNVQFLRSNIGIVSQEPVLFD-CSI 1170
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--KSYQKNIEALRRIGALIEAPGFYPnLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGDNTKEISVERaiaaakqaqlHDFVMSLpekyetnVGIQGS------QLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03268 90 RENLRLLARLLGIRKKR----------IDEVLDV-------VGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1245 ATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:cd03268 153 PTNGLDPDGIKELrELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1100-1321 |
1.55e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1100 SVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRS----NIGIVSQEPVLF-DCSIMDNI 1174
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 KYGDNTKEISV----ERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:PRK10070 128 AFGMELAGINAeerrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1251 --TESEKTVQLALDKAREGRTCIVIAHRL-STIQNSDIIAVMSQGVVIEKGTHKKLMDQKGA-YYKLVITGAPIS 1321
Cdd:PRK10070 197 plIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANdYVRTFFRGVDIS 271
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
420-645 |
2.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEP--VLFSTTIAENIRLGREEAT-----MEDIV-QAAKDANAYNFIMALPQQFdtlvgegggqmSGGQKQRVAIAR 571
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAvpydeMHRRVsEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH--TIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLE 645
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1093-1275 |
2.33e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 100.20 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDgHDSKKVNV------QFL---RSNIGIVSQ-- 1161
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 -------------EPVLfdcsimdnikygdntkEISVERAIAAAKQAQLHDFvMSLPEK----YETNvgiqgsqLSRGEK 1224
Cdd:COG4778 103 rviprvsaldvvaEPLL----------------ERGVDREEARARARELLAR-LNLPERlwdlPPAT-------FSGGEQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1225 QRIAIARAIVRDPKILLLDEATSALDTES-EKTVQLALDKAREGRTCIVIAH 1275
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1100-1306 |
3.30e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.83 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1100 SVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnvqFLRSNIG-----IVSQEPVLFD-CSIMDN 1173
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------LTALPPAerpvsMLFQENNLFPhLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYG--DNTKEISVERA--IAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:COG3840 92 IGLGlrPGLKLTAEQRAqvEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1250 D----TEsekTVQLALDKARE-GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:COG3840 161 DpalrQE---MLDLVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
436-672 |
3.99e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-----PCEGMVTLDGHDIRSLNIRW--LRDQIGIVEQEPVLF 508
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 STTIAENIRLG------REEATMEDIVQAA-KDANAYNFIMalpqqfDTLvGEGGGQMSGGQKQRVAIARALIRKPKILL 581
Cdd:PRK14239 99 PMSIYENVVYGlrlkgiKDKQVLDEAVEKSlKGASIWDEVK------DRL-HDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 582 LDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELlerkgvyFMlvtlqsqe 660
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM-------FM-------- 236
|
250
....*....|....
gi 1390249242 661 DNTHKETG--IKGK 672
Cdd:PRK14239 237 NPKHKETEdyISGK 250
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
172-656 |
4.02e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.17 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 172 RKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYrgwKLTLVILAVSPL 251
Cdd:PTZ00243 1031 RNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSA---SQPFVLVALVPC 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 252 IGIGAAVIGL------------SVAK---FTELE--------LKAYAKAGSIADEVLSSIRTVAAFGgenkeverYEKNL 308
Cdd:PTZ00243 1108 GYLYYRLMQFynsanreirrikSVAKspvFTLLEealqgsatITAYGKAHLVMQEALRRLDVVYSCS--------YLENV 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 309 mfAQRWgiwkgmvMGFFTGYMWCLIFFCYALAFWYGSRLVLDEGEytpgtLIQIFLCVIIAAMNIGNASSCLEIFSTGCS 388
Cdd:PTZ00243 1180 --ANRW-------LGVRVEFLSNIVVTVIALIGVIGTMLRATSQE-----IGLVSLSLTMAMQTTATLNWLVRQVATVEA 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 389 AASS---IFQTIDRQP--VMDCMSGDGYKLDR---------------------------IKGEIEFHNVTFHY-PSRPEV 435
Cdd:PTZ00243 1246 DMNSverLLYYTDEVPheDMPELDEEVDALERrtgmaadvtgtvviepasptsaaphpvQAGSLVFEGVQMRYrEGLPLV 1325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 kiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAEN 515
Cdd:PTZ00243 1326 --LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 516 IR--LgreEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRK-PKILLLDMATS----A 588
Cdd:PTZ00243 1404 VDpfL---EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATAnidpA 1480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 589 LDNESEAKVQGALNkiqhGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYF--MLVTL 656
Cdd:PTZ00243 1481 LDRQIQATVMSAFS----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFhsMVEAL 1546
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1093-1299 |
4.54e-23 |
|
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: 100.11 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD--SKKVnvqFLRSNIGIVS--QEPVLF-D 1167
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitGLPP---HRIARLGIARtfQNPRLFpE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 CSIMDNI------KYGDNTKEISVERAIAAAKQAQLHDFVMSLPEKyetnVGIQG------SQLSRGEKQRIAIARAIVR 1235
Cdd:COG0411 94 LTVLENVlvaahaRLGRGLLAALLRLPRARREEREARERAEELLER----VGLADradepaGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1236 DPKILLLDEATSAL-DTESEKTVQLALD-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:COG0411 170 EPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
420-615 |
4.91e-23 |
|
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: 99.43 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN----IRWL 494
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 RDQIGIVEQ-EPVLFSTTIAENIRLGREEATMEDIVQAAKD----------ANAYnfimalP-------QQfdtlvgegg 556
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALENVMLPLELAGRRDARARARAllervglghrLDHY------PaqlsggeQQ--------- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQG---ALNKiQHGHTIISVAH 615
Cdd:COG4181 154 ---------RVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNR-ERGTTLVLVTH 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
420-632 |
5.16e-23 |
|
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: 98.63 E-value: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRD 496
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFST-TIAENIRLGRE--EATMEDIVQAAKDANAynfIMALPQQFDTLvgegGGQMSGGQKQRVAIARAL 573
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHG 632
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERG 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
420-645 |
5.19e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlnirwLRDQIG 499
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVL---FSTTIAENIRLGR--------------EEATME--DIVQAAKDANaynfimalpQQFDTLvgegggqms 560
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMGRygrrglfrrpsradREAVDEalERVGLEDLAD---------RPIGELsgg------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 561 ggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVII-----GFEHGT 633
Cdd:COG1121 144 --qqqRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLllnrgLVAHGP 221
|
250
....*....|..
gi 1390249242 634 AVERGTHEELLE 645
Cdd:COG1121 222 PEEVLTPENLSR 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
438-646 |
5.46e-23 |
|
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: 99.33 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRDQIGIVEQEPVLF-STTIAENI 516
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 517 RLG---REEATMED---IVQAAKDANaynfimalpqqFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALD 590
Cdd:cd03299 93 AYGlkkRKVDKKEIerkVLEIAEMLG-----------IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 591 NESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEELLER 646
Cdd:cd03299 162 VRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1307 |
6.59e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.20 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEP--VLFDCSIMDNIKYGDNTKEIS----VERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIAR 1231
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1232 AIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
146-393 |
8.13e-23 |
|
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: 100.20 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 146 AGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLS 225
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYE 305
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 306 KNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVlDEGEYTPGTLIQIFLCVIIAAMNIGNASSCLEIFST 385
Cdd:cd18551 203 EAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARV-ASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQK 281
|
....*...
gi 1390249242 386 GCSAASSI 393
Cdd:cd18551 282 ALGALERI 289
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
420-646 |
1.08e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEP--VLFSTTIAENIRLGRE------EATMEDIVQAAKDANAYNFIMALPQQFdtlvgegggqmSGGQKQRVAIAR 571
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLER 646
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1089-1304 |
1.11e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.14 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFL---------------- 1152
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhirmifqdpntsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1153 -RSNIGIVSQEPVLFdcsimdnikygdNTKEISVERA---IAAAKQAQLhdfvmsLPEkyETNVGIQgsQLSRGEKQRIA 1228
Cdd:COG4167 102 pRLNIGQILEEPLRL------------NTDLTAEEREeriFATLRLVGL------LPE--HANFYPH--MLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTeSEKT--VQLALD-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLM 1304
Cdd:COG4167 160 LARALILQPKIIIADEALAALDM-SVRSqiINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1083-1306 |
1.22e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.31 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1083 CKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMI---------------DGHDSKKV 1147
Cdd:PRK13631 29 CVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheliTNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1148 -NVQFLRSNIGIVSQEP--VLFDCSIMDNIKYGDNTKEISVERAiaaAKQAQLHDFVMSLPEKYetnVGIQGSQLSRGEK 1224
Cdd:PRK13631 109 kNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEA---KKLAKFYLNKMGLDDSY---LERSPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1225 QRIAIARAIVRDPKILLLDEATSALDTESEK-TVQLALDKAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGT-HK 1301
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTpYE 262
|
....*
gi 1390249242 1302 KLMDQ 1306
Cdd:PRK13631 263 IFTDQ 267
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1095-1256 |
1.63e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNI 1174
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 KYGDNTKEISVERAIAAAKQAQLhdfvmSLPEK-YETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDtES 1253
Cdd:PRK10247 102 IFPWQIRNQQPDPAIFLDDLERF-----ALPDTiLTKNI----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALD-ES 171
|
...
gi 1390249242 1254 EKT 1256
Cdd:PRK10247 172 NKH 174
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1094-1296 |
2.02e-22 |
|
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: 98.34 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN----------VQFL----------R 1153
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqrrafrrdVQLVfqdspsavnpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1154 SNIGIVSQEPvlfdcsiMDNIKYGDNTKEIsvERAIAAAKQAQLHDFVMS-LPEkyetnvgiqgsQLSRGEKQRIAIARA 1232
Cdd:TIGR02769 105 MTVRQIIGEP-------LRHLTSLDESEQK--ARIAELLDMVGLRSEDADkLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1233 IVRDPKILLLDEATSALDTESEKTV--QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIE 1296
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVIleLLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1078-1298 |
2.03e-22 |
|
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: 97.85 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQG-TVMIDGHDSKKVNVQFLRSNI 1156
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1157 GIVSQEpvlfdcsIMDNIkygdnTKEISVERAIAAAKQAqlhdfVMSLPEKYETN-----------VGIQG------SQL 1219
Cdd:COG1119 81 GLVSPA-------LQLRF-----PRDETVLDVVLSGFFD-----SIGLYREPTDEqrerarellelLGLAHladrpfGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1220 SRGEKQRIAIARAIVRDPKILLLDEATSALDTES-EKTVQLaLDK-AREGRTCIV-IAHRLstiqnSDIIAVMSQGVVIE 1296
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLAL-LDKlAAEGAPTLVlVTHHV-----EEIPPGITHVLLLK 217
|
..
gi 1390249242 1297 KG 1298
Cdd:COG1119 218 DG 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1092-1298 |
2.15e-22 |
|
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: 96.58 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHdskkvNVQFL-RSNIGIVSQEPVLF-DCS 1169
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----PLDIAaRNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGDNTKEISVEraiAAAKQAQ--LHDFvmSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:cd03269 87 VIDQLVYLAQLKGLKKE---EARRRIDewLERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1248 ALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:cd03269 158 GLDPVNVELLkDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
420-646 |
2.17e-22 |
|
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: 102.84 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSR--------PEVKILNNLSMVIKPGETTAFVGSSGAGKST----ALQLIqrfydPCEGMVTLDGHDIR 487
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 488 SLN---IRWLRDQIGIVEQEPvlFST---------TIAENIRL---GREEATMEDIVQAA--------KDANAYnfimal 544
Cdd:COG4172 351 GLSrraLRPLRRRMQVVFQDP--FGSlsprmtvgqIIAEGLRVhgpGLSAAERRARVAEAleevgldpAARHRY------ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 545 PQQFdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS 622
Cdd:COG4172 423 PHEFsgg-----------qrqRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQreHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 1390249242 623 -ADVIIGFEHGTAVERGTHEELLER 646
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1096-1277 |
2.31e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGTVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFDC 1168
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYG-------DNTKEIsVERAIaaaKQAQLHDFVmslPEKYETNvgiqGSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK14243 106 SIYDNIAYGaringykGDMDEL-VERSL---RQAALWDEV---KDKLKQS----GLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1390249242 1242 LDEATSALDTESEKTVQLALDKAREGRTCIVIAHRL 1277
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1080-1319 |
2.40e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1080 FIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIV 1159
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQEPVL-FDCSIMDNIKYG-----------DNTKEISVERAIAAAKQAQLHDFVMslpekyetnvgiqgSQLSRGEKQRI 1227
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPV--------------TSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALDTESE-KTVQLALDKAREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKG------T 1299
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGppadvlT 228
|
250 260
....*....|....*....|....
gi 1390249242 1300 HKKLMDQKGAyYKLV----ITGAP 1319
Cdd:PRK09536 229 ADTLRAAFDA-RTAVgtdpATGAP 251
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1085-1298 |
2.89e-22 |
|
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: 96.49 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRpdiQVLNGLSVSVDPGQTlAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKvNVQFLRSNIGIVSQepv 1164
Cdd:cd03264 8 KRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 lfDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMS---LPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:cd03264 80 --EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLElvnLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1242 LDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQNS-DIIAVMSQGVVIEKG 1298
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
420-646 |
3.62e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIR--SLNIRWLRDQ 497
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFSTTIA-ENIRLG--------REEA-----TMEDIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggq 563
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGplrvrgasKEEAekqarELLAKVGLAERAHHYPSELSGGQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 564 kQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHE 641
Cdd:PRK09493 143 -QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQ 221
|
....*
gi 1390249242 642 ELLER 646
Cdd:PRK09493 222 VLIKN 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1075-1303 |
3.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.29 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1075 QGKIDFIDCKFTYPsrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGTVMIDGHDSKKVNV 1149
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1150 QFLRSNIGIVSQEP-VLFDCSIMDNIKYG-------DNTKEISvERAIAAAKQAQLHDFVmslpekyETNVGIQGSQLSR 1221
Cdd:PRK14247 78 IELRRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKELQ-ERVRWALEKAQLWDEV-------KDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1222 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKGTH 1300
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPT 229
|
...
gi 1390249242 1301 KKL 1303
Cdd:PRK14247 230 REV 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1090-1281 |
3.78e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVL-NGLSVSVDPGQTLAFVGSSGCGKST--------------SIQLlerfydPDQGTVMidghdskkvnvqFLrs 1154
Cdd:COG4178 372 TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTllraiaglwpygsgRIAR------PAGARVL------------FL-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 nigivSQEPVLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEkyETNvgiQGSQLSRGEKQRIAIARAIV 1234
Cdd:COG4178 432 -----PQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDE--EAD---WDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1390249242 1235 RDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQ 1281
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
420-646 |
4.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEvKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDP---CEGMVTLDGHDIRSLNIRWLRD 496
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEP--VLFSTTIAENIRLGRE-----EATMEDIV-QAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVA 568
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLEnravpRPEMIKIVrDVLADVGMLDYIDSEPANLS-----------GGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLER 646
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
420-646 |
4.33e-22 |
|
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: 96.54 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIrsLNIRWLRDQIG 499
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLG------------REEATMEDIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggqkQR 566
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklpkaeikERVAEALDLVQLEGYANRKPSQLSGGQQ-----------------QR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 567 VAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEEL 643
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
...
gi 1390249242 644 LER 646
Cdd:cd03300 219 YEE 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1095-1306 |
4.43e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.41 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCSIMDN 1173
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYGDNTKEISVERAIAAAKQA-QLHDFVmSLPEKYEtnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlELVDLA-GFEDRYV-------DQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1253 SEKTVQlalDKARE-----GRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:PRK11432 171 LRRSMR---EKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1099-1299 |
5.41e-22 |
|
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: 95.64 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCSIMDNIKYG 1177
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1178 DNT----KEISVERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD-TE 1252
Cdd:cd03298 95 LSPglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDpAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1390249242 1253 SEKTVQLALDKARE-GRTCIVIAHrlstiQNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03298 164 RAEMLDLVLDLHAEtKMTVLMVTH-----QPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1092-1303 |
5.87e-22 |
|
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: 95.90 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD----SKKVnvqflRSNIGIVSQEPVLfd 1167
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvrePREV-----RRRIGIVFQDLSV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 csimDNIKYGDNTKEI-----SVERAIAAAKQAQLHDFvMSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:cd03265 85 ----DDELTGWENLYIharlyGVPGAERRERIDELLDF-VGLLEAADRLV----KTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1243 DEATSALDTESEKTVQLALDK--AREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1078-1298 |
5.98e-22 |
|
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: 94.93 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDI---QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGTVMIDGHDSKKVNvqfL 1152
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1153 RSNIGIVSQEPVLFDCsimdnikygdntkeISVERAIAAAkqAQLhdfvmslpekyetnvgiqgSQLSRGEKQRIAIARA 1232
Cdd:cd03213 81 RKIIGYVPQDDILHPT--------------LTVRETLMFA--AKL-------------------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1233 IVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLST--IQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1077-1307 |
5.99e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.54 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1077 KIDFIDCKFTY-PSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDG----HDSKKVNVQ 1150
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1151 FLRSNIGIVSQ--EPVLFDCSIMDNIKYGDNTKEISVERAIAAAkqaqlHDFVMSLpeKYETNVGIQGS-QLSRGEKQRI 1227
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAR--EGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKLM 1304
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 1390249242 1305 DQK 1307
Cdd:PRK13646 235 KDK 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1096-1299 |
6.14e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.43 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD--SKKVNVQFLRSNIGIVSQEP--VLFDCSIM 1171
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1172 DNIKYGD-----NTKEISvERAIAAAKQAQLhdfvmslpeKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK13637 103 KDIAFGPinlglSEEEIE-NRVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1247 SALDTeseKTVQLALDKARE-----GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:PRK13637 173 AGLDP---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
420-642 |
8.79e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHY-PSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI--RSLNIRWLR 495
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQIGIVEQEP--VLFSTTIAENI-----RLGREEATMEDIVQAAKDanaynfIMALPqqFDTLVGEGGGQMSGGQKQRVA 568
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIafgpiNLGLSEEEIENRVKRAMN------IVGLD--YEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVqgaLNKIQHGH-----TIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEE 642
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEI---LNKIKELHkeynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1085-1305 |
1.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRpdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPdQGTVMIDGH--------DSKKVNVQFLRSNI 1156
Cdd:PRK14258 15 FYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRveffnqniYERRVNLNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1157 GIVSQEPVLFDCSIMDNIKYGDNT----KEISVERAIAAA-KQAQLHDFVMSLPEKyetnvgiQGSQLSRGEKQRIAIAR 1231
Cdd:PRK14258 91 SMVHPKPNLFPMSVYDNVAYGVKIvgwrPKLEIDDIVESAlKDADLWDEIKHKIHK-------SALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1232 AIVRDPKILLLDEATSALDTESEKTVQLALD--KAREGRTCIVIAHRLSTIQN-SDIIAVMSQ-----GVVIEKGTHKKL 1303
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKI 243
|
..
gi 1390249242 1304 MD 1305
Cdd:PRK14258 244 FN 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1305 |
1.65e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDIqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPV-LFDCSIMD-NIKYGDNTKEISVERAIAAAKQAqLHDFVMSLPEKYETNvgiqgsQLSRGEKQRIAIARAIVR 1235
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDKAREGR--TCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1082-1307 |
1.70e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1082 DCKFTYPSrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFL--RSNIGIV 1159
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQEP--VLFDCSIMDNIKYGD---NTKEISVERAIAAAKQAqlhdfvmslpekyetnVGIQGSQ------LSRGEKQRIA 1228
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPlnlGLSKEEVEKRVKEALKA----------------VGMEGFEnkpphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTE-SEKTVQLALDKAREGRTCIVIAHRLSTIQ-NSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSD 227
|
.
gi 1390249242 1307 K 1307
Cdd:PRK13639 228 I 228
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
758-1007 |
1.75e-21 |
|
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: 96.43 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 758 GALCAAINGAVTPIYSLLFSQILKTFSL--VDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFG 835
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKesGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 836 FKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSG 915
Cdd:cd18573 81 FKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 916 AVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLA 995
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250
....*....|..
gi 1390249242 996 NSAAYRYGGYLI 1007
Cdd:cd18573 239 LLSVLYYGGSLV 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
438-645 |
1.76e-21 |
|
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: 95.79 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL----RDQIGIVEQEPVLF-STTI 512
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 513 AENIRLG----------REEATMEDIVQAAKDANAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKI 579
Cdd:cd03294 120 LENVAFGlevqgvpraeREERAAEALELVGLEGWEHKYPDELSggmQQ------------------RVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELLE 645
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
795-1314 |
1.76e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.98 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 795 IYSMCLFFVILGCVSLFTQFLQgyNFAKSGelltKRLRKFGFKAMLRQDIGWFDDLKNN--PGVLTTRLATDASQVQGAT 872
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQ--NVGRVG----FRLRSTLVAAIFHKSLRLTHEARKNfaSGKVTNMITTDANALQQIA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 873 GSQVGMMVNSFTNIFVAVL------IAFLFNwklSLVISVFFPFLALSGAVQTKMLT-GFASQDKEIlekagQITNEALS 945
Cdd:PLN03232 416 EQLHGLWSAPFRIIVSMVLlyqqlgVASLFG---SLILFLLIPLQTLIVRKMRKLTKeGLQWTDKRV-----GIINEILA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 946 NIRTVAGIGVEgrfiKAFEVELEKSYKTAI---RKANvygLCYAFSqgiSFLANS-----AAYRYGGYLIVYEDLNFSYV 1017
Cdd:PLN03232 488 SMDTVKCYAWE----KSFESRIQGIRNEELswfRKAQ---LLSAFN---SFILNSipvvvTLVSFGVFVLLGGDLTPARA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1018 FRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQL-------LDRKPPIDVYSGAgekwdnfqgkIDFIDCKFTYPSR 1090
Cdd:PLN03232 558 FTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNPPLQPGAPA----------ISIKNGYFSWDSK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQ-LLERFYDPDQGTVMIdghdskkvnvqflRSNIGIVSQEPVLFDCS 1169
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSVAYVPQVSWIFNAT 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGDNTKEISVERAIAAAkqAQLHDFVMsLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PLN03232 695 VRENILFGSDFESERYWRAIDVT--ALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1250 DTESEKTV-QLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLV 1314
Cdd:PLN03232 772 DAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1093-1296 |
2.00e-21 |
|
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: 94.42 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGTVMIDGHDSKKVN----VQFLRSNIGIVSQE--- 1162
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 -PVLfdcSIMDNIkygdntkEISVERAIA--AAKQAQlhdfvmSLPEKyetnVGIQG------SQLSRGEKQRIAIARAI 1233
Cdd:COG4181 102 lPTL---TALENV-------MLPLELAGRrdARARAR------ALLER----VGLGHrldhypAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1234 VRDPKILLLDEATSALDTE-SEKTVQLALDKARE-GRTCIVIAHRLSTIQNSDIIAVMSQGVVIE 1296
Cdd:COG4181 162 ATEPAILFADEPTGNLDAAtGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
420-644 |
2.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.93 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEP--VLFSTTIAENIRLGRE------EATMEDIVQAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVAIAR 571
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEnqgiprEEMIKRVDEALLAVNMLDFKTREPARLS-----------GGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH--TIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
419-619 |
2.78e-21 |
|
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: 93.00 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTF---HYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLI--QRFYDPCEGMVTLDGHDIRslnIRW 493
Cdd:cd03213 3 TLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQEPVLFST-TIAENIRLgreeatmedivqAAKdanaynfIMALP--QQfdtlvgegggqmsggqkQRVAIA 570
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAK-------LRGLSggER-----------------KRVSIA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 571 RALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLST 619
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSS 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1094-1306 |
3.08e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD-------------SKKVNVQFLRSNIGIVS 1160
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1161 QEPVLFD-CSIMDN-----IKYGDNTKEISVERAIaaakqaqlhdfvmslpeKYETNVGIQGSQ-------LSRGEKQRI 1227
Cdd:PRK10619 99 QHFNLWShMTVLENvmeapIQVLGLSKQEARERAV-----------------KYLAKVGIDERAqgkypvhLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
.
gi 1390249242 1306 Q 1306
Cdd:PRK10619 242 N 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
420-646 |
3.98e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.08 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYP--SRPEVKilnNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ 497
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEP--VLFSTTIA-------ENIRLGREEatMEDIVQAA-KDANAYNFIMALPQQFdtlvgegggqmSGGQKQRV 567
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQddvafglENIGVPREE--MVERVDQAlRQVGMEDFLNREPHRL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLE 645
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
.
gi 1390249242 646 R 646
Cdd:PRK13635 230 S 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
420-646 |
4.35e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.67 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEvkilnNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIrwlrDQ-- 497
Cdd:COG3840 2 LRLDDLTYRYGDFPL-----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFS-TTIAENIRLGRE------EATMEDIVQAAKDANAYNFIMALP-------QQfdtlvgegggqmsggq 563
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIGLGLRpglkltAEQRAQVEQALERVGLAGLLDRLPgqlsggqRQ---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 564 kqRVAIARALIRKPKILLLDMATSALD----NESEAKVQgALNKiQHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERG 638
Cdd:COG3840 137 --RVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVD-ELCR-ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
....*...
gi 1390249242 639 THEELLER 646
Cdd:COG3840 213 PTAALLDG 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1110-1253 |
5.38e-21 |
|
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: 96.32 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1110 AFVGSSGCGKSTSIQL---LERfydPDQGTVMIDGH---DSKKVnvQFL---RSNIGIVSQEPVLFD-CSIMDNIKYGdn 1179
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPhLSVRGNLLYG-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1180 tkeisVERAIAAAKQAQLHDfVMSLpekyetnVGIQG------SQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:COG4148 102 -----RKRAPRAERRISFDE-VVEL-------LGIGHlldrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
420-644 |
5.45e-21 |
|
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: 94.00 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGM-VTLDGHDIRSLNIRWLRDQI 498
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVeqepvlfSTTIAENIR----------------LGR-EEATMEDIVQAAKdanaynfIMAL-------PQQFDTLvge 554
Cdd:COG1119 81 GLV-------SPALQLRFPrdetvldvvlsgffdsIGLyREPTDEQRERARE-------LLELlglahlaDRPFGTL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 555 gggqmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLStvrsaDVIIGFEH- 631
Cdd:COG1119 144 -----SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE-----EIPPGITHv 213
|
250
....*....|....*...
gi 1390249242 632 -----GTAVERGTHEELL 644
Cdd:COG1119 214 lllkdGRVVAAGPKEEVL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1094-1299 |
5.46e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-DCSIMD 1172
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYGdntkeISV----ERAIAAA---KQAQLHDFVM--SLPEKYEtnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:PRK10851 94 NIAFG-----LTVlprrERPNAAAikaKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1244 EATSALDTESEKTVQLALDKARE--GRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
419-651 |
5.81e-21 |
|
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: 93.56 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHYPSRPEvkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRDQI 498
Cdd:cd03296 2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFS-TTIAENIRLG-REEATMEDIVQAAKDANAYNFIMALpqQFDTLVGEGGGQMSGGQKQRVAIARALIRK 576
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLV--QLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELLERKGVYF 651
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1094-1292 |
6.15e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.02 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDS---KKVNVQFLRSNIGIVSQEP-VLFDCS 1169
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKY-----GDNTKEISvERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK10908 96 VYDNVAIpliiaGASGDDIR-RRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1245 ATSALDTE-SEKTVQLALDKAREGRTCIVIAHRLSTIQNSDI-IAVMSQG 1292
Cdd:PRK10908 164 PTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1307 |
7.22e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFDCS 1169
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPdnQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGDNT-----KEIS--VERAIAAAKQAQLHDfvmsLPEKYetnvgiqgsqLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK13636 100 VYQDVSFGAVNlklpeDEVRkrVDNALKRTGIEHLKD----KPTHC----------LSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1243 DEATSALDTES-EKTVQLALDKARE-GRTCIVIAHRLSTIQ-NSDIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:PRK13636 166 DEPTAGLDPMGvSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1092-1305 |
8.24e-21 |
|
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: 92.50 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLF-DCS 1169
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYGDNTKEISVERAIAaakqaqlhDFVMSL-PEKYEtNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARL--------ERVYELfPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1249 LdteSEKTVQL---ALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:cd03224 163 L---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
420-626 |
9.70e-21 |
|
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: 91.77 E-value: 9.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWlRDQIG 499
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENI----RLGREEATMEDIVQAAKdanaynfIMALPQQFDTLVGEgggqmsggqkqRVAIARALI 574
Cdd:COG4133 79 YLGHADGLKPElTVRENLrfwaALYGLRADREAIDEALE-------AVGLAGLADLPVRQlsag----qkrRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 575 RKPKILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTVRSADVI 626
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-632 |
1.06e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-----PCEGMVTLDGHDI--RSLNIR 492
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 493 WLRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIVQAA-KDANAYNfimalpqQFDTLVGEGGGQMSGGQKQ 565
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWD-------EIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 566 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALN--KIQHGHTIISVAHRLSTVRSADVIIGFEHG 632
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
420-633 |
1.19e-20 |
|
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: 91.38 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEV--KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHdirslnirwlrdq 497
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFSTTIAENIRLGRE--EATMEDIVQAA---KDanaynfIMALPQQFDTLVGEGGGQMSGGQKQRVAIARA 572
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACalePD------LEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 573 LIRKPKILLLDMATSALDNESEAK-----VQGALnkiQHGHTIISVAHRLSTVRSADVIIGFEHGT 633
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHifencILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1078-1301 |
1.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDIQ--VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDG----HDSKKVNVQF 1151
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQ--EPVLFDCSIMDNIKYGDNTKEISVERAIAAAKqaqlhdfvmslpEKYETnVGIQGS-------QLSRG 1222
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAR------------EKLAL-VGISESlfeknpfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1223 EKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKARE-GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTH 1300
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
.
gi 1390249242 1301 K 1301
Cdd:PRK13649 230 K 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
419-646 |
1.59e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.83 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlnirWL--RD 496
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLppRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 -QIGIVEQEPVLF-STTIAENI-------RLGREEA---TME--DIVQAAKDANAYnfimalP-------QQfdtlvgeg 555
Cdd:COG1118 75 rRVGFVFQHYALFpHMTVAENIafglrvrPPSKAEIrarVEEllELVQLEGLADRY------PsqlsggqRQ-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmsggqkqRVAIARALIRKPKILLLDMATSALDneseAKVQGALNKI-------QHGHTIIsVAH------RLstvrs 622
Cdd:COG1118 141 ----------RVALARALAVEPEVLLLDEPFGALD----AKVRKELRRWlrrlhdeLGGTTVF-VTHdqeealEL----- 200
|
250 260
....*....|....*....|....
gi 1390249242 623 ADVIIGFEHGTAVERGTHEELLER 646
Cdd:COG1118 201 ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1098-1266 |
1.65e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.39 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1098 GLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLFD-CSIMDN 1173
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYG---DNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:COG4136 97 LAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170
....*....|....*..
gi 1390249242 1251 TESEKTV-QLALDKARE 1266
Cdd:COG4136 166 AALRAQFrEFVFEQIRQ 182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1099-1298 |
1.92e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.90 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNvQFLRSnIGIVSQEPVLF-DCSIMDNIKYG 1177
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1178 dnTKEISVERAIAAAKQAQLHDFV-MSLPEKYETNvgiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKT 1256
Cdd:PRK11607 116 --LKQDKLPKAEIASRVNEMLGLVhMQEFAKRKPH------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390249242 1257 VQLALDK--AREGRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:PRK11607 188 MQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
756-1050 |
2.24e-20 |
|
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: 93.26 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 756 LVGALCAAINGAVTPIYSLLFSQIlktfslVDK---EQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLR 832
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRI------IDSvigGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 833 KFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLA 912
Cdd:cd18542 76 NDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 913 LSGAVQTKMLtgfASQDKEILEKAGQITN---EALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQ 989
Cdd:cd18542 154 LFSYVFFKKV---RPAFEEIREQEGELNTvlqENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 990 GISFLANSAAYRYGGYLIVYEDLNF-------SYVFRVVSSIAMsataVGRTFSytpSYAKAKISAAR 1050
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLVINGEITLgelvafiSYLWMLIWPVRQ----LGRLIN---DMSRASASAER 291
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1090-1296 |
2.46e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN----------VQFL------- 1152
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1153 ---RSNIGIVSQEPV--LFDCSimdnikygdntKEISVERAIAAAKQAQLHDFVMS-LPEkyetnvgiqgsQLSRGEKQR 1226
Cdd:PRK10419 102 vnpRKTVREIIREPLrhLLSLD-----------KAERLARASEMLRAVDLDDSVLDkRPP-----------QLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1227 IAIARAIVRDPKILLLDEATSALDT--ESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIE 1296
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLvlQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
420-626 |
2.60e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ-I 498
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFST-TIAENIRLGRE--------EATMEDivQAAKDANAYNF-------IMALP---QQFdtlvgegggqm 559
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREprrgglidWRAMRR--RARELLARLGLdidpdtpVGDLSvaqQQL----------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 560 sggqkqrVAIARALIRKPKILLLDMATSALdNESEAKVqgaLNKI-----QHGHTIISVAHRLSTVRS-ADVI 626
Cdd:COG1129 149 -------VEIARALSRDARVLILDEPTASL-TEREVER---LFRIirrlkAQGVAIIYISHRLDEVFEiADRV 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1094-1298 |
2.78e-20 |
|
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: 91.18 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGTVMIDGHDSKKVNVQFlrsNIGIVSQepvlFDCsi 1170
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQK---CVAYVRQ----DDI-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 mdnikygdNTKEISVERAIAAAKQAQLH-----------DFVMSLPEKYETNVG---IQGsqLSRGEKQRIAIARAIVRD 1236
Cdd:cd03234 92 --------LLPGLTVRETLTYTAILRLPrkssdairkkrVEDVLLRDLALTRIGgnlVKG--ISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1237 PKILLLDEATSALDTESE-KTVQLALDKAREGRTCIVIAH--RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:cd03234 162 PKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1078-1307 |
3.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTY-PSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH----DSKKVNVQF 1151
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQ--EPVLFDCSIMDNIKYGDN----TKEISVERAIAAAKQAQLHDFVMSlPEKYEtnvgiqgsqLSRGEKQ 1225
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgfSEDEAKEKALKWLKKVGLSEDLIS-KSPFE---------LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
....
gi 1390249242 1304 MDQK 1307
Cdd:PRK13641 233 FSDK 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
436-641 |
3.49e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAEN 515
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 516 IRLG---REEATMEDIVQAAKDAnaynfiMALPqqfDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNE 592
Cdd:PRK10247 101 LIFPwqiRNQQPDPAIFLDDLER------FALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 593 SEAKVQGALNKI--QHGHTIISVAHRLSTVRSADVIIGFE-HGTAVERGTHE 641
Cdd:PRK10247 172 NKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
420-647 |
3.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.11 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEP--VLFSTTIAE-------NIRLGREEatMEDIVQAAKDA-NAYNFIMALPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDdvafgpvNMGLDKDE--VERRVEEALKAvRMWDFRDKPPYHL-----------SYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1092-1303 |
4.03e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERF---YDPD---QGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 1165
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1166 F-DCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDfvMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK14246 102 FpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1245 ATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1087-1275 |
5.63e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1087 YPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdskkVNVQFLRSNIGIVSQEPVLF 1166
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DC-SIMDNIKYGDNTKEISVERAIAAAKQAQlhdfvmslpekyeTNVGIQGS------QLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK11248 83 PWrNVQDNVAFGLQLAGVEKMQRLEIAHQML-------------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390249242 1240 LLLDEATSALDTESEKTVQLALDK--AREGRTCIVIAH 1275
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
420-646 |
6.40e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.49 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYP--------SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN- 490
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 491 --IRWLRDQIGIVEQEPvlFS---------TTIAENIRLGR--EEATMEDIVQA--------AKDANAYnfimalPQQFd 549
Cdd:COG4608 88 reLRPLRRRMQMVFQDP--YAslnprmtvgDIIAEPLRIHGlaSKAERRERVAEllelvglrPEHADRY------PHEFs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 550 tlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVR--SADV 625
Cdd:COG4608 160 gg-----------qrqRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQdeLGLTYLFISHDLSVVRhiSDRV 228
|
250 260
....*....|....*....|.
gi 1390249242 626 IIGFeHGTAVERGTHEELLER 646
Cdd:COG4608 229 AVMY-LGKIVEIAPRDELYAR 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
420-645 |
8.56e-20 |
|
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: 89.42 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN-IRWLRDQI 498
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFST-TIAENIRLG-------REEATMEDIVQ------AAKDANAYNfimaLP---QQFdtlvgegggqmsg 561
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGayarrraKRKARLERVYElfprlkERRKQLAGT----LSggeQQM------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 562 gqkqrVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGT 639
Cdd:cd03224 141 -----LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGT 215
|
....*.
gi 1390249242 640 HEELLE 645
Cdd:cd03224 216 AAELLA 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
437-644 |
1.71e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.42 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI---RSLN-----IRWLRDQIGIVEQEPVLF 508
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 S-TTIAENIRLG--------REEATMEDIVQAAK-----DANAYNFIMALPQQfdtlvgegggqmsggqkQRVAIARALI 574
Cdd:PRK11264 98 PhRTVLENIIEGpvivkgepKEEATARARELLAKvglagKETSYPRRLSGGQQ-----------------QRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 575 RKPKILLLDMATSALDNESEAKVqgaLNKI----QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEV---LNTIrqlaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1092-1321 |
1.76e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNvqflRSNIGIVSQEPVLF-DCSI 1170
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYgdntkeisveraiaaakQAQLHDfvMS----------------LPEKYETNVgiqgSQLSRGEKQRIAIARAIV 1234
Cdd:COG4152 89 GEQLVY-----------------LARLKG--LSkaeakrradewlerlgLGDRANKKV----EELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1235 RDPKILLLDEATSALDTES-EKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQKGAYYK 1312
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTL 225
|
....*....
gi 1390249242 1313 LVITGAPIS 1321
Cdd:COG4152 226 RLEADGDAG 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1086-1275 |
2.04e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.54 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYP-SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQFLRSNIGIVSQEPV 1164
Cdd:COG4525 12 RYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFD-CSIMDNIKYGDNTKEISV--ERAIAAAKQAQlhdfvmslpekyetnVGIQG------SQLSRGEKQRIAIARAIVR 1235
Cdd:COG4525 87 LLPwLNVLDNVAFGLRLRGVPKaeRRARAEELLAL---------------VGLADfarrriWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQ-LALD-KAREGRTCIVIAH 1275
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQeLLLDvWQRTGKGVFLITH 193
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1091-1301 |
2.20e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsKKVNV----QFLRSNIGIVSQEPVLF 1166
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DC-SIMDNIKYG-DNTKEISVERAIAAAKqaqlhdfVMSLPEKY------ETNVGiqgsQLSRGEKQRIAIARAIVRDPK 1238
Cdd:COG3845 93 PNlTVAENIVLGlEPTKGGRLDRKAARAR-------IRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1239 ILLLDEATSALdTESEkTVQL--ALDK-AREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIekGTHK 1301
Cdd:COG3845 162 ILILDEPTAVL-TPQE-ADELfeILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV--GTVD 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1078-1299 |
2.55e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.86 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGTVMIDGHDSKKVNVQFLRS 1154
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQEP--VLFDCSIMDNIKYGDNTKEISVERAIA----AAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIA 1228
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTES-EKTVQLALD-KAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1094-1299 |
4.36e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.29 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FDCSIMD 1172
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYGdntkeisveRAIAAAKQAQLHDfvmsLPEKYETNVGIQG------SQLSRGEKQRIAIARAIVR------DPKIL 1240
Cdd:PRK13548 96 VVAMG---------RAPHGLSRAEDDA----LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1241 LLDEATSALD-TESEKTVQLALDKARE-GRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK13548 163 LLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1094-1299 |
4.44e-19 |
|
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: 92.44 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTS----IQLLERFYDPDQGTVMIDGHDSKKVNVQFLR----SNIGIVSQEPV- 1164
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 ----LFdcsimdnikygdntkeiSVERAIA-------AAKQAQLHDFVMSLPEKyetnVGIQGS---------QLSRGEK 1224
Cdd:COG4172 104 slnpLH-----------------TIGKQIAevlrlhrGLSGAAARARALELLER----VGIPDPerrldayphQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1225 QRIAIARAIVRDPKILLLDEATSALDTesekTVQ---LAL--D-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEK 1297
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDV----TVQaqiLDLlkDlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQ 238
|
..
gi 1390249242 1298 GT 1299
Cdd:COG4172 239 GP 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
447-638 |
4.92e-19 |
|
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: 86.97 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 447 PGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDG---HDIR-SLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLG-R 520
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGlK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 521 EEATMEDIVQAAKdanaynfIMALpQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGA 600
Cdd:cd03297 102 RKRNREDRISVDE-------LLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1390249242 601 LNKIQ---HGHTIIsVAHRLSTV-RSADVIIGFEHGTAVERG 638
Cdd:cd03297 174 LKQIKknlNIPVIF-VTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1093-1275 |
5.35e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.53 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQ---FLRS-NIGIVSQE----PV 1164
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSfmliPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LfdcSIMDNIKY-----GDNTKEiSVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK10584 103 L---NALENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390249242 1240 LLLDEATSALDTES-EKTVQLALDKARE-GRTCIVIAH 1275
Cdd:PRK10584 168 LFADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTH 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1073-1299 |
6.64e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1073 NFQGKIDFIDCKFTYPSRP--DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH----DSKK 1146
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1147 VN-VQFLRSNIGIVSQEP--VLFDCSIMDNIKYGdnTKEISVERAIAAAKQAQLHDFVmSLPEKYetnVGIQGSQLSRGE 1223
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFG--PVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1224 KQRIAIARAIVRDPKILLLDEATSALDTESEK---TVQLALDKaREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1101-1298 |
7.10e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1101 VSVD--PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH------DSKkvnVQFLRSNIGIVSQEPVlfdCSIMD 1172
Cdd:PRK10261 343 VSFDlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlsPGK---LQALRRDIQFIFQDPY---ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYGDNTKE-ISVERAI----AAAKQAQLHDFVMSLPE---KYEtnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK10261 417 RQTVGDSIMEpLRVHGLLpgkaAAARVAWLLERVGLLPEhawRYP-------HEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1245 ATSALDTE-SEKTVQLALDKARE-GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:PRK10261 490 AVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
758-1008 |
7.12e-19 |
|
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: 88.69 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 758 GALCAAINGAVTPIYSLLFSQILKTfslVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFK 837
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDA---ALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 838 AMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAV 917
Cdd:cd18576 78 HLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 918 QTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANS 997
Cdd:cd18576 156 FGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIV 235
|
250
....*....|.
gi 1390249242 998 AAYRYGGYLIV 1008
Cdd:cd18576 236 AVLWYGGRLVL 246
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1095-1307 |
7.76e-19 |
|
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: 88.37 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMDNI 1174
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 kygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1254
Cdd:cd03289 98 ---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1255 KTVQLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
418-615 |
8.80e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.36 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwLRDq 497
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLF-STTIAENI----RL-GREEATMEDIV-QAAKdanaynfIMAL-------P-------QQfdtlvgegg 556
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIafplKLrKVPKAEIDRRVrEAAE-------LLGLedlldrkPkqlsggqRQ--------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH 615
Cdd:COG3839 141 ---------RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTH 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1094-1305 |
9.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ-----GTVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 -DCSIMDNIKYG-------DNTKEISvERAIAAAKQAQLHDFVMSLPEKYETNvgiqgsqLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK14267 98 pHLTIYDNVAIGvklnglvKSKKELD-ERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1239 ILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHrlSTIQN---SDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAarvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
420-638 |
1.10e-18 |
|
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: 86.01 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEvkilnNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRDQIG 499
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLGR------EEATMEDIVQAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVAIARA 572
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLspglklTAEDRQAIEVALARVGLAGLEKRLPGELS-----------GGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 573 LIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERG 638
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1094-1298 |
1.39e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGTVMIDGHDSKKVNVQFL---RSNIGIVSQEPvlfdcsi 1170
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 mdnikYGDNTKEISVERAIAAAkqAQLHDFVMSLPEKYE------TNVGIQG-------SQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK15134 372 -----NSSLNPRLNVLQIIEEG--LRVHQPTLSAAQREQqviavmEEVGLDPetrhrypAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1238 KILLLDEATSALDteseKTVQ---LALDKAREGR---TCIVIAHRLSTIQN-SDIIAVMSQGVVIEKG 1298
Cdd:PRK15134 445 SLIILDEPTSSLD----KTVQaqiLALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
419-641 |
1.53e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGH------DIRSLNIR 492
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 493 WLRDQIGIVEQE----PVLfstTIAENI--------RLGREEATMEDI-----VQAAKDANAYNFIMALPQQfdtlvgeg 555
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMkllarLRLTDKADRFPLHLSGGQQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRS-ADVIIGFEHGT 633
Cdd:COG4161 148 ---------QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGR 218
|
....*...
gi 1390249242 634 AVERGTHE 641
Cdd:COG4161 219 IIEQGDAS 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1086-1306 |
1.61e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEP-- 1163
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 VLFDCSIMDNIKYGDNTKEISvERAIAAAKQAQLHdfvMSLPEKYETNVgiqGSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINLGLD-EETVAHRVSSALH---MLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1244 EATSALDTESEKTVQLALDKARE--GRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1078-1299 |
2.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTY-PSRP-DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTV----MIDGHDSKKVNVQF 1151
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQEP--VLFDCSIMDNIKYGDNTKEISVERAIA-AAKQAQLHDFVMSLPEKyetnvgiQGSQLSRGEKQRIA 1228
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESE-KTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-645 |
2.29e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTA----LQLIqrfydPCEGMVTLDGHDIRSLNIRWL---RDQIGIVEQEP---- 505
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 506 -----VLfsTTIAENIRL--------GREE---ATMEDIVQAAKDANAYnfimalPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:PRK15134 376 nprlnVL--QIIEEGLRVhqptlsaaQREQqviAVMEEVGLDPETRHRY------PAEF-----------SGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTI--ISVAHRLSTVRSA--DVIIgFEHGTAVERGTHEELLE 645
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALchQVIV-LRQGEVVEQGDCERVFA 515
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
420-644 |
2.33e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVL-FSTTIAENIRLGR-----EEATMEDIVQAAKDAN-----AYNFIMALP---QQfdtlvgegggqmsggqkq 565
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALAQVdlahlAGRDYPQLSggeQQ------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 566 RVAIARALIR------KPKILLLDMATSALDneseakvqgalnkIQHGHTIISVAHRLS----------------TVRSA 623
Cdd:PRK13548 142 RVQLARVLAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLRLARQLAherglavivvlhdlnlAARYA 208
|
250 260
....*....|....*....|.
gi 1390249242 624 DVIIGFEHGTAVERGTHEELL 644
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
138-360 |
2.39e-18 |
|
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: 87.15 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 138 VIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQM 217
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 218 ALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLS--SIRTVAAFG 295
Cdd:cd18550 118 TSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFG 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 296 GENKEVERYEKNLMFAQRWGI-------WKGMVMGFFTGYMwcliffcYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18550 198 REDDEAARFARRSRELRDLGVrqalagrWFFAALGLFTAIG-------PALVYWVGGLLVIG-GGLTIGTLV 261
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
423-615 |
2.81e-18 |
|
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: 84.62 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 423 HNVTFHYpsRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlniRWLRDQIGIVE 502
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 503 QEP--VLFSTTIAENIRLGREEA--TMEDIVQAAKDANAYNFIMALP-------QQfdtlvgegggqmsggqkqRVAIAR 571
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHPlslsggqKQ------------------RLAIAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAH 615
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1095-1306 |
2.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKV-NVQFLRSNIGIVSQEPvlfDCSIMDN 1173
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQNP---DNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 I----------KYGDNTKEISvERAIAAAKQAQLHDFvmslpEKYETNVgiqgsqLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:PRK13633 102 IveedvafgpeNLGIPPEEIR-ERVDESLKKVGMYEY-----RRHAPHL------LSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1244 EATSALDTESEKTVQLALDK--AREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
143-1277 |
3.03e-18 |
|
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: 91.51 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITG----ARQIR-KMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQM 217
Cdd:TIGR01271 121 AYYLALGLCLLFIVRTLLLHPAIFGlhhlGMQMRiALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAH 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 218 ALFLQRLSTALsglLLGFYrgWKLTLVI----LAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAA 293
Cdd:TIGR01271 201 FVWIAPLQVIL---LMGLI--WELLEVNgfcgLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 294 FGGENKeVERYEKNLmfaqrwgiwKGMVMGFFTGYMWCLIFfcYALAFWYGSRLVldegeytpgtliqIFLCVIIAAMNI 373
Cdd:TIGR01271 276 YCWEEA-MEKIIKNI---------RQDELKLTRKIAYLRYF--YSSAFFFSGFFV-------------VFLSVVPYALIK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 374 GnaSSCLEIFSTgCSAASSIFQTIDRQ----------------PVMDCMSGDGYKL---DRIKGEIEFHNVT-------- 426
Cdd:TIGR01271 331 G--IILRRIFTT-ISYCIVLRMTVTRQfpgaiqtwydslgaitKIQDFLCKEEYKTleyNLTTTEVEMVNVTaswdegig 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 427 -----------------------FHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDG 483
Cdd:TIGR01271 408 elfekikqnnkarkqpngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 484 hdirslnirwlrdQIGIVEQEPVLFSTTIAENIRLG--REEATMEDIVQAAKDANAynfIMALPQQFDTLVGEGGGQMSG 561
Cdd:TIGR01271 488 -------------RISFSPQTSWIMPGTIKDNIIFGlsYDEYRYTSVIKACQLEED---IALFPEKDKTVLGEGGITLSG 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 562 GQKQRVAIARALIRKPKILLLDMATSALDNESEAKV-QGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTH 640
Cdd:TIGR01271 552 GQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTF 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 641 EELLERKGVYFMLVTLQSQEDNTHKE------TGIKGKDTTEGDTPertfsRGSYQDSLRASIRQ--------RSKS--- 703
Cdd:TIGR01271 632 SELQAKRPDFSSLLLGLEAFDNFSAErrnsilTETLRRVSIDGDST-----VFSGPETIKQSFKQpppefaekRKQSiil 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 704 -------QLSHLSHEP--PLAIGDHKSSYE--DRK-----DNDvLVEEVEP----------------------------- 738
Cdd:TIGR01271 707 npiasarKFSFVQMGPqkAQATTIEDAVREpsERKfslvpEDE-QGEESLPrgnqyhhglqhqaqrrqsvlqlmthsnrg 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 739 --------APVRRILK-----------------------YNISE-----------------------WP----------- 753
Cdd:TIGR01271 786 enrreqlqTSFRKKSSitqqnelaseldiysrrlskdsvYEISEeineedlkecfaderenvfetttWNtylryittnrn 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 754 --YILVGAL---CAAINGAVTPIYSLLFSQILKTFSLVDKEQQRSEI------------YSMCLFFVILGCVSLFTQFLQ 816
Cdd:TIGR01271 866 lvFVLIFCLvifLAEVAASLLGLWLITDNPSAPNYVDQQHANASSPDvqkpviitptsaYYIFYIYVGTADSVLALGFFR 945
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 817 GYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDDLKnnPGVLTTRLATDASQVQgatgSQVGMMVNSFTNIFVAVLIAFlf 896
Cdd:TIGR01271 946 GLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMK--AGRILNRFTKDMAIID----DMLPLTLFDFIQLTLIVLGAI-- 1017
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 897 nwklsLVISVFFPFLALSG---AVQTKMLTGFASQDKEILEkagQITNEALSNIRTVAGIGVEGRF-IKAFEvelEKSY- 971
Cdd:TIGR01271 1018 -----FVVSVLQPYIFIAAipvAVIFIMLRAYFLRTSQQLK---QLESEARSPIFSHLITSLKGLWtIRAFG---RQSYf 1086
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 972 KTAIRKA-NVYglcyafsQGISFLANSaAYRYGGYLIvyeDLNFSYVFRVVSSIAMSATAVGR---------TFSYTPSY 1041
Cdd:TIGR01271 1087 ETLFHKAlNLH-------TANWFLYLS-TLRWFQMRI---DIIFVFFFIAVTFIAIGTNQDGEgevgiiltlAMNILSTL 1155
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1042 AKAKISA----------ARFFQLLDRKPPIDVYSGAGEK-----------------WDNfQGKIDFID--CKFTYPSRpd 1092
Cdd:TIGR01271 1156 QWAVNSSidvdglmrsvSRVFKFIDLPQEEPRPSGGGGKyqlstvlvienphaqkcWPS-GGQMDVQGltAKYTEAGR-- 1232
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 iQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDCSIMD 1172
Cdd:TIGR01271 1233 -AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRK 1310
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIkygDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:TIGR01271 1311 NL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
1370 1380
....*....|....*....|....*
gi 1390249242 1253 SEKTVQLALDKAREGRTCIVIAHRL 1277
Cdd:TIGR01271 1388 TLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
420-647 |
3.41e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHY-PSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIR----SLNIRW 493
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQ--EPVLFSTTIAENIRLGREEATMEDivQAAKDAnAYNFI--MALPQQfdtLVGEGGGQMSGGQKQRVAI 569
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE--DEAKEK-ALKWLkkVGLSED---LISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKV-QGALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
420-647 |
3.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 86.34 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPS-RP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSL----NIRW 493
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQ--EPVLFSTTIAENIRLGREE--ATMEDIVQAAKDAnaynfiMALPQQFDTLVGEGGGQMSGGQKQRVAI 569
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGT------HE 641
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKpkdifqDV 236
|
....*.
gi 1390249242 642 ELLERK 647
Cdd:PRK13649 237 DFLEEK 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1093-1307 |
3.71e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMI---DGHDSKKV---------------------N 1148
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTkekekvleklviqktrfkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1149 VQFLRSNIGIVSQ--EPVLFDCSIMDNIKYGDNTKEISVERAIA-AAKQAQLhdfvMSLPEKYetnvgIQGS--QLSRGE 1223
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKrAAKYIEL----VGLDESY-----LQRSpfELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1224 KQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKA-REGRTCIVIAHRL-STIQNSDIIAVMSQGVVIEKG-TH 1300
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTY 250
|
....*..
gi 1390249242 1301 KKLMDQK 1307
Cdd:PRK13651 251 DILSDNK 257
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
420-644 |
4.30e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.55 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVL-FSTTIAENIRLGR-----EEATMEDIVQAAkdanaynfiMAL-----------------PQQfdtlvgegg 556
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRaphgsSAAQDRQIVREA---------LALvglahlagrsyqtlsggEQQ--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALI-------RKPKILLLDMATSALDneseakvqgalnkIQHGHTIISVAHRLS----------- 618
Cdd:COG4559 141 ---------RVQLARVLAqlwepvdGGPRWLFLDEPTSALD-------------LAHQHAVLRLARQLArrgggvvavlh 198
|
250 260 270
....*....|....*....|....*....|
gi 1390249242 619 ----TVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:COG4559 199 dlnlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1092-1308 |
4.55e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH--DSKKVNVQFLRSNIGIVSQEPvlfdcs 1169
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 iMDNIKYGDNTKEISVE---RAIAAAKQAQLHDFVMSLpekyetnVGIQGSQ------LSRGEKQRIAIARAIVRDPKIL 1240
Cdd:PRK13638 87 -EQQIFYTDIDSDIAFSlrnLGVPEAEITRRVDEALTL-------VDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1241 LLDEATSALDTESeKTVQLALDK--AREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKG------THKKLMDQKG 1308
Cdd:PRK13638 159 LLDEPTAGLDPAG-RTQMIAIIRriVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
143-361 |
4.62e-18 |
|
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: 86.41 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQ 222
Cdd:cd18563 47 LGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 223 RLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVE 302
Cdd:cd18563 127 NILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIK 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 303 RYEK--------NLMFAQRWGIWKGMvMGFFTG----YMWcliffcyalafWYGSRLVLDeGEYTPGTLIQ 361
Cdd:cd18563 207 RFDEanqelldaNIRAEKLWATFFPL-LTFLTSlgtlIVW-----------YFGGRQVLS-GTMTLGTLVA 264
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1085-1275 |
4.94e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHdskkvnvqfLRsnIGIVSQEPV 1164
Cdd:COG0488 6 KSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFD-CSIMDNIKYGDN-TKEISVERAIAAAKQAQLHDFVM---SLPEKYE---------------TNVGIQGSQLSR--- 1221
Cdd:COG0488 72 LDDdLTVLDTVLDGDAeLRALEAELEELEAKLAEPDEDLErlaELQEEFEalggweaearaeeilSGLGFPEEDLDRpvs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1222 ----GEKQRIAIARAIVRDPKILLLDEATSALDTES----EKTVqlaldKAREGrTCIVIAH 1275
Cdd:COG0488 152 elsgGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1100-1250 |
6.44e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1100 SVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQflRSNIGIVSQEPVLFD-CSIMDNIKYG- 1177
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1178 ------DNTKEISVEraiAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:PRK10771 97 npglklNAAQREKLH---AIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
435-642 |
7.15e-18 |
|
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: 84.41 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 435 VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwLRDQIGIVE--QEPVLFST-T 511
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 512 IAENIRLG------------REEATMEDIVQAAK------------DANAYNfiMALPQQfdtlvgegggqmsggqkQRV 567
Cdd:cd03219 92 VLENVMVAaqartgsglllaRARREEREARERAEellervgladlaDRPAGE--LSYGQQ-----------------RRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEE 642
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
148-364 |
7.92e-18 |
|
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: 86.03 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 148 VGVAVL--ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLS 225
Cdd:cd18564 61 VGIALLrgLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYE 305
Cdd:cd18564 141 TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFA 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 306 KNLMFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLIqIFL 364
Cdd:cd18564 221 RENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLA-GRLTPGDLL-VFL 277
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
138-360 |
1.04e-17 |
|
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: 85.13 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 138 VIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDInkidEAIADqm 217
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDT----EALNE-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 218 aLFLQRLSTALSGL--LLG-----FYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRT 290
Cdd:cd18544 114 -LFTSGLVTLIGDLllLIGiliamFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 291 VAAFGGENKEVERYEK---NLMFAQRWGIWkgmVMGFFtgymWCLIFFCYALA----FWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18544 193 IQLFNREKREFEEFDEinqEYRKANLKSIK---LFALF----RPLVELLSSLAlalvLWYGGGQVLS-GAVTLGVLY 261
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
420-647 |
1.07e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.22 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHY-PSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDG----HDIRSLNIRW 493
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQ--EPVLFSTTIAENIRLGREEATMEdiVQAAKDaNAYNFIMALPQQFDTLvGEGGGQMSGGQKQRVAIAR 571
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKN-YAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
162-364 |
1.27e-17 |
|
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: 85.08 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 162 LWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKL 241
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 242 TLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLMFAQRWGIWKGMV 321
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1390249242 322 MGFFTGYMWCLIFFCYALAFWYGSRLvLDEGEYTPGTLIQIFL 364
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQL-IQSGHLTTGSLVSFIL 260
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
693-1307 |
1.28e-17 |
|
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: 89.20 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 693 LRASIRQrsKSQLSHLSHEPPLAIGDHKSSYEDRK-DNDVLVEEVEPAPVRRILKYNIseWPYILVGALC--AAINGAVT 769
Cdd:TIGR01271 24 LRKGYRQ--KLELSDIYQIPSFDSADNLSERLEREwDRELASAKKNPKLLNALRRCFF--WRFVFYGILLyfGEATKAVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 770 PiysLLFSQILKTFSLVDKEQQRSEIY---SMCLFFVILgcvslfTQFLQGYNFAKSGELLTKRLRKFG--FKAMLRQDI 844
Cdd:TIGR01271 100 P---LLLGRIIASYDPFNAPEREIAYYlalGLCLLFIVR------TLLLHPAIFGLHHLGMQMRIALFSliYKKTLKLSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 845 GWFDdlKNNPGVLTTRLATDASQVQGatgsqvGMMVNSF---TNIFVAVLIAFLfnWKLsLVISVF--FPFLALSGAVQT 919
Cdd:TIGR01271 171 RVLD--KISTGQLVSLLSNNLNKFDE------GLALAHFvwiAPLQVILLMGLI--WEL-LEVNGFcgLGFLILLALFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 920 ---KMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEgrfiKAFEVELEKSYKTAIRKANVYGLCYAFsqgisflaN 996
Cdd:TIGR01271 240 clgQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDELKLTRKIAYLRYF--------Y 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 997 SAAYRYGGYLIVY---------EDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPIDVYS-- 1065
Cdd:TIGR01271 308 SSAFFFSGFFVVFlsvvpyaliKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEyn 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1066 -----------------GAGE-----KWDNFQGKIDFIDCK--FTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKST 1121
Cdd:TIGR01271 388 ltttevemvnvtaswdeGIGElfekiKQNNKARKQPNGDDGlfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1122 SIQLLERFYDPDQGTVMIDGHdskkvnvqflrsnIGIVSQEPVLFDCSIMDNIKYGDNTKEIsveRAIAAAKQAQLHDFV 1201
Cdd:TIGR01271 468 LLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLSYDEY---RYTSVIKACQLEEDI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1202 MSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTI 1280
Cdd:TIGR01271 532 ALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHL 611
|
650 660
....*....|....*....|....*..
gi 1390249242 1281 QNSDIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:TIGR01271 612 KKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1095-1307 |
1.31e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.91 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FDCSIMDN 1173
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYGDN-----------TKEISVERAIAAAKQAQLHDFVMslpekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK11231 97 VAYGRSpwlslwgrlsaEDNARVNQAMEQTRINHLADRRL--------------TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1243 DEATSALDTESEktVQLaLDKARE----GRTCIVIAHRLStiQNS---DIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:PRK11231 163 DEPTTYLDINHQ--VEL-MRLMRElntqGKTVVTVLHDLN--QASrycDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1091-1292 |
1.68e-17 |
|
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: 82.76 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKST-------SIQLLE-RFYDPDQGTVMIDGHDSKKVNvqflRSNIGIVSQE 1162
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSlllailgEMQTLEgKVHWSNKNESEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 PVLFDCSIMDNIKYGdntKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:cd03290 88 PWLLNATVEENITFG---SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1243 DEATSALDTE-SEKTVQLALDK--AREGRTCIVIAHRLSTIQNSDIIAVMSQG 1292
Cdd:cd03290 165 DDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
420-615 |
2.27e-17 |
|
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: 82.30 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwLRDqIG 499
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLF-STTIAENIRLGREEATM--EDIVQAAKDAnaynfimALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRK 576
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVpkDEIDERVREV-------AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAH 615
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTH 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1078-1307 |
2.43e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKvNVQFLRSNIG 1157
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQepvlFD-----CSIMDNI-----KYGDNTKEIsvERAIAAakqaqLHDFVmSLPEKYETNVgiqgSQLSRGEKQRI 1227
Cdd:PRK13536 118 VVPQ----FDnldleFTVRENLlvfgrYFGMSTREI--EAVIPS-----LLEFA-RLESKADARV----SDLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALDTESEktvQLALDKAR----EGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKK 1302
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHAR---HLIWERLRsllaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHA 258
|
....*
gi 1390249242 1303 LMDQK 1307
Cdd:PRK13536 259 LIDEH 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1090-1299 |
2.75e-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: 88.53 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVLNglsVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKkVNVQFLRSNIGIVSQEPVLFD-C 1168
Cdd:TIGR01257 943 RPAVDRLN---ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHhL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYGDNTKEISVERAiAAAKQAQLHDFVMSLPEKYEtnvgiqGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEA-QLEMEAMLEDTGLHHKRNEE------AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1249 LDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
420-635 |
2.92e-17 |
|
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: 80.55 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ-I 498
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVlfsttiAEnirlgreeatmedivqaakdanaynfimalpQQfdtlvgegggqmsggqkqRVAIARALIRKPK 578
Cdd:cd03216 78 AMVYQLSV------GE-------------------------------RQ------------------MVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 579 ILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVRS-ADVIIGFEHGTAV 635
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1085-1299 |
3.37e-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: 82.38 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRsNIGIV--SQE 1162
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 PVLFDCSIMDNIKYgdnTKEI-SVERAIAAAKQAQLHDfVMSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:cd03267 105 QLWWDLPVIDSFYL---LAAIyDLPPARFKKRLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1242 LDEATSALDTESEKTVQLALDKAREGRTCIVIahrLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVL---LTSHYMKDIEALARRVLVIDKGR 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
419-643 |
3.39e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHY-PSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI----RSLNIR 492
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 493 WLRDQIGIVEQ--EPVLFSTTIAENIRLGREE--ATMEDIVQAAKDANAynfIMALPQQfdtLVGEGGGQMSGGQKQRVA 568
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEE---LLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEEL 643
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1299 |
3.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPDIQ--VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH----DSKKVNVQF 1151
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1152 LRSNIGIVSQ--EPVLFDCSIMDNIKYGDNTKEISVERAIAAAKQA-QLhdfvMSLPEKYetnvgIQGS--QLSRGEKQR 1226
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMiEL----VGLPEEL-----LARSpfELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1227 IAIARAIVRDPKILLLDEATSALDTESEKTVQ---LALDKaREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
755-1014 |
4.58e-17 |
|
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: 83.21 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQILKTFsLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKF 834
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDY-IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 835 GFKAMLRQDIGWFDdlkNNP-GVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLAL 913
Cdd:cd18544 80 LFSHIQRLPLSFFD---RTPvGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 914 SGAV-QTKMLTGFasqdKEILEKAGQIT---NEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQ 989
Cdd:cd18544 157 ATYLfRKKSRKAY----REVREKLSRLNaflQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVE 232
|
250 260
....*....|....*....|....*
gi 1390249242 990 GISFLANSAAYRYGGYLIVYEDLNF 1014
Cdd:cd18544 233 LLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
755-1050 |
4.71e-17 |
|
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: 83.25 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVtpiySLLFSQILKtfSLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKF 834
Cdd:cd18551 1 LILALLLSLLGTAA----SLAQPLLVK--NLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 835 GFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALS 914
Cdd:cd18551 75 LWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 915 GAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFL 994
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 995 ANSAAYRYGGYLIVYEDLNFS-------YVFRVVSSIAMSATAVGrtfsytpSYAKAKISAAR 1050
Cdd:cd18551 233 ALLVVLGVGGARVASGALTVGtlvafllYLFQLITPLSQLSSFFT-------QLQKALGALER 288
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1090-1299 |
5.54e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLErFYDPD----QGTVMIDGHdskKVNVQFLRSNIGIVSQEPVL 1165
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1166 F-------DCSIMDNIKYGDN-TKEISVERAiaaakQAQLHDfvMSLPEKYETNVGIQGSQ--LSRGEKQRIAIARAIVR 1235
Cdd:TIGR00955 111 IptltvreHLMFQAHLRMPRRvTKKEKRERV-----DEVLQA--LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1236 DPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLST--IQNSDIIAVMSQGVVIEKGT 1299
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVvQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
420-649 |
5.84e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGH--DIRSLNIRWLRDQ 497
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEP--VLFSTTIAENIRLGREEATM-EDIVQA-AKDANAYNFIMALPQQfdtlvgeGGGQMSGGQKQRVAIARAL 573
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpEDEVRKrVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVR-SADVIIGFEHGTAVERGTHEELLERKGV 649
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1077-1299 |
7.26e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1077 KIDFIDCKFTYPSrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKST---SIQLLERFYDpdqGTVMIDGhdsKKVN-VQFL 1152
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLERITS---GEIWIGG---RVVNeLEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1153 RSNIGIVSQEPVLF-DCSIMDNIKYG-DNTK----EISvERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQR 1226
Cdd:PRK11650 75 DRDIAMVFQNYALYpHMSVRENMAYGlKIRGmpkaEIE-ERVAEAARILELEPLLDRKP-----------RELSGGQRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1227 IAIARAIVRDPKILLLDEATSALDTeseK-TVQLALD----KAREGRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDA---KlRVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
438-644 |
8.08e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRD----QIGIVEQEPVLFS-TTI 512
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 513 AENIRLGREEATM------EDIVQAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVAIARALIRKPKILLLDMAT 586
Cdd:PRK10070 124 LDNTAFGMELAGInaeerrEKALDALRQVGLENYAHSYPDELS-----------GGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 587 SALDNESEAKVQGALNKIQ--HGHTIISVAHRL-STVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1091-1292 |
9.11e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGTVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLF 1166
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 -DCSIMDNIKYGDntkEIS----------VERAIAAAKQAQLHdfvmslpekyeTNVGIQGSQLSRGEKQRIAIARAIVR 1235
Cdd:PRK13549 95 kELSVLENIFLGN---EITpggimdydamYLRAQKLLAQLKLD-----------INPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1236 DPKILLLDEATSALdTESEKTVQLAL--DKAREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:PRK13549 161 QARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
426-644 |
9.53e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 81.81 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 426 TFHYPS----RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI-------RSLNIRWL 494
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeygdykyRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 ----------RDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggqk 564
Cdd:COG4167 93 fqdpntslnpRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK----------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 565 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHE 641
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQekLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTA 235
|
...
gi 1390249242 642 ELL 644
Cdd:COG4167 236 EVF 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
420-646 |
1.21e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRDQIG 499
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLG-REEAT-MEDIVQAAKDANAY----NFIMALPQQFdtlvgegggqmSGGQKQRVAIARA 572
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlRMQKTpAAEITPRVMEALRMvqleEFAQRKPHQL-----------SGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 573 LIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH----RLSTvrsADVIIGFEHGTAVERGTHEELLER 646
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
759-995 |
1.33e-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: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 759 ALCAAINGAVTpiySLLFSQILKtfSLVDK---EQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFG 835
Cdd:cd18575 1 ALIALLIAAAA---TLALGQGLR--LLIDQgfaAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 836 FKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVIS-----VFFPF 910
Cdd:cd18575 76 FAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLlviplVVLPI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 911 LALSGAVQTkmLTGfASQDKeiLEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQG 990
Cdd:cd18575 154 ILFGRRVRR--LSR-ASQDR--LADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIF 228
|
....*
gi 1390249242 991 ISFLA 995
Cdd:cd18575 229 LVFGA 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1093-1298 |
1.51e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN-VQFLRSNIGIVSQEPVLF-DCSI 1170
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFpNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGDNTKEISVERAIAAAKQAQLHdfvmslpekyeTNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALd 1250
Cdd:PRK15439 104 KENILFGLPKRQASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1251 TESE-----KTVQLALDKareGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKG 1298
Cdd:PRK15439 172 TPAEterlfSRIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1090-1299 |
1.52e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.37 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPV----- 1164
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 ------LFDCSIMDNIKYGDNTKEisvERAIAAAKQAQLhdfvmsLPEkyetNVGIQGSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK15112 103 rqrisqILDFPLRLNTDLEPEQRE---KQIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1239 ILLLDEATSALD-TESEKTVQLALD-KAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:PRK15112 170 VIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
435-642 |
1.60e-16 |
|
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: 80.85 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 435 VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlrdQI---GIVE--QEPVLFS 509
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIarlGIARtfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 510 T-TIAENIRLG--------------------REEATMEDIVQAA---------KDANAYNfiMALPQQfdtlvgegggqm 559
Cdd:COG0411 93 ElTVLENVLVAaharlgrgllaallrlprarREEREARERAEELlervgladrADEPAGN--LSYGQQ------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 560 sggqkQRVAIARALIRKPKILLLDMATSALdNESE-AKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAV 635
Cdd:COG0411 159 -----RRLEIARALATEPKLLLLDEPAAGL-NPEEtEELAELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVI 232
|
....*..
gi 1390249242 636 ERGTHEE 642
Cdd:COG0411 233 AEGTPAE 239
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
420-615 |
1.68e-16 |
|
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: 79.86 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIG 499
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENIRL-----GREEATMEDIVQAAKDanaynfIMALPQQFDTLVgeggGQMSGGQKQRVAIARAL 573
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAH 615
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1085-1299 |
1.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN-VQFLRSNIGIVSQEP 1163
Cdd:PRK13644 9 YSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 --VLFDCSIMDNIKYGDNT-----KEIS--VERAIAAAKQaqlhdfvmslpEKYETNvgiQGSQLSRGEKQRIAIARAIV 1234
Cdd:PRK13644 87 etQFVGRTVEEDLAFGPENlclppIEIRkrVDRALAEIGL-----------EKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1235 RDPKILLLDEATSALDTESEKTVQLALDKA-REGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1097-1320 |
1.85e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1097 NGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN-VQFL--RSNIGIVSQEPVlfdCSIMDN 1173
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPL---ASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYGDNTKEiSVERAIAAAKQAQLHDFVMSLPEKyetnVGIQGSQLSR-------GEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK15079 115 MTIGEIIAE-PLRTYHPKLSRQEVKDRVKAMMLK----VGLLPNLINRyphefsgGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1247 SALDTESE-KTVQLALDKARE-GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLM-DQKGAYYKLVITGAPI 1320
Cdd:PRK15079 190 SALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYhNPLHPYTKALMSAVPI 267
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1094-1299 |
2.11e-16 |
|
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: 79.89 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVqFLRSNIGI--VSQEPVLF-DCSI 1170
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIK-----YGDNTKEISvERAiaaakQAQLHDF-VMSLPEKYetnvgiqGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03218 93 EENILavleiRGLSKKERE-EKL-----EELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1245 ATSALDTESEKTVQLALDKAREGRTCIVIA-HRLS-TIQNSDIIAVMSQGVVIEKGT 1299
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGT 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1095-1278 |
2.61e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQF---LRSN-IGIVSQ-EPVLFDCS 1169
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIkygdntkeiSVERAIAAAKQAQLHD--FVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:PRK11629 104 ALENV---------AMPLLIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|...
gi 1390249242 1248 ALDTESEKTVQLALDK--AREGRTCIVIAHRLS 1278
Cdd:PRK11629 175 NLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
755-1008 |
3.61e-16 |
|
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: 80.53 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVtpiySLLFSQILKTF--SLVDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLR 832
Cdd:cd18541 1 YLLGILFLILVDLL----QLLIPRIIGRAidALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 833 KFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLA 912
Cdd:cd18541 77 NDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 913 LSGAVQTKMLTgfaSQDKEILEKAGQITN---EALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQ 989
Cdd:cd18541 155 LLVYRLGKKIH---KRFRKVQEAFSDLSDrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
250
....*....|....*....
gi 1390249242 990 GISFLANSAAYRYGGYLIV 1008
Cdd:cd18541 232 LLIGLSFLIVLWYGGRLVI 250
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
827-1008 |
3.93e-16 |
|
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: 80.43 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 827 LTKRLRKFGFKAMLRQDIGWFDDLKNnpGVLTTRLATDASQVQgatgSQVGMMVNSFTNIFVAVL--IAFLF--NWKLSL 902
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFDTVKT--GDITSRLTSDTTTMS----DTVSLNLNIFLRSLVKAIgvIVFMFklSWQLSL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 903 VISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYG 982
Cdd:cd18784 141 VTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG 220
|
170 180
....*....|....*....|....*...
gi 1390249242 983 LcYAFSQGISFLANSAA--YrYGGYLIV 1008
Cdd:cd18784 221 G-YVWSNELTELALTVStlY-YGGHLVI 246
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1086-1275 |
4.65e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPS-RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVN----VQFLRSNIGIVS 1160
Cdd:PRK10535 13 SYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1161 QE-PVLFDCSIMDNIK----YGDNTKEISVERAIAAAKQAQLHDfvmslpekyetNVGIQGSQLSRGEKQRIAIARAIVR 1235
Cdd:PRK10535 93 QRyHLLSHLTAAQNVEvpavYAGLERKQRLLRAQELLQRLGLED-----------RVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDKARE-GRTCIVIAH 1275
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
424-644 |
5.37e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSL-------------N 490
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 491 IRWLRDQIGIVEQEPVLFS-TTIAENIR--------LGREEATMEDIVQAAK---DANA---YNFIMALPQQfdtlvgeg 555
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWShMTVLENVMeapiqvlgLSKQEARERAVKYLAKvgiDERAqgkYPVHLSGGQQ-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVIIGFEH-GT 633
Cdd:PRK10619 159 ---------QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHqGK 229
|
250
....*....|.
gi 1390249242 634 AVERGTHEELL 644
Cdd:PRK10619 230 IEEEGAPEQLF 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
418-616 |
5.69e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYPS-RPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDiRSLnirwlrd 496
Cdd:COG4178 361 GALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 qigIVEQEPVLFSTTIAENIR--LGREEATMEDIVQAAKDANaynfimaLP--------------------QQfdtlvge 554
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVG-------LGhlaerldeeadwdqvlslgeQQ------- 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 555 gggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHR 616
Cdd:COG4178 493 -----------RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1091-1305 |
6.55e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdskkVNVQF------LRSNIGIVSQEPV 1164
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-----QEMRFasttaaLAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LF-DCSIMDNIKYGD--NTKEISVERAIAAAKQAQLH----DFVMSLPEKYetnvgiqgsqLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK11288 90 LVpEMTVAENLYLGQlpHKGGIVNRRLLNYEAREQLEhlgvDIDPDTPLKY----------LSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1238 KILLLDEATSALDT-ESEKTVQLALDKAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEkgTHKKLMD 1305
Cdd:PRK11288 160 RVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMAQ 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1069-1306 |
6.55e-16 |
|
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: 82.54 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1069 EKWDNFQGKIDFI---DCKFTYPS--RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTV------ 1137
Cdd:TIGR03269 268 EKECEVEVGEPIIkvrNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgd 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1138 -MIDGHDSKKVNVQFLRSNIGIVSQEPVLF-DCSIMDNIkygdnTKEISVERAIAAAKQAQLHDFVMS-LPEKYETNV-G 1213
Cdd:TIGR03269 348 eWVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEIlD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1214 IQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKARE--GRTCIVIAHRLSTIQN-SDIIAVMS 1290
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMR 502
|
250
....*....|....*.
gi 1390249242 1291 QGVVIEKGTHKKLMDQ 1306
Cdd:TIGR03269 503 DGKIVKIGDPEEIVEE 518
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
421-590 |
6.97e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.91 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDP---CEGMVTLDGHDIRSLNIRwlRDQ 497
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFS-TTIAENI------RLGREEAtmEDIVQAA-KDANAYNFIMALPqqfDTLvgegggqmSGGQKQRVAI 569
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLafalppTIGRAQR--RARVEQAlEEAGLAGFADRDP---ATL--------SGGQRARVAL 144
|
170 180
....*....|....*....|.
gi 1390249242 570 ARALIRKPKILLLDMATSALD 590
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLD 165
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1095-1307 |
8.10e-16 |
|
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: 79.52 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHdskkvnvqflrsnIGIVSQEPVLFDCSIMDNI 1174
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 KYGDNTKEIsveRAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1254
Cdd:cd03291 119 IFGVSYDEY---RYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1255 KTV-QLALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:cd03291 196 KEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
424-646 |
8.61e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.01 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSR-----PE--VKILNNLSMVIKPGETTAFVGSSGAGKST---ALQLIQRfydPCEGMVTLDGHDIR------ 487
Cdd:PRK11308 10 DLKKHYPVKrglfkPErlVKALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIET---PTGGELYYQGQDLLkadpea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 488 -----------------SLNIRWlrdQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYnfimalPQQFdt 550
Cdd:PRK11308 87 qkllrqkiqivfqnpygSLNPRK---KVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 551 lvgegggqmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVII 627
Cdd:PRK11308 156 ---------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEHiADEVM 226
|
250
....*....|....*....
gi 1390249242 628 GFEHGTAVERGTHEELLER 646
Cdd:PRK11308 227 VMYLGRCVEKGTKEQIFNN 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-646 |
8.74e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-----PCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLF 508
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 ST-TIAENIRLG-------REEATMEDIVQAAKDAnaynfiMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKIL 580
Cdd:PRK14247 95 PNlSIFENVALGlklnrlvKSKKELQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 581 LLDMATSALDNESEAKVQGALNKIQHGHTIISVAH-RLSTVRSADVIIGFEHGTAVERGTHEELLER 646
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
420-646 |
1.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYpsRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEP--VLFSTTIAENI-----RLGREEATMEDIVQAA-KDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVAIAR 571
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIafgpiNLGLDEETVAHRVSSAlHMLGLEELRDRVPHHLS-----------GGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEELLER 646
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1084-1276 |
1.53e-15 |
|
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: 75.65 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1084 KFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHdskkvnvqflrSNIGIVSQEP 1163
Cdd:cd03223 5 NLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 VLFDCSIMDNIKYgdntkeisveraiaaakqaqlhdfvmslPekyetnvgiQGSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:cd03223 74 YLPLGTLREQLIY----------------------------P---------WDDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 1390249242 1244 EATSALDTESEKTV-QLALDkarEGRTCIVIAHR 1276
Cdd:cd03223 117 EATSALDEESEDRLyQLLKE---LGITVISVGHR 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
424-646 |
1.56e-15 |
|
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: 81.27 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSRpEVKILNNLSMVIKPGETTAFVGSSGAGKS-TAL---QLIQRFYDPCEGMVTLDGHDIRSLNIRWLR---- 495
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQIGIVEQEPV-----LFS--TTIAENIRL----GREEATME--------DIVQAAKDANAYnfimalP-------QQfd 549
Cdd:COG4172 92 NRIAMIFQEPMtslnpLHTigKQIAEVLRLhrglSGAAARARalellervGIPDPERRLDAY------PhqlsggqRQ-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 550 tlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVI 626
Cdd:COG4172 164 ----------------RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 1390249242 627 IGFEHGTAVERGTHEELLER 646
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1094-1303 |
1.56e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKS-TSIQLLERFYDPD----QGTVMIDGHDSKKVNVQFLR----SNIGIVSQEP- 1163
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 ---------------VLfdcSIMDNIKYGDNTKEI--SVER-AIAAAKQaQLHDFvmslPEkyetnvgiqgsQLSRGEKQ 1225
Cdd:PRK15134 103 vslnplhtlekqlyeVL---SLHRGMRREAARGEIlnCLDRvGIRQAAK-RLTDY----PH-----------QLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALD-TESEKTVQLALDKARE-GRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKK 1302
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDvSVQAQILQLLRELQQElNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAAT 243
|
.
gi 1390249242 1303 L 1303
Cdd:PRK15134 244 L 244
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
420-590 |
1.61e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.31 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTF---HYPSRpevkilnnLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRD 496
Cdd:PRK10771 2 LKLTDITWlyhHLPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFS-TTIAENIRLG---------REEATMEDIvqaAKDANAYNFIMALPQQFdtlvgegggqmSGGQKQR 566
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGlnpglklnaAQREKLHAI---ARQMGIEDLLARLPGQL-----------SGGQRQR 137
|
170 180
....*....|....*....|....
gi 1390249242 567 VAIARALIRKPKILLLDMATSALD 590
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALD 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
436-643 |
1.65e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRDQIGIVEQEPvLFSTT- 511
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 512 -------IAENIR-----LGREEatMEDIVQA--AKDANAYNFIMALPQQFdtlvgegggqmSGGQKQRVAIARALIRKP 577
Cdd:PRK15079 114 rmtigeiIAEPLRtyhpkLSRQE--VKDRVKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEEL 643
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
420-643 |
2.08e-15 |
|
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: 76.64 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIG 499
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPvlfsttIAENIRLGREEATMEDIVQAAKDANAYNFI------MALPQQFDTLVgeggGQMSGGQKQRVAIARAL 573
Cdd:cd03265 77 IVFQDL------SVDDELTGWENLYIHARLYGVPGAERRERIdelldfVGLLEAADRLV----KTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEEL 643
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1095-1280 |
2.12e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQFL----RSN-IGIVSQEPVLFDC- 1168
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLpeykRAKyIGRVFQDPMMGTAp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 --SIMDN------------IKYGDNTKEisveRAIAAAKQAQLHdfvMSLPEKYETNVGiqgsQLSRGEKQRIAIARAIV 1234
Cdd:COG1101 96 smTIEENlalayrrgkrrgLRRGLTKKR----RELFRELLATLG---LGLENRLDTKVG----LLSGGQRQALSLLMATL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390249242 1235 RDPKILLLDEATSALDTeseKTVQLALDKAREgrtcIVIAHRLSTI 1280
Cdd:COG1101 165 TKPKLLLLDEHTAALDP---KTAALVLELTEK----IVEENNLTTL 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
420-641 |
2.13e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.36 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGH------DIRSLNIRW 493
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQEPVLFS-TTIAENI--------RLGREEATME-----DIVQAAKDANAYNFIMALPQQfdtlvgegggqm 559
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLieapcrvlGLSKDQALARaekllERLRLKPYADRFPLHLSGGQQ------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 560 sggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRS-ADVIIGFEHGTAVER 637
Cdd:PRK11124 148 -----QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
....
gi 1390249242 638 GTHE 641
Cdd:PRK11124 223 GDAS 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1096-1292 |
2.24e-15 |
|
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: 77.12 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQFLRSNIGIVSQEPVLFD-CSIMDNI 1174
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPGPDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 KygdntkeISVERAIAAAKQAQLHDFVmslpEKYETNVGIQGS------QLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:TIGR01184 76 A-------LAVDRVLPDLSKSERRAIV----EEHIALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1390249242 1249 LDTESEKTVQLALDKARE--GRTCIVIAHRL-STIQNSDIIAVMSQG 1292
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
420-644 |
2.35e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNV--TFHYPS----RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI------- 486
Cdd:PRK15112 5 LEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 487 RSLNIRWL----------RDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQfdtlvgegg 556
Cdd:PRK15112 85 RSQRIRMIfqdpstslnpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQK--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTI--ISVAHRLSTVRS-ADVIIGFEHGT 633
Cdd:PRK15112 156 --------QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGE 227
|
250
....*....|.
gi 1390249242 634 AVERGTHEELL 644
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1092-1306 |
2.39e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.03 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL---ERfYDPDQGTVMIDGHD---------SKK------------- 1146
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDilelspderARAgiflafqypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1147 -VNV-QFLRSNIGIVSQEPVlfdcSIMDNIKygdntkeisveRAIAAAKQaqlhdfvMSLPEKY---ETNVGiqgsqLSR 1221
Cdd:COG0396 91 gVSVsNFLRTALNARRGEEL----SAREFLK-----------LLKEKMKE-------LGLDEDFldrYVNEG-----FSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1222 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAR-EGRTCIVIAH--RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
....*...
gi 1390249242 1299 ThKKLMDQ 1306
Cdd:COG0396 224 G-KELALE 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1092-1292 |
2.46e-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: 80.64 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGTVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLF- 1166
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DCSIMDNIKYGDntkEIS-----------VERAIAAAKQAQLHDFVMSLPekyetnVGiqgsQLSRGEKQRIAIARAIVR 1235
Cdd:TIGR02633 92 ELSVAENIFLGN---EITlpggrmaynamYLRAKNLLRELQLDADNVTRP------VG----DYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1236 DPKILLLDEATSALdTESEKTVQLAL--DKAREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:TIGR02633 159 QARLLILDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1095-1303 |
2.58e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDP-----DQGTVMIDGHDSKKV-NVQFLRSNIGIVSQEPVLFDC 1168
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYGDNTKEISVERAIAAAKQAQLHDfvMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1249 LDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKL 1303
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1089-1292 |
3.19e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSN-IGIVSQE-PVLF 1166
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DCSIMDNIKYGDN-TKEISVERAIAAAK---QAQLHDFVMSLPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK09700 94 ELTVLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1243 DEATSALDTESEKTVQLALDKAR-EGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1088-1299 |
3.32e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1088 PSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdskkvNVQFL-------------RS 1154
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALlelgagfhpeltgRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVsqepvlfdCSIMdnikyGDNTKEI-SVERAIAAAkqAQLHDFvMSLPEKYetnvgiqgsqLSRGEKQRIAIARAI 1233
Cdd:COG1134 108 NIYLN--------GRLL-----GLSRKEIdEKFDEIVEF--AELGDF-IDQPVKT----------YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1234 VRDPKILLLDEATSALDTE-SEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1092-1305 |
3.64e-15 |
|
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: 76.56 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQFLRSN------IGIVSQEPVL 1165
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHriarlgIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1166 F-DCSIMDNIkygdntkEISVERAIAAAKQAQLHDFVMSL-PEKYEtNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:COG0410 90 FpSLTVEENL-------LLGAYARRDRAEVRADLERVYELfPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1244 EATSALdteSEKTVQLALDK----AREGRTCIVI---AHRLSTIqnSDIIAVMSQGVVIEKGTHKKLMD 1305
Cdd:COG0410 162 EPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
136-306 |
4.14e-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: 77.44 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 136 SEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIAD 215
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 216 QMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFG 295
Cdd:cd18547 122 SLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFN 201
|
170
....*....|.
gi 1390249242 296 GENKEVERYEK 306
Cdd:cd18547 202 REEEAIEEFDE 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1078-1287 |
4.29e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPsrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhDSKKVNVQFLRSNIG 1157
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQ----EPvlfDCSIMDNIK-YGdntKEISVERAIAAAKQAQLHDFVmSLPEKYETNVGiqgsQLSRGEKQRIAIARA 1232
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvFG---RYFGLSAAAARALVPPLLEFA-KLENKADAKVG----ELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1233 IVRDPKILLLDEATSALDTESE--------------KTVQLALDKAREG-RTCiviaHRLSTIQNSDIIA 1287
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARhlmwerlrsllargKTILLTTHFMEEAeRLC----DRLCVIEEGRKIA 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
421-649 |
4.88e-15 |
|
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: 76.17 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNI-RWLRDQIG 499
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST-TIAENIRLGREEATMEDIVQAAKDanaynFIMAL-P-----------------QQFdtlvgegggqms 560
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLE-----RVYELfPrlkerrrqragtlsggeQQM------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 561 ggqkqrVAIARALIRKPKILLLDmatsaldnE-SE-------AKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFE 630
Cdd:COG0410 145 ------LAIGRALMSRPKLLLLD--------EpSLglaplivEEIFEIIRRLnREGVTILLVEQNARFALEiADRAYVLE 210
|
250
....*....|....*....
gi 1390249242 631 HGTAVERGTHEELLERKGV 649
Cdd:COG0410 211 RGRIVLEGTAAELLADPEV 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
423-636 |
7.90e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 423 HNVTFHYPS------RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRW 493
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQ-----------------EPVLFSTTIAENIRLGREEATMEDIVQAAKDANAynfimaLPQQFdtlvgegg 556
Cdd:PRK10419 87 FRRDIQMVFQdsisavnprktvreiirEPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK------RPPQL-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTV-RSADVIIGFEHGT 633
Cdd:PRK10419 153 ---SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNGQ 229
|
...
gi 1390249242 634 AVE 636
Cdd:PRK10419 230 IVE 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
419-639 |
8.20e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHYPSRPEVKilnNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-----PCEGMVTLDGHDIRSLNIR- 492
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 493 -WLRDQIGIVEQEPVLFSTTIAENIRLGRE----EATMEDIVQAA-KDAnaynfimALPQQFDTLVGEGGGQMSGGQKQR 566
Cdd:PRK14243 87 vEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSlRQA-------ALWDEVKDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 567 VAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTV-RSADvIIGFEHGTAVERGT 639
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSD-MTAFFNVELTEGGG 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1094-1298 |
8.40e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVD---PGQTL-AFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH---DS-KKVNVQFLRSNIGIVSQEPVL 1165
Cdd:PRK11144 8 QQLGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1166 F-DCSIMDNIKYGdntkeisveraIAAAKQAQLHDFVMSLpekyetnvGIQG------SQLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK11144 88 FpHYKVRGNLRYG-----------MAKSMVAQFDKIVALL--------GIEPlldrypGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1239 ILLLDEATSALDTESEKTVQLALDK-AREGRTCIV-IAHRLSTI-QNSDIIAVMSQGVVIEKG 1298
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
430-638 |
1.01e-14 |
|
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: 74.71 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 430 PSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIrSLNIRWLRDQIGIVEQEPVLFS 509
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 510 -TTIAENIR-------LGREEAT--MEDIVQAAkdanaynfimalpqQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKI 579
Cdd:cd03266 92 rLTARENLEyfaglygLKGDELTarLEELADRL--------------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 580 LLLDMATSALDNESeakVQGALNKIQH----GHTIISVAHRLSTVRS-ADVIIGFEHGTAVERG 638
Cdd:cd03266 158 LLLDEPTTGLDVMA---TRALREFIRQlralGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
420-645 |
1.11e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHY-PSRP-EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN----IRW 493
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQIGIVEQEP--VLFSTTIAENIRLGREEATMEDiVQAAKDANAYNFIMALPQQFdtlVGEGGGQMSGGQKQRVAIAR 571
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEELLE 645
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
420-622 |
1.44e-14 |
|
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: 74.15 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGeTTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIG 499
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFSTTIAE----------NIRLGREEATmedIVQAAKDANAYNFIMALPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:cd03264 76 YLPQEFGVYPNFTVRefldyiawlkGIPSKEVKAR---VDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 622
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVES 194
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
793-1007 |
1.65e-14 |
|
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: 75.45 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 793 SEIYSMCLFFVIlgcvSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGAT 872
Cdd:cd18590 37 SAIGLMCLFSLG----SSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSRSV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 873 GSQVGMMVNSFtnIFVAVLIAFLF--NWKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTV 950
Cdd:cd18590 111 ALNANVLLRSL--VKTLGMLGFMLslSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 951 AGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLI 1007
Cdd:cd18590 189 RSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLI 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
420-626 |
1.71e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGhdiRSLNIRWLRD--- 496
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 -QIGIVEQEPVLFST-TIAENIRLGREEATME--DIVQAAKD----ANAYNF-------IMALP---QQfdtlvgegggq 558
Cdd:COG3845 80 lGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARARirelSERYGLdvdpdakVEDLSvgeQQ----------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 559 msggqkqRVAIARALIRKPKILLLDMATSAL-DNESEaKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVI 626
Cdd:COG3845 149 -------RVEILKALYRGARILILDEPTAVLtPQEAD-ELFEILRRLaAEGKSIIFITHKLREVMAiADRV 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1099-1299 |
1.96e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.93 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYD-PdqGTVM-----IDGHD----SKKVNVQFLRSNIGIVSQEPV--LF 1166
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaekleFNGQDlqriSEKERRNLVGAEVAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DC-----SIMDNIKY--GDNTKEiSVERAIAAAKQAQLHDfvmslPEkyeTNVGIQGSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK11022 104 PCytvgfQIMEAIKVhqGGNKKT-RRQRAIDLLNQVGIPD-----PA---SRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1240 LLLDEATSALD-TESEKTVQLALD-KAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK11022 175 LIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1085-1296 |
2.02e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIdGHdskkvNVQflrsnIGIVSQEPV 1164
Cdd:COG0488 323 KSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDC--SIMDNIK-YGDNTKEISVeRAIaaakqaqLHDFVMSlPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:COG0488 389 ELDPdkTVLDELRdGAPGGTEQEV-RGY-------LGRFLFS-GDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1242 LDEATSALDTESEKTVQLALDkAREGrTCIVIAH-R--LSTIQNSdIIAVmSQGVVIE 1296
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRVATR-ILEF-EDGGVRE 509
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1089-1295 |
2.22e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsKKVNVQFLRSN----IGIVSQEPV 1164
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFD-CSIMDNIKYGdntKEISveRAIAAAKQAQLHDFV------MSLPEKYETNVGiqgsQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK10762 90 LIPqLTIAENIFLG---REFV--NRFGRIDWKKMYAEAdkllarLNLRFSSDKLVG----ELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1238 KILLLDEATSAL-DTESEKTVQLALDKAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVI 1295
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
420-658 |
2.35e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.02 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSrpEVKILNNLSMVIKPGETTAFVGSSGAGKST-ALQLiQRFYDPCEGMVTLDGHDIRSLN-IRWLRDQ 497
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTlALHL-NGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEP--VLFSTTIAENIRLGREEATMEDI-VQAAKDanaynfiMALPQ-QFDTLVGEGGGQMSGGQKQRVAIARAL 573
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIeIRKRVD-------RALAEiGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVYFM 652
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
....*.
gi 1390249242 653 LVTLQS 658
Cdd:PRK13644 232 GLTPPS 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
420-643 |
2.80e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.74 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVK---ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRW-LR 495
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQIGIVEQEP--VLFSTTIAENIRLGRE------EATMEDIVQAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRV 567
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEnlgippEEIRERVDESLKKVGMYEYRRHAPHLLS-----------GGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEEL 643
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1093-1316 |
3.08e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRsNIGIV----SQepVLFDC 1168
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYgdnTKEI-SVERAIAAAKQAQLHDfVMSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:COG4586 112 PAIDSFRL---LKAIyRIPDAEYKKRLDELVE-LLDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1248 ALDTESEKTVQ--LALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQKGAYYKLVIT 1316
Cdd:COG4586 184 GLDVVSKEAIRefLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLE 255
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
438-592 |
3.15e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIR---WLRDQIGIVEQEP-VLFSTTIA 513
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 514 EN--IRLGREEATMEDI---VQAAKDA-----NAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKIL 580
Cdd:PRK10908 98 DNvaIPLIIAGASGDDIrrrVSAALDKvglldKAKNFPIQLSggeQQ------------------RVGIARAVVNKPAVL 159
|
170
....*....|..
gi 1390249242 581 LLDMATSALDNE 592
Cdd:PRK10908 160 LADEPTGNLDDA 171
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
790-1050 |
3.49e-14 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 74.74 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 790 QQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDDLKnnPGVLTTRLATDASQVQ 869
Cdd:cd18548 33 GDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFG--TSSLITRLTNDVTQVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 870 GATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALS-GAVQTKMLTGFASQDKEiLEKAGQITNEALSNIR 948
Cdd:cd18548 111 NFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVvFLIMKKAIPLFKKVQKK-LDRLNRVVRENLTGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 949 TVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLNF-------SYVFRVV 1021
Cdd:cd18548 190 VIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVgdlvafiNYLMQIL 269
|
250 260
....*....|....*....|....*....
gi 1390249242 1022 SSIAMsataVGRTFSytpSYAKAKISAAR 1050
Cdd:cd18548 270 MSLMM----LSMVFV---MLPRASASAKR 291
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1086-1244 |
3.58e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRpdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSiqllerFY------DPDQGTVMIDGHDSKKVNVqFLRSNIGI- 1158
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1159 -VSQEPVLF-DCSIMDNIkygdntkeisveRAIA------AAKQAQ-----LHDFvmslpekyetnvGIQ------GSQL 1219
Cdd:COG1137 82 yLPQEASIFrKLTVEDNI------------LAVLelrklsKKEREErleelLEEF------------GIThlrkskAYSL 137
|
170 180
....*....|....*....|....*
gi 1390249242 1220 SRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDE 162
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
141-360 |
4.42e-14 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 74.40 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 141 FSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSdDINKIDEAIADQM-AL 219
Cdd:cd18570 44 ISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTiSL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 220 FLQRLSTALSGLLLGFYrGWKLTLVILAVSPLIgigaAVIGLSVAKF----TELELKAYAKAGSIADEVLSSIRTVAAFG 295
Cdd:cd18570 123 FLDLLMVIISGIILFFY-NWKLFLITLLIIPLY----ILIILLFNKPfkkkNREVMESNAELNSYLIESLKGIETIKSLN 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 296 GENKEVERYEKNL-----------MFAQRWGIWKGMVMGFFTgymwcliffcyALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18570 198 AEEQFLKKIEKKFskllkksfklgKLSNLQSSIKGLISLIGS-----------LLILWIGSYLVIK-GQLSLGQLI 261
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
420-590 |
5.45e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.12 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTfhyPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRDQIG 499
Cdd:PRK10851 3 IEIANIK---KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLG------REEATME----------DIVQAAKDANAYnfimalPQQFdtlvgegggqmSGG 562
Cdd:PRK10851 78 FVFQHYALFRhMTVFDNIAFGltvlprRERPNAAaikakvtqllEMVQLAHLADRY------PAQL-----------SGG 140
|
170 180
....*....|....*....|....*...
gi 1390249242 563 QKQRVAIARALIRKPKILLLDMATSALD 590
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
420-645 |
8.23e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.87 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVkilNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIrSLNIRWLRdQIG 499
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR-PIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFS-TTIAENIRLGREEatmeDIVQAAKDANAYNFIMALP--QQFdtlVGEGGGQMSGGQKQRVAIARALIRK 576
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGLKQ----DKLPKAEIASRVNEMLGLVhmQEF---AKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAH-RLSTVRSADVIIGFEHGTAVERGTHEELLE 645
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDIleRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
133-373 |
8.45e-14 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 73.73 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 133 DINSEVIKFSGIYagVGVAVLILGYfqIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEA 212
Cdd:cd18574 40 DLKKPALKLLGLY--LLQSLLTFAY--ISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 213 iadqmalFLQRLSTAL--SGLLLG-----FYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVL 285
Cdd:cd18574 116 -------FKQCVSQGLrsVTQTVGcvvslYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 286 SSIRTVAAFGGENKEVERYEKNLMFAQRWGIWKGMVMGFFTGyMWCLIFFCYALA-FWYGSRLVlDEGEYTPGTLIQiFL 364
Cdd:cd18574 189 GNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQG-LSNLALNGIVLGvLYYGGSLV-SRGELTAGDLMS-FL 265
|
....*....
gi 1390249242 365 cviIAAMNI 373
Cdd:cd18574 266 ---VATQTI 271
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1094-1298 |
8.56e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 8.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMidghdSKKVNVQFLRSNIGIVSQEPVLFDC-SIMD 1172
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPWkKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYGdnTKEISVERAIAAAKQAQLHDFVMSLPekyetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:PRK11247 101 NVGLG--LKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1390249242 1253 SEKTVQLALDK--AREGRTCIVIAHRLstiqnSDIIAVMSQGVVIEKG 1298
Cdd:PRK11247 168 TRIEMQDLIESlwQQHGFTVLLVTHDV-----SEAVAMADRVLLIEEG 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
429-624 |
8.72e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 429 YPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDirslnirwlrdQIGIVEQ---EP 505
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 506 VLFSTTIAENIRLGR-------EEATMED--IVQAAKDANAynfIMAL-PQQFDTLvgegggqmSGGQKQRVAIARALIR 575
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwRRLTRDDraAVDDALERVG---LADLaGRQLGEL--------SGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 576 KPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRSAD 624
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
420-633 |
9.84e-14 |
|
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: 69.78 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLdGHDIRslnirwlrdqIG 499
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQepvlFSttiaenirlGREEAtmedivqaakdanaynfimalpqqfdtlvgegggqmsggqkqRVAIARALIRKPKI 579
Cdd:cd03221 67 YFEQ----LS---------GGEKM------------------------------------------RLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQhgHTIISVAH-R--LSTVrsADVIIGFEHGT 633
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1089-1298 |
1.02e-13 |
|
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: 71.79 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSkkvnvQFLRSNIGIvsqEPVLfdc 1168
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGGF---NPEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIK-----YGDNTKEI-SVERAIAAAkqAQLHDFvMSLPEKyetnvgiqgsQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:cd03220 100 TGRENIYlngrlLGLSRKEIdEKIDEIIEF--SELGDF-IDLPVK----------TYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1243 DEATSALDTE-SEKTVQLALDKAREGRTCIVIAHRLSTIQNsdiiaVMSQGVVIEKG 1298
Cdd:cd03220 167 DEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKR-----LCDRALVLEKG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
420-615 |
1.03e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHY-PSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRW---LR 495
Cdd:PRK10584 7 VEVHHLKKSVgQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 DQ-IGIVEQEPVLFSTTIA-ENIRL-----GREEAtmedivQAAKDANAYNFIMALPQQFDTLvgegGGQMSGGQKQRVA 568
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTLNAlENVELpallrGESSR------QSRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQG---ALNKiQHGHTIISVAH 615
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNR-EHGTTLILVTH 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1092-1306 |
1.10e-13 |
|
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: 71.02 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGTVMIDGHDSKKVNVQfLRSNIGI--VSQEPVlfd 1167
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 csimdnikygdntkeisverAIAAAKqaqLHDFVMSLpekyetNVGiqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:cd03217 88 --------------------EIPGVK---NADFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1248 ALDTESEKTVQLALDKAR-EGRTCIVIAH--RLSTIQNSDIIAVMSQGVVIEKGThKKLMDQ 1306
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
418-644 |
1.12e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.12 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYPSRP--EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI-----RSLN 490
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 491 IRWLRDQIGIVEQEP--VLFSTTIAENIRLGREEATmEDIVQAAKDANAYNFIMALPQQFdtlVGEGGGQMSGGQKQRVA 568
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQG---ALNKiQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINlfeRLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
437-652 |
1.13e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.99 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWlRDqIGIVEQEPVLFS-TTIAEN 515
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFPhMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 516 I-----RLGREEatmEDIVQAAKDANAY-----------NFIMALPQQfdtlvgegggqmsggqkqRVAIARALIRKPKI 579
Cdd:PRK11432 99 VgyglkMLGVPK---EERKQRVKEALELvdlagfedryvDQISGGQQQ------------------RVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 580 LLLDMATSALDNESEAKVQGALNKIQHGHTIIS--VAHRLSTVRS-ADVIIGFEHGTAVERGTHEELLERKGVYFM 652
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSlyVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPASRFM 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
420-616 |
1.18e-13 |
|
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: 70.26 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPS-RPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVtldghdirslnIRWLRDQI 498
Cdd:cd03223 1 IELENLSLATPDgRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFSTTIAENIrlgreeatmedivqaakdanAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIR 575
Cdd:cd03223 67 LFLPQRPYLPLGTLREQL--------------------IYPWDDVLSggeQQ------------------RLAFARLLLH 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390249242 576 KPKILLLDMATSALDNESEAKVQGALNkiQHGHTIISVAHR 616
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
433-626 |
1.80e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 433 PEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdPC---EGMVTLDGHDIRSLNIR-WLRDQIGIVEQEPVLF 508
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 ST-TIAENIRLGRE--------EATM----EDIVQAAK-DANAYNFIMALP---QQFdtlvgegggqmsggqkqrVAIAR 571
Cdd:PRK13549 95 KElSVLENIFLGNEitpggimdYDAMylraQKLLAQLKlDINPATPVGNLGlgqQQL------------------VEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 572 ALIRKPKILLLDMATSALdNESEAKVqgALNKIQ----HGHTIISVAHRLSTVRS-ADVI 626
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAV--LLDIIRdlkaHGIACIYISHKLNEVKAiSDTI 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
420-620 |
2.60e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVK-ILNNLSMVIKPGETTAFVGSSGAGKSTALQ-LIQRFYD-PCEGMVTLDGhdiRSLNIRWLRd 496
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILING---RPLDKNFQR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVLFST-TIAENIRLgreeatmedivqaakdaNAYNFIMALPQQfdtlvgegggqmsggqkQRVAIARALIR 575
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRF-----------------SALLRGLSVEQR-----------------KRLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390249242 576 KPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV 620
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1092-1298 |
2.86e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsKKVN-VQFLRSNIGIVSQEPVLF-DCS 1169
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNdVPPAERGVGMVFQSYALYpHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNIKYG-----DNTKEISvERAIAAAKQAQLHDFVMSLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK11000 92 VAENMSFGlklagAKKEEIN-QRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1245 ATSALDteSEKTVQLALDKA----REGRTCIVIAH-RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:PRK11000 160 PLSNLD--AALRVQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
136-366 |
3.05e-13 |
|
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: 72.10 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 136 SEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEaiad 215
Cdd:cd18549 39 RLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 216 qMA------LFLQRLSTALSGLLLgFYRGWKLTLVILAVSPLIGIGAAVIGLsvaKFTELELKAYAKAGSIADEV---LS 286
Cdd:cd18549 115 -LAhhgpedLFISIITIIGSFIIL-LTINVPLTLIVFALLPLMIIFTIYFNK---KMKKAFRRVREKIGEINAQLedsLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 287 SIRTVAAFGGENKEVERYEK-NLMF--AQRWGIWkgmVMGFFTGYMWCLIFFCYALAFWYGSRLVLdEGEYTPGTLIQIF 363
Cdd:cd18549 190 GIRVVKAFANEEYEIEKFDEgNDRFleSKKKAYK---AMAYFFSGMNFFTNLLNLVVLVAGGYFII-KGEITLGDLVAFL 265
|
...
gi 1390249242 364 LCV 366
Cdd:cd18549 266 LYV 268
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-644 |
3.37e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.23 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRF---YDP---CEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFS- 509
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 510 TTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSAL 589
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 590 DNESEAKVQGALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
434-633 |
3.41e-13 |
|
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: 70.54 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEG------------MVTLDGHDIrsLNIRwlRDQIGIV 501
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsilvrhdggwvdLAQASPREI--LALR--RRTIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 502 EQepvlFSTTI---------AEN-IRLGREEATMEDIvqaAKDANAYnfiMALP---------------QQfdtlvgegg 556
Cdd:COG4778 99 SQ----FLRVIprvsaldvvAEPlLERGVDREEARAR---ARELLAR---LNLPerlwdlppatfsggeQQ--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNES---------EAKVQGAlnkiqhghTIISVAHRLSTV-RSADVI 626
Cdd:COG4778 160 ---------RVNIARGFIADPPLLLLDEPTASLDAANravvvelieEAKARGT--------AIIGIFHDEEVReAVADRV 222
|
....*..
gi 1390249242 627 IGFEHGT 633
Cdd:COG4778 223 VDVTPFS 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
424-646 |
3.90e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYpSRPEVKILNNLSMVIKPGETTAFVGSSGAGKS-TALQLIqRFYDPCEGMVTLDGHDIRSLN--IRWLRDQ--- 497
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 ---------IGIVEQEPV-----LFST--TIAENIRL----GREEATME--DIVQAAKDANAYNFIMALPQQFDtlvgeg 555
Cdd:PRK10261 97 qmrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRLhqgaSREEAMVEakRMLDQVRIPEAQTILSRYPHQLS------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmsGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHT--IISVAHRLSTVRS-ADVIIGFEHG 632
Cdd:PRK10261 171 -----GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQG 245
|
250
....*....|....
gi 1390249242 633 TAVERGTHEELLER 646
Cdd:PRK10261 246 EAVETGSVEQIFHA 259
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
136-371 |
3.98e-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: 71.66 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 136 SEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIAD 215
Cdd:cd18548 36 SYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 216 QMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIG-LSVAKFTELeLKAYAKAGSIADEVLSSIRTVAAF 294
Cdd:cd18548 116 LLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMkKAIPLFKKV-QKKLDRLNRVVRENLTGIRVIRAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 295 GGENKEVERYEK-------NLMFAQRWgiwkgmvMGFFTGYMWCLIFFCYALAFWYGSRLVlDEGEYTPGTLI------- 360
Cdd:cd18548 195 NREDYEEERFDKanddltdTSLKAGRL-------MALLNPLMMLIMNLAIVAILWFGGHLI-NAGSLQVGDLVafinylm 266
|
250
....*....|.
gi 1390249242 361 QIFLCVIIAAM 371
Cdd:cd18548 267 QILMSLMMLSM 277
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1092-1299 |
4.97e-13 |
|
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: 73.30 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGTVM-----------ID------------GHDSKK 1146
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVErpskvgepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1147 VNVQF----------LRSNIGIVSQEP-VLF-DCSIMDNI-----KYGDNTKEiSVERAIAAAKQAQLHDFVMSLpekye 1209
Cdd:TIGR03269 92 EEVDFwnlsdklrrrIRKRIAIMLQRTfALYgDDTVLDNVlealeEIGYEGKE-AVGRAVDLIEMVQLSHRITHI----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1210 tnvgiqGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKA--REGRTCIVIAHRLSTIQN-SDII 1286
Cdd:TIGR03269 166 ------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKA 239
|
250
....*....|...
gi 1390249242 1287 AVMSQGVVIEKGT 1299
Cdd:TIGR03269 240 IWLENGEIKEEGT 252
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
142-360 |
5.20e-13 |
|
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: 71.34 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 142 SGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAiadqmalfl 221
Cdd:cd18545 43 ALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDL--------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 qrLSTALSGL------LLG-----FYRGWKLTLVILAVSPLIGIGAAVIG-LSVAKFTELELKAYAKAGSIAdEVLSSIR 289
Cdd:cd18545 114 --LSNGLINLipdlltLVGiviimFSLNVRLALVTLAVLPLLVLVVFLLRrRARKAWQRVRKKISNLNAYLH-ESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 290 TVAAFGGENKEVERYE---KNLMFAQRWGIwkgMVMGFFtgymWCLIFFCYALA----FWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18545 191 VIQSFAREDENEEIFDelnRENRKANMRAV---RLNALF----WPLVELISALGtalvYWYGGKLVLG-GAITVGVLV 260
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
424-647 |
6.18e-13 |
|
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: 69.86 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL-RDQIGIVE 502
Cdd:TIGR03410 5 NLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 503 QEPVLFST-TIAENIRLGREeatmediVQAAKDANAYNFIMAL-P-----------------QQfdtlvgegggqmsggq 563
Cdd:TIGR03410 82 QGREIFPRlTVEENLLTGLA-------ALPRRSRKIPDEIYELfPvlkemlgrrggdlsggqQQ---------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 564 kqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTH 640
Cdd:TIGR03410 139 --QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAG 216
|
....*..
gi 1390249242 641 EELLERK 647
Cdd:TIGR03410 217 DELDEDK 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-593 |
6.42e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 422 FHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGhDIRslnirwlrdqIGIV 501
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 502 EQEPVLFST-TIAENIRLGREE----------------ATMEDIVQAAK------DANAYNF------IMA--------L 544
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAElraleaeleeleaklaEPDEDLERLAElqeefeALGGWEAearaeeILSglgfpeedL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 545 PQQFDTL-----VgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNES 593
Cdd:COG0488 147 DRPVSELsggwrR-------------RVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1094-1299 |
7.26e-13 |
|
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: 69.48 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLF-DCSIM 1171
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDiTKLPPHERARAGIAYVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1172 DNIKYGdntkeisveRAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD- 1250
Cdd:TIGR03410 94 ENLLTG---------LAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQp 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1251 ---TESEKTVQLAldKAREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGT 1299
Cdd:TIGR03410 165 siiKDIGRVIRRL--RAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
436-644 |
8.40e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.04 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVlfsttIAEN 515
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHL-----TPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 516 I------------------RLGREEatmEDIVQAAKDANaynfimalpqQFDTLVGEGGGQMSGGQKQRVAIARALIRKP 577
Cdd:PRK11231 91 ItvrelvaygrspwlslwgRLSAED---NARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-644 |
9.16e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKS-TALQLIQRFydPCEGMVTLDGhDIR----SL------NIRWLR-DQIGIVEQE 504
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgeSLlhaseqTLRGVRgNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 505 PVL-------FSTTIAENIRL----GREEATME--------DIVQAAKDANAYnfimalPQQFDtlvgegggqmsGGQKQ 565
Cdd:PRK15134 101 PMVslnplhtLEKQLYEVLSLhrgmRREAARGEilncldrvGIRQAAKRLTDY------PHQLS-----------GGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 566 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEE 642
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAAT 243
|
..
gi 1390249242 643 LL 644
Cdd:PRK15134 244 LF 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
420-529 |
9.79e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.73 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIG 499
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110
....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLfsttiaeNIRLgreeaTMEDIV 529
Cdd:COG4604 79 ILRQENHI-------NSRL-----TVRELV 96
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-364 |
9.81e-13 |
|
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: 70.26 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 130 GLVDINSEVIKFSGIYAGVGVAVLI----LGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDD 205
Cdd:cd18778 27 DLVTIGSKSLGLLLGLALLLLGAYLlralLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVIND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 206 INKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVL 285
Cdd:cd18778 107 VANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 286 SSIRTVAAFGGENKEVER-------YEKNLMFAQRWGIWKGMVMGFFTGymwclifFCYALAFWYGSRLVLDeGEYTPGT 358
Cdd:cd18778 187 SGIREIQAFGREEEEAKRfealsrrYRKAQLRAMKLWAIFHPLMEFLTS-------LGTVLVLGFGGRLVLA-GELTIGD 258
|
....*.
gi 1390249242 359 LIQIFL 364
Cdd:cd18778 259 LVAFLL 264
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1095-1298 |
1.07e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFY--DPDQGTVMIDghdskkvNVQFLRsnigivsqepvlfDCSIMD 1172
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------DNQFGR-------------EASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1173 NIKYGDNTKEisverAIAAAKQAQLHDFVMSLpEKYetnvgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:COG2401 105 AIGRKGDFKD-----AVELLNAVGLSDAVLWL-RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1390249242 1253 SEKTVQLALDKA--REGRTCIVIAHRlstiqnSDIIAVMSQGVVIEKG 1298
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHH------YDVIDDLQPDLLIFVG 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
420-627 |
1.10e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPE-VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN----IRWL 494
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 RDQIGIVEQEPVLFS-TTIAENIRLgreEATMEDIVQAAKDANAYNFIMAL---------PQQFdtlvgegggqmSGGQK 564
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLgledrveyqPSQL-----------SGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 565 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVII 627
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1075-1303 |
1.14e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1075 QGKIDFIDCKFTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFL-- 1152
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1153 -RSNIGIVSQEPVLF-DCSIMDNIKYGdntkeisvERAIAAAKQAQLHDFVMSlpeKYETnVGIQG------SQLSRGEK 1224
Cdd:PRK11831 82 vRKRMSMLFQSGALFtDMNVFDNVAYP--------LREHTQLPAPLLHSTVMM---KLEA-VGLRGaaklmpSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1225 QRIAIARAIVRDPKILLLDEATSALDTESEKT-VQL--ALDKAReGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTH 1300
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVlVKLisELNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSA 228
|
...
gi 1390249242 1301 KKL 1303
Cdd:PRK11831 229 QAL 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
438-615 |
1.21e-12 |
|
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: 69.03 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNirwlRDQIGIVEQEPVLFSTTIAENIR 517
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 518 LG------------REEATMEDI----VQAAKDANAYNFIMALPQqfdtlvgegggqmsggqkqRVAIARALIRKPKILL 581
Cdd:TIGR01184 77 LAvdrvlpdlskseRRAIVEEHIalvgLTEAADKRPGQLSGGMKQ-------------------RVAIARALSIRPKVLL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1390249242 582 LDMATSALDNESEAKVQGALNKI--QHGHTIISVAH 615
Cdd:TIGR01184 138 LDEPFGALDALTRGNLQEELMQIweEHRVTVLMVTH 173
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
447-652 |
1.22e-12 |
|
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: 70.91 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 447 PG-ETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL----RDQIGIVEQEPVLFS-TTIAENIRLGR 520
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPhLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 521 EEATMEDiVQAAKDAnaynfIMALpQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGA 600
Cdd:TIGR02142 101 KRARPSE-RRISFER-----VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 601 LNKIqHGHT---IISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERKGVYFM 652
Cdd:TIGR02142 174 LERL-HAEFgipILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
755-982 |
1.34e-12 |
|
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: 70.12 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQILKTFSLVDKEQQR---SEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRL 831
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 832 RKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPF- 910
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLs 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 911 LALSGAVQTKMLTGFASQDKEILEKAGQItNEALSNIRTVAGIGVEGRFIKAFEvELEKSYKTAIRKANVYG 982
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYI-EEMISGQKVVKAFNREEEAIEEFD-EINEELYKASFKAQFYS 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
424-632 |
1.39e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVtLDGhdirSLNIRWLRDQIGIVEQ 503
Cdd:PRK11247 17 AVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 504 EPVLFS-TTIAENIRLG-----REEATME-DIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggqkQRVAIARALIRK 576
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGlkgqwRDAALQAlAAVGLADRANEWPAALSGGQK-----------------QRVALARALIHR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-TVRSADVIIGFEHG 632
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
162-308 |
1.41e-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: 69.81 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 162 LWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLGFYRGWKL 241
Cdd:cd18589 59 IYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKL 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 242 TLVILAVSPLIgigaavigLSVAKFT-----ELEL---KAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNL 308
Cdd:cd18589 139 ALLTALGLPLL--------LLVPKFVgkfqqSLAVqvqKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRL 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1094-1304 |
1.54e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNV-QFLRSNIGIVSQEPVLFD-CSIM 1171
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1172 DNIK-----YGDNTKEISVERAIAAAKQAQLHDFVMSLpekyetnvgiqGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK10895 97 DNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1247 SALDTESEKTVQLALDKARE-GRTCIVIAHRL-STIQNSDIIAVMSQGVVIEKGTHKKLM 1304
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
420-643 |
1.54e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.34 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPEVkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL--RDQ 497
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEP--VLFSTTIAENIRLG------REEATMEDIVQAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVAI 569
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHLS-----------GGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEEL 643
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
424-617 |
1.61e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSRPEVKILNNLSMVIKPGEttaFV---GSSGAGKSTALQLIQRFYDPCEGMVTLDGHDI-------RSlniRW 493
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRA---KY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 lrdqIGIVEQEPVL---FSTTIAENIRLgreeatmedivqAAKDANAYNFIMALPQQFDTLVgegggqmsggqkqRVAIA 570
Cdd:COG1101 82 ----IGRVFQDPMMgtaPSMTIEENLAL------------AYRRGKRRGLRRGLTKKRRELF-------------RELLA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 571 R----------------------------ALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRL 617
Cdd:COG1101 133 TlglglenrldtkvgllsggqrqalsllmATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
420-638 |
1.73e-12 |
|
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: 68.33 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPS-------------------RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVT 480
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 481 LDGhdirslNIRWLRD-QIGIveqEPVLfstTIAENIRLG-------REE--ATMEDIVQAAkdanaynfimALPQQFDT 550
Cdd:cd03220 81 VRG------RVSSLLGlGGGF---NPEL---TGRENIYLNgrllglsRKEidEKIDEIIEFS----------ELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 551 LVgeggGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGAL-NKIQHGHTIISVAHRLSTVRS-ADVIIG 628
Cdd:cd03220 139 PV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALV 214
|
250
....*....|
gi 1390249242 629 FEHGTAVERG 638
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1101-1306 |
1.78e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1101 VSVD--PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQ---------FLRSNIGIVSQEPvlfdcs 1169
Cdd:PRK11701 25 VSFDlyPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaerrrLLRTEWGFVHQHP------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 iMD----NIKYGDNTkeisVER--AIAAAKQAQLHDFVMSLPEKYEtnvgIQGSQL-------SRGEKQRIAIARAIVRD 1236
Cdd:PRK11701 99 -RDglrmQVSAGGNI----GERlmAVGARHYGDIRATAGDWLERVE----IDAARIddlpttfSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1237 PKILLLDEATSALDTesekTVQLA-LDKARE-----GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGthkkLMDQ 1306
Cdd:PRK11701 170 PRLVFMDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG----LTDQ 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
435-622 |
2.02e-12 |
|
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: 71.39 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 435 VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdPC---EGMVTLDGHDIRSLNIRWL-RDQIGIVEQEPVLF-S 509
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 510 TTIAENIRLGrEEATMEDIVQAakDANAYNFIMALPQQF---DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMAT 586
Cdd:TIGR02633 93 LSVAENIFLG-NEITLPGGRMA--YNAMYLRAKNLLRELqldADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1390249242 587 SALdneSEAKVQGALNKI----QHGHTIISVAHRLSTVRS 622
Cdd:TIGR02633 170 SSL---TEKETEILLDIIrdlkAHGVACVYISHKLNEVKA 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-645 |
2.17e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-----PCEGMVTLDGHDIRSLNIRWL 494
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 --RDQIGIVEQEPVLFS-TTIAENIRLG-------REEATMEDIVQ-AAKDAnaynfimALPQQFDTLVGEGGGQMSGGQ 563
Cdd:PRK14267 82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDERVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 564 KQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHR-LSTVRSADVIIGFEHGTAVERGTHEE 642
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
...
gi 1390249242 643 LLE 645
Cdd:PRK14267 235 VFE 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1090-1299 |
2.35e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTV-------------MIDGHDSKKVNVQFLR-SN 1155
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1156 IGIVSQEPVlfdCSIMDNIKYGDNTKE-------ISVERAIAAAKQaqLHDFVmSLPEKyETNVGIQGSQLSRGEKQRIA 1228
Cdd:PRK10261 106 MAMIFQEPM---TSLNPVFTVGEQIAEsirlhqgASREEAMVEAKR--MLDQV-RIPEA-QTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1229 IARAIVRDPKILLLDEATSALD-TESEKTVQLALDKARE-GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDvTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
434-638 |
2.64e-12 |
|
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: 67.24 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIrSLNIRWLRdQIGIVEQEPVLF-STTI 512
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALR-RIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 513 AENIRLG------REEATME--DIV--QAAKDANAYNFIMALPQqfdtlvgegggqmsggqkqRVAIARALIRKPKILLL 582
Cdd:cd03268 90 RENLRLLarllgiRKKRIDEvlDVVglKDSAKKKVKGFSLGMKQ-------------------RLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 583 DMATSALDNESEAKVQGAL-NKIQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERG 638
Cdd:cd03268 151 DEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
415-644 |
3.10e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 415 RIKGEiefhNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL 494
Cdd:PRK10253 7 RLRGE----QLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 RDQIGIVEQEPVL-FSTTIAENIRLGRE---------EATMEDIVQAAKDANAYNFIMAlpQQFDTLvgegggqmSGGQK 564
Cdd:PRK10253 80 ARRIGLLAQNATTpGDITVQELVARGRYphqplftrwRKEDEEAVTKAMQATGITHLAD--QSVDTL--------SGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 565 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHE 641
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPK 229
|
...
gi 1390249242 642 ELL 644
Cdd:PRK10253 230 EIV 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1090-1274 |
4.07e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1090 RPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVqflRSNIGIVSQ----EPVL 1165
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1166 fdcSIMDNIK-----YGdnTKEISVERAIAAAkqaQLHDfVMSLPEKYetnvgiqgsqLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:PRK13539 89 ---TVAENLEfwaafLG--GEELDIAAALEAV---GLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....
gi 1390249242 1241 LLDEATSALDTESEKTVqLALDKAREGRTCIVIA 1274
Cdd:PRK13539 150 ILDEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
436-583 |
4.48e-12 |
|
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: 67.18 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNI-RWLRDQIGIVEQEPVLF-STTIA 513
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 514 ENIRLGREEATMEDIVQAAKdanaynfIMALPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLD 583
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEK-------LEELLEEFhiTHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
435-621 |
4.57e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 435 VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwLRDQIGI--VEQEPVLF-STT 511
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 512 IAENI--RLGREEATMEDIVQAAK--------DANAYNFIMAlPQQFdtlvgegggqmsggqkqrVAIARALIRKPKILL 581
Cdd:PRK15439 103 VKENIlfGLPKRQASMQKMKQLLAalgcqldlDSSAGSLEVA-DRQI------------------VEILRGLMRDSRILI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1390249242 582 LDMATSALD-NESEA---KVQGALNKiqhGHTIISVAHRLSTVR 621
Cdd:PRK15439 164 LDEPTASLTpAETERlfsRIRELLAQ---GVGIVFISHKLPEIR 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1094-1292 |
4.91e-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: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL-ERFYDPD-QGTVMIDGhdsKKVNVQFLRSnIGIVSQEPVLFDCS-I 1170
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING---RPLDKNFQRS-TGYVEQQDVHSPNLtV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1171 MDNIKYGDNTKEISVEraiaaakqaqlhdfvmslpekyetnvgiqgsqlsrgEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:cd03232 97 REALRFSALLRGLSVE------------------------------------QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390249242 1251 TESEKTVQLALDK-AREGRTCIVIAHRLS--TIQNSDIIAVMSQG 1292
Cdd:cd03232 141 SQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
418-650 |
5.90e-12 |
|
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: 67.96 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEIEFHNVTFHYPSRPEVkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDpCEGMVTLDGHDIRSLNIRWLRDQ 497
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFSTTIAENIRlGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKP 577
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
431-644 |
5.96e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVL-FS 509
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 510 TTIAENIRLGR----------EEATMEDIVQAAKDANAYNFImalPQQFDTLvgegggqmSGGQKQRVAIARALIRKPKI 579
Cdd:PRK09536 92 FDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFA---DRPVTSL--------SGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 580 LLLDMATSALD-NESEAKVQGALNKIQHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK09536 161 LLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1097-1299 |
6.17e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.32 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1097 NGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD-----SKKVnvqflrSNIGIVS--QEPVLFdcs 1169
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpGHQI------ARMGVVRtfQHVRLF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 imdnikygdntKEISVERAIAAAKQAQLH-----------DFVMSLPEKYE------TNVGI------QGSQLSRGEKQR 1226
Cdd:PRK11300 93 -----------REMTVIENLLVAQHQQLKtglfsgllktpAFRRAESEALDraatwlERVGLlehanrQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1227 IAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKARE--GRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGT 1299
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
799-976 |
8.36e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 67.92 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 799 CLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGatgsqvgM 878
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQD-------L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 879 MVNSFTNIFVAVL-------IAFLFNWKLSLVISVFFPFLALSGAVQTKMLTGFAsqdKEILEKAGQIT---NEALSNIR 948
Cdd:cd18564 128 LVSGVLPLLTNLLtlvgmlgVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEAS---REQRRREGALAsvaQESLSAIR 204
|
170 180
....*....|....*....|....*...
gi 1390249242 949 TVAGIGVEGRFIKAFEVELEKSYKTAIR 976
Cdd:cd18564 205 VVQAFGREEHEERRFARENRKSLRAGLR 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
424-645 |
9.60e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQ 503
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 504 E-PVLFSTTIAENIRLGRE-------EATMEDiVQAAKDANAYNFIMALPQQF-DTLvgegggqmSGGQKQRVAIARALI 574
Cdd:PRK10575 93 QlPAAEGMTVRELVAIGRYpwhgalgRFGAAD-REKVEEAISLVGLKPLAHRLvDSL--------SGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 575 RKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELLE 645
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
824-1012 |
1.22e-11 |
|
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: 67.18 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 824 GELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLV 903
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 904 ISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSyktaiRKANVY-G 982
Cdd:cd18574 148 LLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA-----AKLNEKlG 222
|
170 180 190
....*....|....*....|....*....|....
gi 1390249242 983 LCYAFSQGISFLA-NS---AAYRYGGYLIVYEDL 1012
Cdd:cd18574 223 LGIGIFQGLSNLAlNGivlGVLYYGGSLVSRGEL 256
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
420-679 |
1.31e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.06 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRslniRWLRDQIG 499
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLF-STTIAENIR-------LGREEAT------ME--DIVQAAKDA-------NaynfimalpQQfdtlvgegg 556
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVylarlkgLSKAEAKrradewLErlGLGDRANKKveelskgN---------QQ--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 557 gqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGAL-NKIQHGHTIISVAHRLSTV-RSAD--VIIGfeHG 632
Cdd:COG4152 137 ---------KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDriVIIN--KG 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1390249242 633 TAVERGTHEELLERKGVYFMLVTLQSQEDNTHKETGIKGKDTTEGDT 679
Cdd:COG4152 206 RKVLSGSVDEIRRQFGRNTLRLEADGDAGWLRALPGVTVVEEDGDGA 252
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
432-590 |
1.42e-11 |
|
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: 65.76 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 432 RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLI---QRFYDPCEGMVTLDGhdiRSLNIRWLRDQIGIVEQEPVLF 508
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 ST-TIAE------NIRLGREeatMEDIVQAAKDAnaynfIMALPQQFDTLVGEGGGQMSGG-QKQRVAIARALIRKPKIL 580
Cdd:cd03234 94 PGlTVREtltytaILRLPRK---SSDAIRKKRVE-----DVLLRDLALTRIGGNLVKGISGgERRRVSIAVQLLWDPKVL 165
|
170
....*....|
gi 1390249242 581 LLDMATSALD 590
Cdd:cd03234 166 ILDEPTSGLD 175
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1078-1275 |
1.55e-11 |
|
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: 63.24 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDghdsKKVNVQFLrsnig 1157
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 ivsqepvlfdcsimdnikygdntkeisveraiaaakqaqlhdfvmslpekyetnvgiqgSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03221 69 -----------------------------------------------------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALdKAREGrTCIVIAH 1275
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
432-618 |
1.76e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 432 RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQrFYDP----CEGMVTLDGHDIrslNIRWLRDQIGIVEQEPVL 507
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 508 FST-TIAENI------RLGREEAT------MEDIVQAAKDANAYNFIMALPQQFDTLvgegggqmSGGQKQRVAIARALI 574
Cdd:TIGR00955 111 IPTlTVREHLmfqahlRMPRRVTKkekrerVDEVLQALGLRKCANTRIGVPGRVKGL--------SGGERKRLAFASELL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390249242 575 RKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLS 618
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPS 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1089-1306 |
1.78e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsKKVNV----QFLRSNIGIVSQE-P 1163
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFksskEALENGISMVHQElN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 VLFDCSIMDNIKYGD-NTKEISVEraiaaakQAQLHDFVMSLPEKYETNVG--IQGSQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:PRK10982 84 LVLQRSVMDNMWLGRyPTKGMFVD-------QDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1241 LLDEATSALdteSEKTVQ---LALDKAREgRTC--IVIAHRLSTI-QNSDIIAVMSQGVVIEKGTHKKL-MDQ 1306
Cdd:PRK10982 157 IMDEPTSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQWIATQPLAGLtMDK 225
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
143-314 |
2.09e-11 |
|
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: 66.34 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQ 222
Cdd:cd18606 39 GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 223 RLSTALSGLLLgfyrgwkltlvILAVSPLIGIGAAVIGL---SVAKF---TELELK---------AYAKAGsiadEVLSS 287
Cdd:cd18606 119 TLSSIIGTFIL-----------IIIYLPWFAIALPPLLVlyyFIANYyraSSRELKrlesilrsfVYANFS----ESLSG 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1390249242 288 IRTVAAFGGENKEVERYEKN---------LMFA-QRW 314
Cdd:cd18606 184 LSTIRAYGAQDRFIKKNEKLidnmnrayfLTIAnQRW 220
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
143-339 |
2.11e-11 |
|
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: 66.37 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGArqIRKMRKFY---FRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMAL 219
Cdd:cd18580 42 GVYAALLVLASVLLVLLRWLLFVLAG--LRASRRLHdklLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 220 FLQRLSTALSGLllgfyrgwkltLVILAVSPLIGIGAAVIGLSVA-------------KFTELELKA--YakagSIADEV 284
Cdd:cd18580 120 FLQSLFSVLGSL-----------IVIAIVSPYFLIVLPPLLVVYYllqryylrtsrqlRRLESESRSplY----SHFSET 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 285 LSSIRTVAAFGGENKEVERYEKNL----------MFAQRW-GIWKGMVMGFFTGymwCLIFFCYAL 339
Cdd:cd18580 185 LSGLSTIRAFGWQERFIEENLRLLdasqrafyllLAVQRWlGLRLDLLGALLAL---VVALLAVLL 247
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
420-590 |
2.11e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.04 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYP-SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlRdqi 498
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFS-TTIAENIRLG----------REEATMEDIVQAAKDANAYNFIMALP---QQfdtlvgegggqmsggqk 564
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlrgvpkaeRRARAEELLALVGLADFARRRIWQLSggmRQ----------------- 141
|
170 180
....*....|....*....|....*.
gi 1390249242 565 qRVAIARALIRKPKILLLDMATSALD 590
Cdd:COG4525 142 -RVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
431-638 |
3.08e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwLRDQ--IGIVEQE-PVL 507
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 508 FSTTIAENIRLGR---EEATMEDIVQAAK---DANAYNFIMALPQQFDTLVGEGGGQMSGGqkqrVAIARALIRKPKILL 581
Cdd:PRK09700 93 DELTVLENLYIGRhltKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVANLSISHKQM----LEIAKTLMLDAKVII 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 582 LDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERG 638
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1096-1298 |
3.28e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVnvqfLRSN-IGIVSQE-------PVLFD 1167
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 CSIMDNiKYGD-----NTKEISVERAIAAAKQAQLHDFvmslpeKYEtnvgiQGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK15056 99 DVVMMG-RYGHmgwlrRAKKRDRQIVTAALARVDMVEF------RHR-----QIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1243 DEATSALDTESEKTVQLALDKAR-EGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
800-976 |
3.36e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 65.61 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 800 LFFVILGCV-----SLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQG-ATG 873
Cdd:cd18563 42 LLLLVLGLAgayvlSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLSD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 874 SQVGMMVNSFTNIFVAVLIaFLFNWKLSLVISVFFPFLA-LSGAVQTKMLTGFASQDKeileKAGQIT---NEALSNIRT 949
Cdd:cd18563 120 GLPDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVwGSYFFWKKIRRLFHRQWR----RWSRLNsvlNDTLPGIRV 194
|
170 180
....*....|....*....|....*..
gi 1390249242 950 VAGIGVEGRFIKAFEVELEKSYKTAIR 976
Cdd:cd18563 195 VKAFGQEKREIKRFDEANQELLDANIR 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1082-1304 |
3.45e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1082 DCKFTYPSRpdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH-----DSKKvnvqFLRSNI 1156
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswSSKA----FARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1157 GIVSQEPVLFDCSIMDNI------------KYGDNTKEiSVERAIAAAKQAQL-HDFVMSLpekyetnvgiqgsqlSRGE 1223
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVaigrypwhgalgRFGAADRE-KVEEAISLVGLKPLaHRLVDSL---------------SGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1224 KQRIAIARAIVRDPKILLLDEATSALDTESEKTVqLALDK--ARE-GRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGT 1299
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV-LALVHrlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGT 231
|
....*
gi 1390249242 1300 HKKLM 1304
Cdd:PRK10575 232 PAELM 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1091-1296 |
3.53e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGTVMIDG--------HDSKKVNvqflrsnIGIV 1159
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfkdiRDSEALG-------IVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQE----PVLfdcSIMDNIKYGDNTKE---ISVERAIAAAKQaqLHDFVmSLPEKYETNVgiqgSQLSRGEKQRIAIARA 1232
Cdd:NF040905 84 HQElaliPYL---SIAENIFLGNERAKrgvIDWNETNRRARE--LLAKV-GLDESPDTLV----TDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1233 IVRDPKILLLDEATSAL-DTESEKTVQLALDKAREGRTCIVIAHRLSTI-QNSDIIAVMSQGVVIE 1296
Cdd:NF040905 154 LSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
420-646 |
3.59e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYP-------------------SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVT 480
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 481 LDGhdirslNIRWLrdqIGiveqepvlFST------TIAENIRLG-------REE--ATMEDIVQAA--KDanaynFI-- 541
Cdd:COG1134 85 VNG------RVSAL---LE--------LGAgfhpelTGRENIYLNgrllglsRKEidEKFDEIVEFAelGD-----FIdq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 542 --------MALpqqfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALN-KIQHGHTIIS 612
Cdd:COG1134 143 pvktyssgMRA---------------------RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIReLRESGRTVIF 201
|
250 260 270
....*....|....*....|....*....|....*
gi 1390249242 613 VAHRLSTVRS-ADVIIGFEHGTAVERGTHEELLER 646
Cdd:COG1134 202 VSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1105-1297 |
3.73e-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: 62.39 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1105 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIdghdskkvnvqflrsnigivsqepvlfdcsimdnikygdntkeIS 1184
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------------------------------------------ID 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1185 VERAIAAAKQAQLHDFVmslpekyetnvGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALD-- 1262
Cdd:smart00382 38 GEDILEEVLDQLLLIIV-----------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|....*....
gi 1390249242 1263 ----KAREGRTCIVIAHRLSTIQNSDIIAVMSQGVVIEK 1297
Cdd:smart00382 107 llllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
146-360 |
3.89e-11 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 65.58 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 146 AGVGVAVLILGYFQiRLWVITGARQI-RKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIAdqMALFL-QR 223
Cdd:cd18543 46 LALGVAEAVLSFLR-RYLAGRLSLGVeHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA--FGPFLlGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 224 LSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAvigLSVAKFTELELKAYAKAG---SIADEVLSSIRTVAAFGGENKE 300
Cdd:cd18543 123 LLTLVVGLVVMLVLSPPLALVALASLPPLVLVAR---RFRRRYFPASRRAQDQAGdlaTVVEESVTGIRVVKAFGRERRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 301 VERYEK--NLMFAQRwgIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18543 200 LDRFEAaaRRLRATR--LRAARLRARFWPLLEALPELGLAAVLALGGWLVAN-GSLTLGTLV 258
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
420-645 |
4.68e-11 |
|
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: 67.13 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPS--RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMV-----------TLDGHDI 486
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 487 RSLNIRWlrdqIGIVEQEPVLFS-TTIAENI----------RLGREEATMEDIVQAAKDANAYNFIMALPQQFDtlvgeg 555
Cdd:TIGR03269 360 RGRAKRY----IGILHQEYDLYPhRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPDELS------ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmsGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNK--IQHGHTIISVAHRLSTVRS-ADVIIGFEHG 632
Cdd:TIGR03269 430 -----EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDG 504
|
250
....*....|...
gi 1390249242 633 TAVERGTHEELLE 645
Cdd:TIGR03269 505 KIVKIGDPEEIVE 517
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1089-1293 |
4.76e-11 |
|
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: 63.67 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDC 1168
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKY--GDNTKEiSVERAIAAAKQAQLHDfvmslpekyetnvgIQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03231 89 SVLENLRFwhADHSDE-QVEEALARVGLNGFED--------------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249242 1247 SALDTESEK--TVQLALDKAREGrtCIVIAHRLSTIQNSDIIAVMSQGV 1293
Cdd:cd03231 154 TALDKAGVArfAEAMAGHCARGG--MVVLTTHQDLGLSEAGARELDLGF 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
421-643 |
5.05e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 421 EFHNVTFHYPSrpeVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIR-WLRDQIG 499
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQE----PVLfstTIAENIRLGR--EEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGqkqrVAIARAL 573
Cdd:PRK11288 83 IIYQElhlvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQM----VEIAKAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 574 IRKPKILLLDMATSALD-NESEA--KVQGALNKiqHGHTIISVAHRLSTV-RSADVIIGFEHGTAVErgTHEEL 643
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSaREIEQlfRVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
420-647 |
5.65e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIG 499
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVL-FSTTIAENIRL-GRE--------EATMEDIVQAAKdanaynfimaLPQQFDTLVGEGGGQMSGgqkqRVAI 569
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVfGRYfgmstreiEAVIPSLLEFAR----------LESKADARVSDLSGGMKR----RLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
419-643 |
5.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHYPSRP--EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSL------- 489
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 490 -----------------NIRWLRDQIGIVEQ--EPVLFSTTIAENIRLGREEATMEDiVQAAKDANAYNFIMALPQQFdt 550
Cdd:PRK13651 82 kvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 551 lVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIG 628
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*.
gi 1390249242 629 FEHGTAVERG-THEEL 643
Cdd:PRK13651 238 FKDGKIIKDGdTYDIL 253
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
146-369 |
5.87e-11 |
|
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: 64.91 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 146 AGVGVAVLILGYFQI---RLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDdINKIDEAIADQMALFLQ 222
Cdd:cd18566 46 IGVVIAILLESLLRLlrsYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 223 RLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVE 302
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLR 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 303 RYE----KNLMFAQRWGIWKGMVMGFFTGYMWCLIFfcyaLAFWYGSRLVLDeGEYTPGTLIQiflCVIIA 369
Cdd:cd18566 205 RYErlqaNAAYAGFKVAKINAVAQTLGQLFSQVSMV----AVVAFGALLVIN-GDLTVGALIA---CTMLS 267
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1092-1298 |
6.10e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.20 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGTVMIDGHDSKKVNVQ------------------- 1150
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPDeraraglflafqypeeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1151 -----FLRSNIGIVSQEPVLFDCSIMDNIKygdntkEISVERAIAAAKQAQLHDFVmslpekyetNVGIQGsqlsrGEKQ 1225
Cdd:TIGR01978 92 vsnleFLRSALNARRSARGEEPLDLLDFEK------LLKEKLALLDMDEEFLNRSV---------NEGFSG-----GEKK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAR-EGRTCIVIAH--RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:TIGR01978 152 RNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1094-1277 |
6.18e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.36 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMidgHDSKkvnvqfLRsnIGIVSQEPVLfdcsimdn 1173
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGK------LR--IGYVPQKLYL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 ikygDNTKEISVER---------------AIAAAKQAQLHDFVMSlpekyetnvgiqgsQLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK09544 79 ----DTTLPLTVNRflrlrpgtkkedilpALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390249242 1239 ILLLDEATSALDTESektvQLAL----DKAREGRTCIV--IAHRL 1277
Cdd:PRK09544 141 LLVLDEPTQGVDVNG----QVALydliDQLRRELDCAVlmVSHDL 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1095-1289 |
6.24e-11 |
|
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: 64.31 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVsVDPGQTLAFVGSSGCGKSTSIQLLE--------RFYDPD---------QGTV-------MIDGHDSKKVNVQ 1150
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPdwdeildefRGSElqnyftkLLEGDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1151 FlrsnigiVSQEPVLFDCSIMDNIKYGD--NTKEISVERaiaaakqaqlhdfvMSLPEKYETNVgiqgSQLSRGEKQRIA 1228
Cdd:cd03236 95 Y-------VDLIPKAVKGKVGELLKKKDerGKLDELVDQ--------------LELRHVLDRNI----DQLSGGELQRVA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1229 IARAIVRDPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVM 1289
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQRLNAaRLIRELAEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
755-1008 |
6.90e-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: 64.81 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSLLFSQIlktfslVDK---EQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRL 831
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREI------IDDalpQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 832 RKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTnIFVAVLIA-FLFNWKLSLVISVFFPF 910
Cdd:cd18550 75 RVQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV-TLVATLVAmLALDWRLALLSLVLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 911 LALSGAVQTKMLTGFASQDKEILEKAGQITNEALSnirtVAGI------GVEGRFIKAFEVELEKSYKTAIRkANVYGlc 984
Cdd:cd18550 152 FVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLS----VSGAllvklfGREDDEAARFARRSRELRDLGVR-QALAG-- 224
|
250 260
....*....|....*....|....*..
gi 1390249242 985 YAFSQGISFLANSAA---YRYGGYLIV 1008
Cdd:cd18550 225 RWFFAALGLFTAIGPalvYWVGGLLVI 251
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1095-1292 |
8.45e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLE-RFYDPD-QGTVMIDGhdsKKVNVQFLRsNIGIVSQEPVLFD----- 1167
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 -----CSIMDNIKYGDNTKEISV-ERAIAAAKQAQLHDFVMSlpekyetNVGIQGsqLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PLN03211 159 etlvfCSLLRLPKSLTKQEKILVaESVISELGLTKCENTIIG-------NSFIRG--ISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1242 LDEATSALD-TESEKTVQLALDKAREGRTCIVIAHRLST--IQNSDIIAVMSQG 1292
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
147-360 |
9.08e-11 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 64.49 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 147 GVGVAVLILGYF---QIRLWVITGAR---QIRKMRKFyFRRIMRMEIGWFDCTSVGELNSRFSDdINKIDEAIADQMalf 220
Cdd:cd18779 45 GLGLAALVLTQLlagLLRSHLLLRLRtrlDTQLTLGF-LEHLLRLPYRFFQQRSTGDLLMRLSS-NATIRELLTSQT--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 221 lqrLSTALSGLLLGFYrgwklTLVILAVSPL-----IGIGAAVIGLSVAKF------TELELKAYAKAGSIADEVLSSIR 289
Cdd:cd18779 120 ---LSALLDGTLVLGY-----LALLFAQSPLlglvvLGLAALQVALLLATRrrvrelMARELAAQAEAQSYLVEALSGIE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 290 TVAAFGGENKEVERYEkNLMFAQ-RWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18779 192 TLKASGAEDRALDRWS-NLFVDQlNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLD-GQLSLGTML 261
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1095-1304 |
1.05e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FDCSIMDN 1173
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1174 IKYGDNTKEISVER-------AIAAAKQAqlhdfvMSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK10253 102 VARGRYPHQPLFTRwrkedeeAVTKAMQA------TGITHLADQSV----DTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1247 SALDTESE-KTVQLALDKARE-GRTCIVIAHRLSTI--QNSDIIAvMSQGVVIEKGTHKKLM 1304
Cdd:PRK10253 172 TWLDISHQiDLLELLSELNREkGYTLAAVLHDLNQAcrYASHLIA-LREGKIVAQGAPKEIV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
451-646 |
1.23e-10 |
|
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: 64.74 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 451 TAFVGSSGAGKSTALQLI---QRfydPCEGMVTLDGH---DIRSLniRWL---RDQIGIVEQEPVLFST-TIAENIRLGR 520
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPHlSVRGNLLYGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 521 EeatmedivQAAKDANAYNF--IMAL----------P-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILL 581
Cdd:COG4148 103 K--------RAPRAERRISFdeVVELlgighlldrrPatlsggeRQ------------------RVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 582 LDMATSALDNESEAKVQGALNKIqHGHT---IISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLER 646
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERL-RDELdipILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1094-1307 |
1.47e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQG----------TVMIDGHDSKkvNVQFLRSNIGIVSQEP 1163
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLAR--DIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 VLFD-CSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLpekyeTNVGI------QGSQLSRGEKQRIAIARAIVRD 1236
Cdd:PRK09984 96 NLVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGMvhfahqRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1237 PKILLLDEATSALDTESEKTVQLALD--KAREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGTHKKLMDQK 1307
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
142-366 |
1.57e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 63.66 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 142 SGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDInkideaiaDQMALFL 221
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDI--------DALSELL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 QR-LSTALSGLL--LG-----FYRGWKLTLVILAVSPLIGIGAAViglsvakFTELELKAYAKA-GSIAD------EVLS 286
Cdd:cd18546 114 QTgLVQLVVSLLtlVGiavvlLVLDPRLALVALAALPPLALATRW-------FRRRSSRAYRRArERIAAvnadlqETLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 287 SIRTVAAFGGE-------NKEVERYEKNLMFAQRwgiwkgmVMGFFTGYMWCLIFFCYALAFWYGSRLVLDeGEYTPGTL 359
Cdd:cd18546 187 GIRVVQAFRRErrnaerfAELSDDYRDARLRAQR-------LVAIYFPGVELLGNLATAAVLLVGAWRVAA-GTLTVGVL 258
|
....*..
gi 1390249242 360 IQIFLCV 366
Cdd:cd18546 259 VAFLLYL 265
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
434-650 |
1.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLD----GHDIRSL------------NIRWLRDQ 497
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEP--VLFSTTIAENIRLGrEEATMEDIVQAAKDANAYNFIMALPQQFdtlVGEGGGQMSGGQKQRVAIARALIR 575
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 576 KPKILLLDMATSALDNESEAK-VQGALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
433-636 |
2.08e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 433 PEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdPC---EGMVTLDG-----HDIRSlnirwlRDQIGIV--E 502
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRD------SEALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 503 QE----PVLfstTIAENIRLGREEATM------EDIVQAAK-------DANAYNFIMAL---PQQFdtlvgegggqmsgg 562
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNERAKRgvidwnETNRRAREllakvglDESPDTLVTDIgvgKQQL-------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 563 qkqrVAIARALIRKPKILLLDMATSAL-DNESEAKVQGALNKIQHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVE 636
Cdd:NF040905 148 ----VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
439-643 |
2.47e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.70 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 439 NNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSL---------------NIRWLRdQIGIVEQ 503
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFR-EMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 504 EPV-------------LFSTTI---AENIRLGREeATMEDIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggqkQRV 567
Cdd:PRK11300 101 LLVaqhqqlktglfsgLLKTPAfrrAESEALDRA-ATWLERVGLLEHANRQAGNLAYGQQ-----------------RRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 568 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHGTAVERGTHEEL 643
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
755-1007 |
2.84e-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: 62.85 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPIYSllfsQILKTFSLVDKEQQRseIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKF 834
Cdd:cd18570 7 ILLLSLLITLLGIAGSFFF----QILIDDIIPSGDINL--LNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 835 GFKAMLRQDIGWFDDLKNnpGVLTTRLaTDASQVQGA-TGSQVGMMVNSFTNIFVAVLIaFLFNWKLSLVISVFFPFLAL 913
Cdd:cd18570 81 YFKHLLKLPLSFFETRKT--GEIISRF-NDANKIREAiSSTTISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 914 SGAVQTKMltgFASQDKEILEKAGQIT---NEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQG 990
Cdd:cd18570 157 IILLFNKP---FKKKNREVMESNAELNsylIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
250
....*....|....*..
gi 1390249242 991 ISFLANSAAYRYGGYLI 1007
Cdd:cd18570 234 ISLIGSLLILWIGSYLV 250
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
420-649 |
3.41e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.82 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNI-RWLRDQI 498
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFS-TTIAENIRLGREEATMEDIVQaaKDANAYNFimaLPQQFDTLVGEGGGQMSGGQkQRVAIARALIRKP 577
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAGTMSGGEQ-QMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 578 KILLLDMATSALdneSEAKVQGALNKIQH----GHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELLERKGV 649
Cdd:PRK11614 157 RLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
143-508 |
3.78e-10 |
|
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: 64.05 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILG-YFQIRLwVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIAdQMALFL 221
Cdd:COG4615 52 LLFAGLLVLLLLSRlASQLLL-TRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 QRLSTALSGLLLGFYRGWKLTLVILAVsplIGIGAAVIGLSVAKFteleLKAYAKAGSIADEVLSSIRTVaaFGGeNKEV 301
Cdd:COG4615 130 QSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLVRRA----RRHLRRAREAEDRLFKHFRAL--LEG-FKEL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 302 -------------------ERYEKNLMFAQRWgiwkgmvmgFFTGYMW--CLIFFCYALAFWYGSRLvldeGEYTPGTLI 360
Cdd:COG4615 200 klnrrrrraffdedlqptaERYRDLRIRADTI---------FALANNWgnLLFFALIGLILFLLPAL----GWADPAVLS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 361 QIFLCVIIAAMNIGNASSCLEIFSTGCSAASSIfQTIDRQ-----PVMDCMSGDGYKLDRikGEIEFHNVTFHYPSRPEV 435
Cdd:COG4615 267 GFVLVLLFLRGPLSQLVGALPTLSRANVALRKI-EELELAlaaaePAAADAAAPPAPADF--QTLELRGVTYRYPGEDGD 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 436 K--ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLF 508
Cdd:COG4615 344 EgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF 418
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
437-618 |
4.12e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRW---LRDQ-IGIVEQ-EPVLFSTT 511
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 512 IAENIrlgreeaTMEDIVQAAKDANAYN--FIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSAL 589
Cdd:PRK11629 104 ALENV-------AMPLLIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|..
gi 1390249242 590 DN---ESEAKVQGALNkIQHGHTIISVAHRLS 618
Cdd:PRK11629 177 DArnaDSIFQLLGELN-RLQGTAFLVVTHDLQ 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
437-643 |
4.83e-10 |
|
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: 62.18 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLrdqigiveqepvlFSTTIAENI 516
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWI-------------MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 517 RLG--REEATMEDIVQAAKDANAynfIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESE 594
Cdd:cd03291 119 IFGvsYDEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 595 AKV-QGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGTHEEL 643
Cdd:cd03291 196 KEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-644 |
5.04e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGM-----VTLDGHDIRSL-NIRWLRDQIGIVEQEPVLFST 510
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 511 TIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALD 590
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 591 NESEAKVQGALNKIQHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
760-1015 |
5.56e-10 |
|
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: 62.08 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 760 LCAAINGAVTPIYSLLFSQILKTFsLVDKEQQRseIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAM 839
Cdd:cd18549 9 FCAVLIAALDLVFPLIVRYIIDDL-LPSKNLRL--ILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 840 LRQDIGWFDdlKNNPGVLTTRLATDASQVqgatgSQV-----GMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALS 914
Cdd:cd18549 86 QKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELahhgpEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 915 GAVQT-KMLTGFASQDKEILEKAGQITNealsnirTVAGIgvegRFIKAF---EVELEK------SYKTAirKANVYGLC 984
Cdd:cd18549 159 TIYFNkKMKKAFRRVREKIGEINAQLED-------SLSGI----RVVKAFaneEYEIEKfdegndRFLES--KKKAYKAM 225
|
250 260 270
....*....|....*....|....*....|....
gi 1390249242 985 YAFSQGISFLANS---AAYRYGGYLIVYEDLNFS 1015
Cdd:cd18549 226 AYFFSGMNFFTNLlnlVVLVAGGYFIIKGEITLG 259
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1092-1299 |
6.46e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLlerfydpdqgtvmIDGHDSKKV---NVQF-----------LRSNIG 1157
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV-------------IAGHPAYKIlegDILFkgesildlepeERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 I--VSQEPV-LFDCSIMDNIKYGDNTKEisveraiaaaKQAQLHD-----FVMSLPEKYETnVGIQGSQLSR-------- 1221
Cdd:CHL00131 86 IflAFQYPIeIPGVSNADFLRLAYNSKR----------KFQGLPEldpleFLEIINEKLKL-VGMDPSFLSRnvnegfsg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1222 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIV-IAH--RLSTIQNSDIIAVMSQGVVIEKG 1298
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
.
gi 1390249242 1299 T 1299
Cdd:CHL00131 235 D 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
431-617 |
6.52e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ-IGIVEQEPVLFS 509
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 510 T-TIAENIRLGREEATMEDIVQAAK---DANAYNFIMALPQQFDTLVGEGGGQMSGGqkqrVAIARALIRKPKILLLDMA 585
Cdd:PRK10762 93 QlTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQM----VEIAKVLSFESKVIIMDEP 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1390249242 586 TSAL-DNESEA--KVQGALNkiQHGHTIISVAHRL 617
Cdd:PRK10762 169 TDALtDTETESlfRVIRELK--SQGRGIVYISHRL 201
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
792-998 |
7.69e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 61.74 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 792 RSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQG- 870
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSEl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 871 ATGSQVGMMVNSFTNIFVAVLIaFLFNWKLSLVISVFFPFLALSGAV-QTKMLTGFASQDKEILEKAGQITnEALSNIRT 949
Cdd:cd18546 113 LQTGLVQLVVSLLTLVGIAVVL-LVLDPRLALVALAALPPLALATRWfRRRSSRAYRRARERIAAVNADLQ-ETLAGIRV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 950 VAGIGVEGRFIKAFEvELEKSYktaiRKANVYGLCYA--FSQGISFLANSA 998
Cdd:cd18546 191 VQAFRRERRNAERFA-ELSDDY----RDARLRAQRLVaiYFPGVELLGNLA 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
420-646 |
8.12e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLdGHDIRslnirwlrdqIG 499
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLF--STTIAENIRLGREEATMEDIVQAAKDanaYNFImalPQQFDTLVgegggqmsggqKQ-------RVAIA 570
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGR---FLFS---GDDAFKPV-----------GVlsggekaRLALA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 571 RALIRKPKILLLDMATSALDNESEAKVQGALNKIQhGhTIISVAH-R--LSTVrsADVIIGFEHGTAVER-GTHEELLER 646
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1089-1253 |
8.63e-10 |
|
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: 59.68 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDC 1168
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYgdntkeisvERAIAAAKQAQLHDfvmSLpekyeTNVGIQG------SQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:TIGR01189 89 SALENLHF---------WAAIHGGAQRTIED---AL-----AAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|.
gi 1390249242 1243 DEATSALDTES 1253
Cdd:TIGR01189 152 DEPTTALDKAG 162
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
427-659 |
8.63e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 427 FHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGH--DIRSLNIRWLRDQIGIVEQE 504
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 505 P--VLFSTTIAENI-----RLGREEAtmeDIVQAAKDAnaynFIMALPQQFDtlvGEGGGQMSGGQKQRVAIARALIRKP 577
Cdd:PRK13638 86 PeqQIFYTDIDSDIafslrNLGVPEA---EITRRVDEA----LTLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALNKI--QHGHTIISvAHRLSTVRS-ADVIIGFEHGTAVERG------THEELLERKG 648
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIS-SHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
250
....*....|..
gi 1390249242 649 VYF-MLVTLQSQ 659
Cdd:PRK13638 235 LTQpWLVKLHTQ 246
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1089-1306 |
1.00e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKST-SIQLLERF-YDPDQGTVMIDGHDSKKVNVQfLRSNIGI--VSQEPV 1164
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDcSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFV------MSLPEKYET---NVGIQGsqlsrGEKQRIAIARAIVR 1235
Cdd:PRK09580 89 EIP-GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMeekialLKMPEDLLTrsvNVGFSG-----GEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1236 DPKILLLDEATSALDTESEKTVQLALDKAREG-RTCIVIAH--RLSTIQNSDIIAVMSQGVVIEKGTH---KKLMDQ 1306
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1066-1278 |
1.04e-09 |
|
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: 62.84 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1066 GAGEKWDNFQGkIDFIDCKFTYPSrpDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsk 1145
Cdd:TIGR00954 441 GRGIVEYQDNG-IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA---- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1146 kvnvqflRSNIGIVSQEPVLFDCSIMDNIKYGDnTKEISVERAIAAAKQAQLHDFVmSLPEKYETNVGIQGSQ-----LS 1220
Cdd:TIGR00954 514 -------KGKLFYVPQRPYMTLGTLRDQIIYPD-SSEDMKRRGLSDKDLEQILDNV-QLTHILEREGGWSAVQdwmdvLS 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1221 RGEKQRIAIARAIVRDPKILLLDEATSALDTESE-KTVQLALDKareGRTCIVIAHRLS 1278
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEgYMYRLCREF---GITLFSVSHRKS 640
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
427-617 |
1.28e-09 |
|
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: 63.11 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 427 FHYPSRPEVKILNnlsMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIGIVEQEPV 506
Cdd:TIGR01257 938 FEPSGRPAVDRLN---ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 507 LFS-TTIAENIRL-----GRE--------EATMEDI-VQAAKDANAYNFIMALPQqfdtlvgegggqmsggqkqRVAIAR 571
Cdd:TIGR01257 1014 LFHhLTVAEHILFyaqlkGRSweeaqlemEAMLEDTgLHHKRNEEAQDLSGGMQR-------------------KLSVAI 1074
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390249242 572 ALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRL 617
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
148-360 |
1.36e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 61.07 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 148 VGVAVL--ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSdDINKIDEAIADQMalflqrLS 225
Cdd:cd18782 49 LVAALLeaVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTA------LT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 226 TALSGLLLGFYRG------WKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENK 299
Cdd:cd18782 122 TLLDVLFSVIYIAvlfsysPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 300 EVERYEKNLM-FAQRwgIWKGMVMGFFTGYMWCLI-FFCYALAFWYGSRLVLdEGEYTPGTLI 360
Cdd:cd18782 202 ARWRWQNRYArSLGE--GFKLTVLGTTSGSLSQFLnKLSSLLVLWVGAYLVL-RGELTLGQLI 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
409-651 |
1.36e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 409 DGYKLDRIKGEIEFH--NVTFHYPSRPEVK-ILNNLSMVIKPGETTAFVGSSGAGKSTALQ-LIQRFydpCEGMVTldgH 484
Cdd:TIGR00956 747 DEKDMEKESGEDIFHwrNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVIT---G 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 485 DIRSLNIRWLRD----QIGIVEQEPV-LFSTTIAENIRLG---REEATMEDivqaaKDANAY-NFIMAL---PQQFDTLV 552
Cdd:TIGR00956 821 GDRLVNGRPLDSsfqrSIGYVQQQDLhLPTSTVRESLRFSaylRQPKSVSK-----SEKMEYvEEVIKLlemESYADAVV 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 553 GEGGGQMSGGQKQRVAIARALIRKPKILL-LDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRlstvRSADVIIGFE 630
Cdd:TIGR00956 896 GVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQ----PSAILFEEFD 971
|
250 260
....*....|....*....|....
gi 1390249242 631 hgtavergthEELLERKG---VYF 651
Cdd:TIGR00956 972 ----------RLLLLQKGgqtVYF 985
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
803-1044 |
1.48e-09 |
|
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: 60.56 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 803 VILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNS 882
Cdd:cd18589 43 SLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 883 FTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKA 962
Cdd:cd18589 121 LARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 963 FEVELEKSYKTAIRKANVYGLCyAFSQGISFLA-NSAAYRYGGYLIVYEDLNF-SYVFRVVSSIAMSaTAVGRTFSYTPS 1040
Cdd:cd18589 201 YRQRLQKTYRLNKKEAAAYAVS-MWTSSFSGLAlKVGILYYGGQLVTAGTVSSgDLVTFVLYELQFT-SAVEVLLSYYPS 278
|
....
gi 1390249242 1041 YAKA 1044
Cdd:cd18589 279 VMKA 282
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
143-309 |
1.49e-09 |
|
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: 60.94 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIrLWVITGArqIRKMRKFYFR---RIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMAL 219
Cdd:cd18604 47 GIYALISLLSVLLGTLRY-LLFFFGS--LRASRKLHERllhSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 220 FLQRLSTALSGLllgfyrgwkltLVILAVSPLIGIGAAVIGLSVAKFTELelkaYAKAG-------SIA--------DEV 284
Cdd:cd18604 124 LLESTLSLLVIL-----------IAIVVVSPAFLLPAVVLAALYVYIGRL----YLRASrelkrleSVArspilshfGET 188
|
170 180
....*....|....*....|....*
gi 1390249242 285 LSSIRTVAAFGGEnkevERYEKNLM 309
Cdd:cd18604 189 LAGLVTIRAFGAE----ERFIEEML 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
420-647 |
1.67e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSlNIRWLRDQIG 499
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQ----EPvlfSTTIAENIRL-----GREEATMEDIVQAAKDanaynfIMALPQQFDTLVGEGGGQMSGgqkqRVAIA 570
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLVfgryfGLSAAAARALVPPLLE------FAKLENKADAKVGELSGGMKR----RLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 571 RALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1099-1304 |
1.73e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKSTsiqLLERFYD--PDQGTVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFdcsIMDNIK 1175
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPlEAWSAAELARHRAYLSQQQTPPF---AMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1176 Y-----GDNTKEISVERAIAaakqaQLHDFVMsLPEKYETNVGiqgsQLSRGEKQRIAIARAIVR-------DPKILLLD 1243
Cdd:PRK03695 89 YltlhqPDKTRTEAVASALN-----EVAEALG-LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1244 EATSALDTesekTVQLALDK-----AREGRTCIVIAHRLS-TIQNSDIIAVMSQGVVIEKGTHKKLM 1304
Cdd:PRK03695 159 EPMNSLDV----AQQAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
420-620 |
1.96e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVtldghdIRSLNIRwlrdqIG 499
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLR-----IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLFST---TIAENIRLgREEATMEDIVQAAKDANAYNFIMALPQQFDtlvgegggqmsGGQKQRVAIARALIRK 576
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQKLS-----------GGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTV 620
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
427-633 |
2.02e-09 |
|
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: 59.65 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 427 FHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRdQIGIV--EQE 504
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 505 PVLFSTTIAENIRLGREeatMEDIVQAAKDANAYNFIMALpqQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDM 584
Cdd:cd03267 105 QLWWDLPVIDSFYLLAA---IYDLPPARFKKRLDELSELL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 585 ATSALDNESEAKVQG---ALNKiQHGHTIISVAHRLSTVRS-ADVIIGFEHGT 633
Cdd:cd03267 180 PTIGLDVVAQENIRNflkEYNR-ERGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1093-1249 |
2.59e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFD-CSI 1170
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFSrMTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1171 MDNIKYGDntkeISVERAIAAAKQAQLHDFvmsLPEKYETNVGIQGSqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK11614 98 EENLAMGG----FFAERDQFQERIKWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1092-1299 |
2.73e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKS-TSIQLLERFYDPDQ--GTVMIDGHD-----SKKVNVqfLRS-NIGIVSQE 1162
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREilnlpEKELNK--LRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 PVlfdCSIMDNIKYGDNTKEI-----SVERAIAAAKQAQLHDFVmSLPEKYEtNVGIQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK09473 106 PM---TSLNPYMRVGEQLMEVlmlhkGMSKAEAFEESVRMLDAV-KMPEARK-RMKMYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1238 KILLLDEATSALDTesekTVQ-----LALDKAREGRTCIV-IAHRLSTIQNS-DIIAVMSQGVVIEKGT 1299
Cdd:PRK09473 181 KLLIADEPTTALDV----TVQaqimtLLNELKREFNTAIImITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1076-1252 |
3.44e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1076 GKIDFIDCKFTYpSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVmidgHDSKKVNVQFL--- 1152
Cdd:PRK11147 316 GKIVFEMENVNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFdqh 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1153 RSNIgivsqEPvlfDCSIMDNIkyGDNTKEISV---ERAIAaakqAQLHDFVMSlPEKYETNVgiqgSQLSRGEKQRIAI 1229
Cdd:PRK11147 391 RAEL-----DP---EKTVMDNL--AEGKQEVMVngrPRHVL----GYLQDFLFH-PKRAMTPV----KALSGGERNRLLL 451
|
170 180
....*....|....*....|...
gi 1390249242 1230 ARAIVRDPKILLLDEATSALDTE 1252
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVE 474
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
752-1244 |
4.06e-09 |
|
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: 60.97 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 752 WPYILVGALCAAINGAVTpiySLLFSQILKTFSlvdkeQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRL 831
Cdd:COG4615 12 RWLLLLALLLGLLSGLAN---AGLIALINQALN-----ATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 832 RKFGFKAMLRQDIGWFDDLKNNPgvLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLfNWKLSLVISVFfpfL 911
Cdd:COG4615 84 RLRLSRRILAAPLERLERIGAAR--LLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWL-SPPLFLLTLVL---L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 912 ALSGAVQTKMLtgfaSQDKEILEKAGQITNEALSNIRTVagigVEG---------RFIKAFEVELEKSYKTA----IRKA 978
Cdd:COG4615 158 GLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRAL----LEGfkelklnrrRRRAFFDEDLQPTAERYrdlrIRAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 979 NVYGLCYAFSQGISFLAnsaayrYGGYLIV---YEDLNFSYVFRVVSSIAMSATAVGRTFSYTPSYAKAKISAARFFQL- 1054
Cdd:COG4615 230 TIFALANNWGNLLFFAL------IGLILFLlpaLGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1055 --LDRKPPIDVYSGAGEKWDNFQgKIDFIDCKFTYPSRPDIQ--VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFY 1130
Cdd:COG4615 304 laLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1131 DPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFDcsimdniKYGDNTKEISVERAiaaakQAQLHDFVMSlpEKyet 1210
Cdd:COG4615 383 RPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------RLLGLDGEADPARA-----RELLERLELD--HK--- 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 1390249242 1211 nVGIQG-----SQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:COG4615 446 -VSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
420-638 |
5.23e-09 |
|
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: 57.68 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNirwlRDQIG 499
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPVLF-STTIAENIR-------LGREEA--TMEDIVQAAKDANAYNfimalpQQFDTLvgegggqmSGGQKQRVAI 569
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVylaqlkgLKKEEArrRIDEWLERLELSEYAN------KRVEEL--------SKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 570 ARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTV-RSADVIIGFEHGTAVERG 638
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
143-359 |
6.66e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 59.12 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQ 222
Cdd:cd18565 58 GLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 223 RLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGaaviglsVAKFTELELKAYA----KAGSIA---DEVLSSIRTVAAFG 295
Cdd:cd18565 138 VVVTVLGIGAILFYLNWQLALVALLPVPLIIAG-------TYWFQRRIEPRYRavreAVGDLNarlENNLSGIAVIKAFT 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 296 GENKEVERYEK--NLMFAQRWGIWKgmVMGFFTGYMWCLIFFCYALAFWYGSRLVLD-----EGEYTPGTL 359
Cdd:cd18565 211 AEDFERERVADasEEYRDANWRAIR--LRAAFFPVIRLVAGAGFVATFVVGGYWVLDgpplfTGTLTVGTL 279
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1089-1252 |
8.62e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNvqflRSN-IGIVSQEPVL-F 1166
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLkA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 DCSIMDNIKYGDNTKeisveraiaaAKQAQlhdfvmSLPEKYETNVGIQG------SQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:PRK13543 96 DLSTLENLHFLCGLH----------GRRAK------QMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|..
gi 1390249242 1241 LLDEATSALDTE 1252
Cdd:PRK13543 160 LLDEPYANLDLE 171
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
424-643 |
1.02e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.58 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPSrPEVKILNNLSMVIKPGETTAFVGSSGAGKS-TALQLIQRFYDP--CEGMVTLDGHDIRSLNIRWLR----D 496
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGIVEQEPVlfsTTIAENIRLG--------------REEATMEDI--VQAAKDANAYNFIMALPQQFdtlvgegggqmS 560
Cdd:PRK09473 98 QISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmsKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------S 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 561 GGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVR-SADVIIGFEHGTAVER 637
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEY 243
|
....*.
gi 1390249242 638 GTHEEL 643
Cdd:PRK09473 244 GNARDV 249
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
132-360 |
1.46e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 57.91 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 132 VDINSEVIKFSGIYAGVGVAVLILGYFQ-IRLWVIT--GARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDdINK 208
Cdd:cd18555 32 VIVPGNLNLLNVLGIGILILFLLYGLFSfLRGYIIIklQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANS-NVY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 209 IDEAIADQMALFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSI 288
Cdd:cd18555 111 IRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 289 RTVAAFGGE----NKEVERYEKNLMFAQRWGIWKGMVMGFFTGymwclIFFCYALA-FWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18555 191 ETIKSLGSEkniyKKWENLFKKQLKAFKKKERLSNILNSISSS-----IQFIAPLLiLWIGAYLVIN-GELTLGELI 261
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
423-615 |
1.47e-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: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 423 HNVTFHYPsrPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLiqrfydpcegMVTLD----GHDIRSLNIRwlrdqI 498
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkdfnGEARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFST-TIAENI-----------------------------RLGREEATMEDIVQAAkdaNAYNFIMALPQQF 548
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisakyaepdadfdKLAAEQAELQEIIDAA---DAWDLDSQLEIAM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 549 DTLVGEGGGQMSGGQK----QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALnkIQHGHTIISVAH 615
Cdd:TIGR03719 148 DALRCPPWDADVTKLSggerRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1111-1309 |
1.50e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1111 FVGSSGCGKSTSIQLLERFYDPDQGTVMIDGH--DSKKVNVqflRSNIGIVSQEPVLfdcsimdnikYGdntkEISV--- 1185
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---RRRVGYMSQAFSL----------YG----ELTVrqn 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1186 -----------ERAIAAAKQAQLHDF----VM-SLPEkyetnvgiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:NF033858 360 lelharlfhlpAAEIAARVAEMLERFdladVAdALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1250 DtesekTV------QLALDKAREGRTCIVIA-HRLSTIQNSDIIAVMSQGVVIEKGTHKKLMDQKGA 1309
Cdd:NF033858 429 D-----PVardmfwRLLIELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARGA 490
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
114-377 |
1.74e-08 |
|
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: 57.54 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 114 WINSSFNQNmtngtscgLVDINSEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCT 193
Cdd:cd18605 25 WVSHSNNSF--------FNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 194 SVGELNSRFSDDINKIDEAIADQMALFLQRLST---ALSGLLLGFYrgWkltlVILAVSPLigigaAVIGLSVAKF---T 267
Cdd:cd18605 97 PVGRILNRFSSDVYTIDDSLPFILNILLAQLFGllgYLVVICYQLP--W----LLLLLLPL-----AFIYYRIQRYyraT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 268 ELELK-----AYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLMFAQRwgiwkgmvmGFFTGymwcliffcYALAFW 342
Cdd:cd18605 166 SRELKrlnsvNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQR---------AQLAS---------QAASQW 227
|
250 260 270
....*....|....*....|....*....|....*
gi 1390249242 343 YGSRLVLdegeytPGTLIQIFLCVIIAAMNIGNAS 377
Cdd:cd18605 228 LSIRLQL------LGVLIVTFVALTAVVQHFFGLS 256
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
426-632 |
2.12e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.94 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 426 TFHypsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQ----LIQRFYDPcEGMVTLDGHDIR-----SLNIRWLRD 496
Cdd:PRK09984 13 TFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLGRTVQregrlARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIG-IVEQEPVLFSTTIAENIRLGREEAT--------------MEDIVQAAKDANAYNFIMalpQQFDTLvgegggqmSG 561
Cdd:PRK09984 87 NTGyIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAH---QRVSTL--------SG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 562 GQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLS-TVRSADVIIGFEHG 632
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
424-632 |
2.57e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 424 NVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDghDIRSLNIRWLRDQIGIVEQ 503
Cdd:PRK11000 8 NVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 504 EPVLFS-TTIAENIRLGREEATMEDIvQAAKDANAYNFIMalpqQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLL 582
Cdd:PRK11000 83 SYALYPhLSVAENMSFGLKLAGAKKE-EINQRVNQVAEVL----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 583 DMATSALDNESEAKVQGALNKIQH--GHTIISVAH-RLSTVRSADVIIGFEHG 632
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAG 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
432-599 |
3.27e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 432 RPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL------RDQIgiveqEP 505
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAM-----KP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 506 VLfstTIAENIR-----LGREEAtmeDIVQAAKDANAYNfIMALP-------QQfdtlvgegggqmsggqkQRVAIARAL 573
Cdd:PRK13539 87 AL---TVAENLEfwaafLGGEEL---DIAAALEAVGLAP-LAHLPfgylsagQK-----------------RRVALARLL 142
|
170 180
....*....|....*....|....*.
gi 1390249242 574 IRKPKILLLDMATSALDNESEAKVQG 599
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
423-583 |
3.37e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.81 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 423 HNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTAlqliqrFY------DPCEGMVTLDGHDIRSLNIrWLRD 496
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 497 QIGI--VEQEPVLF-STTIAENIRLGREEATMEDIVQAAKdanaynfIMALPQQF----------DTLvgegggqmsggq 563
Cdd:COG1137 77 RLGIgyLPQEASIFrKLTVEDNILAVLELRKLSKKEREER-------LEELLEEFgithlrkskaYSLsgg--------e 141
|
170 180
....*....|....*....|
gi 1390249242 564 kqRVAIARALIRKPKILLLD 583
Cdd:COG1137 142 rrRVEIARALATNPKFILLD 161
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
431-615 |
3.77e-08 |
|
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: 55.19 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFST 510
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 511 TIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALD 590
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSA-----------GQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 1390249242 591 NESEAKVQGAL-NKIQHGHTIISVAH 615
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
434-620 |
4.40e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLN---IRWLRDQIGIVEQEPV---- 506
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 507 ---LFSTTIAENIR---LGREEATMEDIVQ-----AAKDANAYNFimalPQQFDtlvgegggqmsGGQKQRVAIARALIR 575
Cdd:PRK10261 416 prqTVGDSIMEPLRvhgLLPGKAAAARVAWllervGLLPEHAWRY----PHEFS-----------GGQRQRICIARALAL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1390249242 576 KPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTV 620
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVV 527
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
428-606 |
4.59e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.86 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 428 HYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIrwlrdQIGIVEQ-EPV 506
Cdd:PRK11248 10 DYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-----ERGVVFQnEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 507 LFSTTIAENIRLG----------REEATMEDIVQAAKDANAYNFIMALpqqfdtlvgegggqmSGGQKQRVAIARALIRK 576
Cdd:PRK11248 82 LPWRNVQDNVAFGlqlagvekmqRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRVGIARALAAN 146
|
170 180 190
....*....|....*....|....*....|
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNKIQH 606
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQ 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
437-644 |
6.21e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRfyDPCE----------GMVTLDGHDIRSLNIRWLRDQIGIVEQ--E 504
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 505 PVlFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQfDTLVGEGGGQMSGGQKQRVAIARAL---------IR 575
Cdd:PRK13547 94 PA-FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 576 KPKILLLDMATSALDneseakvqgalnkIQHGHTIISVAHRLS----------------TVRSADVIIGFEHGTAVERGT 639
Cdd:PRK13547 172 PPRYLLLDEPTAALD-------------LAHQHRLLDTVRRLArdwnlgvlaivhdpnlAARHADRIAMLADGAIVAHGA 238
|
....*
gi 1390249242 640 HEELL 644
Cdd:PRK13547 239 PADVL 243
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
433-633 |
6.88e-08 |
|
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: 54.64 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 433 PEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMV----TLDGHDIRSLNIRWLRDQIGIVEQEPVLF 508
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 STTIAENIRLGreEATMEDIVQAAKDANAYN-FIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATS 587
Cdd:cd03290 92 NATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249242 588 ALD-NESEAKVQ-GALNKIQHG-HTIISVAHRLSTVRSADVIIGFEHGT 633
Cdd:cd03290 170 ALDiHLSDHLMQeGILKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
114-340 |
1.10e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 55.30 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 114 WINSSFNQNMTNGTSCGLVDINSEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCT 193
Cdd:cd18602 25 WTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 194 SVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLllgfyrgwkltLVILAVSP---LIGIGAAVIGLSVAKF---- 266
Cdd:cd18602 105 PIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAI-----------IVNAIVTPyflIALIPIIIVYYFLQKFyras 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 267 -TEL-ELKAYAKAGSIA--DEVLSSIRTVAAFGGENKEVERYEKN----------LMFAQRWgiwkgmvMGFFTGYMWCL 332
Cdd:cd18602 174 sRELqRLDNITKSPVFShfSETLGGLTTIRAFRQQARFTQQMLELidrnntaflfLNTANRW-------LGIRLDYLGAV 246
|
....*...
gi 1390249242 333 IFFCYALA 340
Cdd:cd18602 247 IVFLAALS 254
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
798-1012 |
1.32e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 54.78 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 798 MCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVG 877
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 878 MMVNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAV-QTKMLTGFasqdKEILEKAGQIT---NEALSNIRTVAGI 953
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLlRRRARKAW----QRVRKKISNLNaylHESISGIRVIQSF 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 954 GVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDL 1012
Cdd:cd18545 196 AREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAI 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1088-1292 |
1.46e-07 |
|
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: 55.60 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1088 PSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPDQ--GTVMIDGHDSKKVN-VQFLRSNIGIVSQEP- 1163
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNpAQAIRAGIAMVPEDRk 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 ---VLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEK-YETNVGIQGsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:TIGR02633 347 rhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtASPFLPIGR--LSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1240 LLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIyKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEG 479
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
149-360 |
1.57e-07 |
|
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: 54.49 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 149 GVAVLILGYFQIrlwVITGARQI----------RKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDiNKIDEAIADQ-M 217
Cdd:cd18568 45 LIGLLIVGIFQI---LLSAVRQYlldyfanridLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSaL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 218 ALFLQRLSTALSGLLLgFYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGE 297
Cdd:cd18568 121 TTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 298 N----KEVERYEKNLMF---AQRWGIWKGMVMGFFTgymwcliFFCYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18568 200 RpirwRWENKFAKALNTrfrGQKLSIVLQLISSLIN-------HLGTIAVLWYGAYLVIS-GQLTIGQLV 261
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1085-1250 |
1.66e-07 |
|
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: 53.04 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDqGTVMIDGHDSKKVNVQFlRSNIGIVS 1160
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1161 QEPVLFdcsimdnikygdntKEISVERAIAAAKQAQLHDFVMslpekyetnvGIQGsqlsrGEKQRIAIARAIVRDPKIL 1240
Cdd:cd03233 90 EEDVHF--------------PTLTVRETLDFALRCKGNEFVR----------GISG-----GERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 1390249242 1241 LLDEATSALD 1250
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1094-1286 |
1.69e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIdgHDSKKVNVQ-----FLRSNIGIVSqepvlfDC 1168
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYIGHNLGLKL------EM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKYGDNTKEiSVERAIAAAKQAQLHDFvmsLPEKYETnvgiqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:PRK13541 86 TVFENLKFWSEIYN-SAETLYAAIHYFKLHDL---LDEKCYS--------LSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1390249242 1249 LDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQNSDII 1286
Cdd:PRK13541 154 LSKENRDLLnNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1078-1284 |
1.71e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRS--- 1154
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQlcf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 -------NIGIVSQEPVLFDCSImdnikygdNTKEISVERAIAAAKQAQLHDFVMSLpekyetnvgiqgsqLSRGEKQRI 1227
Cdd:PRK13540 79 vghrsgiNPYLTLRENCLYDIHF--------SPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAR-EGRTCIVIAHRLSTIQNSD 1284
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1085-1252 |
1.77e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.95 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRpdIQVLNGLSVSVDPG-----QTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDskkvnVQFLRSNIGIV 1159
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----VSYKPQYIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQEPVLFDCSIMDNIKYGDNTKEISVeraiaaAKQAQLHDFvmslpekYETNVgiqgSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03237 74 YEGTVRDLLSSITKDFYTHPYFKTEI------AKPLQIEQI-------LDREV----PELSGGELQRVAIAACLSKDADI 136
|
170
....*....|...
gi 1390249242 1240 LLLDEATSALDTE 1252
Cdd:cd03237 137 YLLDEPSAYLDVE 149
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
434-506 |
1.88e-07 |
|
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: 52.91 E-value: 1.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRF--YDPCEGMVTLDGHDIRSLNI--RwLRDQIGIVEQEPV 506
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeeR-ARLGIFLAFQYPP 87
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
755-1012 |
2.16e-07 |
|
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: 54.10 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 755 ILVGALCAAINGAVTPiyslLFSQILktfslVDK---EQQRSEIYSMCLFFVILGCVSLFTQFLQGYnfaksgeLLTKRL 831
Cdd:cd18568 7 ILLASLLLQLLGLALP----LFTQII-----LDRvlvHKNISLLNLILIGLLIVGIFQILLSAVRQY-------LLDYFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 832 RKFG-------FKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTnIFVAVLIAFLFNWKLSLVI 904
Cdd:cd18568 71 NRIDlsllsdfYKHLLSLPLSFFA--SRKVGDIITRFQENQKIRRFLTRSALTTILDLLM-VFIYLGLMFYYNLQLTLIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 905 SVFFPFLALSGAVQTKMLTGFAsqdKEILEKAGQITN---EALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVY 981
Cdd:cd18568 148 LAFIPLYVLLTLLSSPKLKRNS---REIFQANAEQQSflvEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLS 224
|
250 260 270
....*....|....*....|....*....|.
gi 1390249242 982 GLCYAFSQGISFLANSAAYRYGGYLIVYEDL 1012
Cdd:cd18568 225 IVLQLISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1091-1287 |
2.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1091 PDIQV-LNGLSVSVDPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGTVmidghdSKKVNV----QFLRSNI-GIV 1159
Cdd:PRK13409 344 PDLTKkLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKIsykpQYIKPDYdGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1160 SQepVLFdcSIMDNikYGDN--TKEIsveraiaaAKQAQLHDFvmslpekYETNVgiqgSQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK13409 418 ED--LLR--SITDD--LGSSyyKSEI--------IKPLQLERL-------LDKNV----KDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKAREGR--TCIVIAHRLSTIqnsDIIA 1287
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1078-1294 |
2.47e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1078 IDFIDCKFTYPSRPdiQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMidghDSKKVnvqflrsNIG 1157
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----RSAKV-------RMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1158 IVSQEPVlfdcsimDNIKYGDNTKeISVERAIAAAKQAQLHDFVMSLpekyetnvGIQGS-------QLSRGEKQRIAIA 1230
Cdd:PLN03073 576 VFSQHHV-------DGLDLSSNPL-LYMMRCFPGVPEQKLRAHLGSF--------GVTGNlalqpmyTLSGGQKSRVAFA 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1231 RAIVRDPKILLLDEATSALDTES-EKTVQ-LALdkaREGRTCIViAHRLSTIQNS-DIIAVMSQGVV 1294
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDAvEALIQgLVL---FQGGVLMV-SHDEHLISGSvDELWVVSEGKV 702
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
420-636 |
3.05e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRP--------------------EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdpcEGMV 479
Cdd:COG2401 8 FVLMRVTKVYSSVLdlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 480 TLDGHDIRSLNIrwlrdqigivEQEpvlfsTTIAENI-RLGREEATMEdIVQAAKDANAYNFI-----MALPQQFdtlvg 553
Cdd:COG2401 85 VAGCVDVPDNQF----------GRE-----ASLIDAIgRKGDFKDAVE-LLNAVGLSDAVLWLrrfkeLSTGQKF----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 554 egggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRlSTVRSA---DVIIG 628
Cdd:COG2401 144 ------------RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATHH-YDVIDDlqpDLLIF 210
|
....*...
gi 1390249242 629 FEHGTAVE 636
Cdd:COG2401 211 VGYGGVPE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1095-1295 |
3.10e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLerF--YDPDQGTVMIDGhdsKKVNV----QFLRSNIGIVS----QEPV 1164
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDG---KPVRIrsprDAIRAGIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LFDCSIMDNI------KYGD----NTKEisvERAIAAAKQAQLhDFVMSLPEkyeTNVGiqgsQLSRGEKQRIAIARAIV 1234
Cdd:COG1129 342 VLDLSIRENItlasldRLSRggllDRRR---ERALAEEYIKRL-RIKTPSPE---QPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1235 RDPKILLLDEATSALDtesektV-------QLALDKAREGRTCIVIahrlST-----IQNSDIIAVMSQGVVI 1295
Cdd:COG1129 411 TDPKVLILDEPTRGID------VgakaeiyRLIRELAAEGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-1008 |
3.15e-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: 53.64 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 752 WPYILVGALCAAINGAVTPIYSLLFSQILKTFslvDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRL 831
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHF---ITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 832 RKFGFKAMLRQDIGWFDdlKNNPGVLTTRLATDASQVqgatgSQV---GMM--VNSFTNIFVAVLIAFLFNWKLSLVISV 906
Cdd:cd18540 78 RKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRL-----GEIiswGLVdlVWGITYMIGILIVMLILNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 907 FFPFLAL-SGAVQTKMLtgfaSQDKEILEKAGQIT---NEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYG 982
Cdd:cd18540 151 VVPVLAVvSIYFQKKIL----KAYRKVRKINSRITgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSA 226
|
250 260
....*....|....*....|....*.
gi 1390249242 983 LCYAFSQGISFLANSAAYRYGGYLIV 1008
Cdd:cd18540 227 LFLPIVLFLGSIATALVLWYGGILVL 252
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
447-639 |
3.20e-07 |
|
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: 51.22 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 447 PGETTAFVGSSGAGKSTALQLIQRFYDP-CEGMVTLDGHDIRSLNIRWLRdqigiveqepvlfsttiaenirlgreeatm 525
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 526 edivqaakdanaynfimalpqqfDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQ------- 598
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390249242 599 GALNKIQHGHTIISVAHRLSTVRSADVIIGFEHGTAVERGT 639
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1085-1309 |
3.94e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1085 FTYPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIdghdSKKvnvqflrSNIGIVSQEPV 1164
Cdd:PRK15064 327 KGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----SEN-------ANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 L-FDC--SIMDNI----KYGDNtkEISVeRAIaaakqaqLHDFVMSlpekyETNVGIQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK15064 393 YdFENdlTLFDWMsqwrQEGDD--EQAV-RGT-------LGRLLFS-----QDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1238 KILLLDEATSALDTESEKTVQLALDKArEGrTCIVIAH-R--LSTIQNSdIIAVMSQGVVIEKGTHKKLMDQKGA 1309
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSLATR-IIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1092-1280 |
4.55e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL-ERFYDP--DQGTVMIDGHdskKVNVQFLRSnIGIVSQEPVlfdc 1168
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGviTGGDRLVNGR---PLDSSFQRS-IGYVQQQDL---- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 simdnikygdNTKEISVERAI---AAAKQAQ---------LHDFVMSLPE--KY-ETNVGIQGSQLSRGEKQRIAIARAI 1233
Cdd:TIGR00956 847 ----------HLPTSTVRESLrfsAYLRQPKsvsksekmeYVEEVIKLLEmeSYaDAVVGVPGEGLNVEQRKRLTIGVEL 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249242 1234 VRDPKILL-LDEATSALDTESE-KTVQLALDKAREGRTCIVIAHRLSTI 1280
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAwSICKLMRKLADHGQAILCTIHQPSAI 965
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
113-233 |
6.89e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging 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: 350043 [Multi-domain] Cd Length: 313 Bit Score: 52.57 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 113 VWIN--SSFNQNMTNGTSCGLVDI--NSEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIG 188
Cdd:cd18599 28 YWLKqgSGNTTNNVDNSTVDSGNIsdNPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMS 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1390249242 189 WFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLL 233
Cdd:cd18599 108 FFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLII 152
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1086-1292 |
8.53e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL--ERfyDPDQGTVMIDGHDSKKVNV-QFLRSNIGIVSQE 1162
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 P-----VLfDCSIMDNIKYGDNTKEISVERAI----AAAKQAQlhdfvmSLPEKYE---TNVGIQGSQLSRGEKQRIAIA 1230
Cdd:COG3845 342 RlgrglVP-DMSVAENLILGRYRRPPFSRGGFldrkAIRAFAE------ELIEEFDvrtPGPDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1231 RAIVRDPKILLLDEATSALDTESEKTVQLALDKAR-EGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEG 478
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
800-1051 |
8.89e-07 |
|
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: 52.10 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 800 LFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDDLKnnPGVLTTRLATDASQVQGATgSQVGMM 879
Cdd:cd18543 43 LLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFL-AFGPFL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 880 VNSFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAVQTKMLTG--FASQDKeilekAGQIT---NEALSNIRTVAGIG 954
Cdd:cd18543 120 LGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPasRRAQDQ-----AGDLAtvvEESVTGIRVVKAFG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 955 VEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLN-------FSYVFRVVSSIAMS 1027
Cdd:cd18543 195 RERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTlgtlvafSAYLTMLVWPVRML 274
|
250 260
....*....|....*....|....
gi 1390249242 1028 ATAVGRTFSytpsyakAKISAARF 1051
Cdd:cd18543 275 GWLLAMAQR-------ARAAAERV 291
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
139-360 |
1.03e-06 |
|
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: 52.10 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 139 IKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMA 218
Cdd:cd18540 42 TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 219 LFLQRLSTALSGLLLGFYRGWKLTLVILAVSPLIgigaAVIGLsvaKFTELELKAYAKA--------GSIaDEVLSSIRT 290
Cdd:cd18540 122 DLVWGITYMIGILIVMLILNWKLALIVLAVVPVL----AVVSI---YFQKKILKAYRKVrkinsritGAF-NEGITGAKT 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 291 VAAFGGENKEVERYEK--NLMFAQ--RWGIWKGMvmgfftgYMWCLIFFCY---ALAFWYGSRLVLdEGEYTPGTLI 360
Cdd:cd18540 194 TKTLVREEKNLREFKEltEEMRRAsvRAARLSAL-------FLPIVLFLGSiatALVLWYGGILVL-AGAITIGTLV 262
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
146-360 |
1.37e-06 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 51.75 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 146 AGVGVAVL---ILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDdINKIDEAIADQMalflq 222
Cdd:cd18783 46 IGVVIALLfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTGQL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 223 rLSTAL--SGLLLG----FYRGWKLTLVILAVSPLIgigAAVIGLSVAKFTELELKAY---AKAGSIADEVLSSIRTVAA 293
Cdd:cd18783 120 -FGTLLdaTSLLVFlpvlFFYSPTLALVVLAFSALI---ALIILAFLPPFRRRLQALYraeGERQAFLVETVHGIRTVKS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 294 FGGENKEVERYEK------NLMFA-QRWGIWKGMVMGFFTGYMwcliffcYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18783 196 LALEPRQRREWDErvaraiRARFAvGRLSNWPQTLTGPLEKLM-------TVGVIWVGAYLVFA-GSLTVGALI 261
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
802-1012 |
1.60e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 51.43 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 802 FVILGCVSLFtQFLQGYNFAKSGELLTKRLRKFGFKAMLRQDIGWFDdlKNNPGVLTTRLAtDASQVQGATGSQVGMMVN 881
Cdd:cd18566 49 VIAILLESLL-RLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 882 SFTNIFVAVLIAFLFNWKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIK 961
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLR 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 962 AFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDL 1012
Cdd:cd18566 205 RYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1086-1253 |
2.20e-06 |
|
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: 51.86 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTsiqLLErfydpdqgtvMIDGHDSKKVNVQFLRSNI--GIVSQEP 1163
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVDKDFNGEARPQPGIkvGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1164 VLfDCS--IMDNIKYG--------DNTKEISVERA-------IAAAKQAQLHDFV------------------MSLPEKy 1208
Cdd:TIGR03719 78 QL-DPTktVRENVEEGvaeikdalDRFNEISAKYAepdadfdKLAAEQAELQEIIdaadawdldsqleiamdaLRCPPW- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390249242 1209 ETNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:TIGR03719 156 DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1096-1287 |
3.17e-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: 51.71 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1096 LNGLSVSVDPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGTVmidghdSKKVNV----QFLRSNIgivsqepvlf 1166
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPDY---------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1167 dcsimdnikygdntkEISVERAIAAAKQAQL------HDFV--MSLPEKYETNVgiqgSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:COG1245 415 ---------------DGTVEEFLRSANTDDFgssyykTEIIkpLGLEKLLDKNV----KDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 1239 ILLLDEATSALDTESEKTVQLALDKAREGR--TCIVIAHRLSTIqnsDIIA 1287
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1094-1302 |
5.36e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1094 QVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDQGTVMIDGHDSKKVnVQFLRSNIGIVSQEPVLF-DC 1168
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFpHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1169 SIMDNIKY-----GDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVG---IQGsqLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:TIGR00956 154 TVGETLDFaarckTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGndfVRG--VSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1241 LLDEATSALDTESektvqlALDKAREGRTCIVIAHRLSTI---QNS-------DIIAVMSQGVVIEKGTHKK 1302
Cdd:TIGR00956 232 CWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyQCSqdayelfDKVIVLYEGYQIYFGPADK 297
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
179-360 |
5.56e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 49.77 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 179 FRRIMRMEIGWFDCTSVGELNSRFsDDINKIDEAIADQM-ALFLQRLSTALSGLLLGFYrGWKLTLVILAVSpligigAA 257
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFvEALLDGLMAILTLVMMFLY-SPKLALIVLAAV------AL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 258 VIGLSVAKF------TELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEkNLMFA--------QRWGIWKGMVMG 323
Cdd:cd18567 154 YALLRLALYpplrraTEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWL-NLLVDainadirlQRLQILFSAANG 232
|
170 180 190
....*....|....*....|....*....|....*..
gi 1390249242 324 FFTGymwclifFCYALAFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18567 233 LLFG-------LENILVIYLGALLVLD-GEFTVGMLF 261
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1217-1289 |
6.34e-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: 50.55 E-value: 6.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1217 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALD-TESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVM 1289
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
438-611 |
7.28e-06 |
|
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: 47.81 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIR-WLRDQIGIV----EQEPVLFSTTI 512
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 513 AENIRLGREeatmedivqaakdanaynfimaLP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSAL 589
Cdd:cd03215 96 AENIALSSL----------------------LSggnQQ------------------KVVLARWLARDPRVLILDEPTRGV 135
|
170 180
....*....|....*....|...
gi 1390249242 590 DNESEAKVQGALNKI-QHGHTII 611
Cdd:cd03215 136 DVGAKAEIYRLIRELaDAGKAVL 158
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1099-1311 |
7.36e-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: 50.78 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhDSKKVNVQFLRSNIGIVSQepvlFDcsimdnikygd 1178
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-KSILTNISDVHQNMGYCPQ----FD----------- 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1179 ntkeiSVERAIAAAKQAQLHDFVMSLP-EKYE--TNVGIQGSQL-----------SRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:TIGR01257 2022 -----AIDDLLTGREHLYLYARLRGVPaEEIEkvANWSIQSLGLslyadrlagtySGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1245 ATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQKGAYY 1311
Cdd:TIGR01257 2097 PTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGY 2165
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1098-1275 |
9.05e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1098 GLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNVQFLRSNI------GIVS----QEPVLFD 1167
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGIKTeltaLENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1168 CSIMDnikygdntkEISVERAIAAAKQAQLHDFvMSLPekyetnvgiqGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:PRK13538 99 QRLHG---------PGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 1390249242 1248 ALDTESEKTV-QLALDKAREGRTCIVIAH 1275
Cdd:PRK13538 159 AIDKQGVARLeALLAQHAEQGGMVILTTH 187
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
431-615 |
9.32e-06 |
|
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: 47.74 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDG------HDIRSLNIRWLRDQIGIveqE 504
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqRDEPHENILYLGHLPGL---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 505 PVLfstTIAENIR-----LGREEATMEDIVQAAKDANAYNFIMAL---PQQfdtlvgegggqmsggqkQRVAIARALIRK 576
Cdd:TIGR01189 86 PEL---SALENLHfwaaiHGGAQRTIEDALAAVGLTGFEDLPAAQlsaGQQ-----------------RRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1390249242 577 PKILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAH 615
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1219-1304 |
1.03e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1219 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVV-- 1294
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIyQLINQFKAEGLSIILVSSEMPEVLGmSDRILVMHEGRIsg 475
|
90
....*....|...
gi 1390249242 1295 ---IEKGTHKKLM 1304
Cdd:PRK10762 476 eftREQATQEKLM 488
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1086-1253 |
1.15e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1086 TYPsrPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMI-DGHdskkvnvqflrsNIGIVSQEPV 1164
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI------------KVGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1165 LfDCS--IMDNIKYG--------DNTKEISVERAIA-------AAKQAQLHDFV------------------MSLPEKyE 1209
Cdd:PRK11819 81 L-DPEktVRENVEEGvaevkaalDRFNEIYAAYAEPdadfdalAAEQGELQEIIdaadawdldsqleiamdaLRCPPW-D 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1390249242 1210 TNVgiqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:PRK11819 159 AKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1099-1292 |
1.23e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1099 LSVSVDPGQTLAFVGSSGCGKStsiQLLERFY---DPDQGTVMIDGHDSKKVNVQfLRSNIGIV-----SQEPVLF-DCS 1169
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1170 IMDNI-KYGDNTKEISVERAIAAAkqaqlhdfvmsLPEKYETNVGIQGSQ-------LSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK15439 358 LAWNVcALTHNRRGFWIKPARENA-----------VLERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1242 LDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTI-QNSDIIAVMSQG 1292
Cdd:PRK15439 427 VDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQG 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
420-468 |
1.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1390249242 420 IEFHNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLI 468
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1087-1285 |
1.34e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1087 YPSRPdiqVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERfyDPDQG---TVMIDGH---------DSKKvnvqflrs 1154
Cdd:PRK10938 270 YNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRrrgsgetiwDIKK-------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1155 NIGIVSQEPVL---FDCSIMDNIKYG--DNtkeISVERAIAAAKQaqlhdfvmSLPEKYETNVGIQGSQ-------LSRG 1222
Cdd:PRK10938 337 HIGYVSSSLHLdyrVSTSVRNVILSGffDS---IGIYQAVSDRQQ--------KLAQQWLDILGIDKRTadapfhsLSWG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 1223 EkQRIA-IARAIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRT--------------CivIAHRLSTIQNSDI 1285
Cdd:PRK10938 406 Q-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGDI 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
436-590 |
1.36e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.97 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIR--SLNIRWLRDqIGIVEQEPVLFST-TI 512
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRG-IGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 513 AENIRLG---REEATMEdivQAAKDANAynfimaLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATS 587
Cdd:PRK10895 96 YDNLMAVlqiRDDLSAE---QREDRANE------LMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 1390249242 588 ALD 590
Cdd:PRK10895 167 GVD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1217-1289 |
1.37e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 1217 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVM 1289
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
420-516 |
1.46e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.22 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFhypSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWL---RD 496
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100
....*....|....*....|.
gi 1390249242 497 QIGIVEQEPVLFS-TTIAENI 516
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNV 105
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
420-646 |
1.46e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFhYPSRPEVKilnNLSMVIKPGETTAFVGSSGAGKS----TALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLr 495
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 496 dQIGIVEQEP-VLFST--TIAENIR-----LGRE--EATMEDIVQAAKDANA------YNFIMAlpqqfdtlvgegggqm 559
Cdd:PRK10418 80 -KIATIMQNPrSAFNPlhTMHTHARetclaLGKPadDATLTAALEAVGLENAarvlklYPFEMS---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 560 sGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTV-RSADVIIGFEHGTAVE 636
Cdd:PRK10418 143 -GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVE 221
|
250
....*....|
gi 1390249242 637 RGTHEELLER 646
Cdd:PRK10418 222 QGDVETLFNA 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1088-1292 |
2.23e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1088 PSRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYdPD--QGTVMIDGhdsKKVNV----QFLRSNIGIVSQ 1161
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDG---KPVKIrnpqQAIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 E-------PVLfdcSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEKY---ETNVGiqgsQLSRGEKQRIAIAR 1231
Cdd:PRK13549 346 DrkrdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTaspELAIA----RLSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1232 AIVRDPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIyKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEG 481
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
753-1008 |
2.27e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.95 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 753 PYILVGAlcaAINGAV--TPIYSLLFSQILKTfslvdkEQQRSEIY-SMCLFFVILGCVSLFtQFLQGYNFAKSGELLTK 829
Cdd:cd18565 18 PPLLIGV---AIDAVFngEASFLPLVPASLGP------ADPRGQLWlLGGLTVAAFLLESLF-QYLSGVLWRRFAQRVQH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 830 RLRKFGFKAMLRQDIGWFDDlkNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIFVAVLIAFLFNWKLSLVISVFFP 909
Cdd:cd18565 88 DLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 910 FLALSGAVQTKMLtgfASQDKEILEKAGQItNEALSNirTVAGIGVegrfIKAF---EVELEK------SYKTAIRKAnv 980
Cdd:cd18565 166 LIIAGTYWFQRRI---EPRYRAVREAVGDL-NARLEN--NLSGIAV----IKAFtaeDFERERvadaseEYRDANWRA-- 233
|
250 260 270
....*....|....*....|....*....|..
gi 1390249242 981 YGLCYAFSQGISFLANsAAYR----YGGYLIV 1008
Cdd:cd18565 234 IRLRAAFFPVIRLVAG-AGFVatfvVGGYWVL 264
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
423-615 |
2.41e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 423 HNVTFHYPsrPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLiqrfydpcegMVTLD----GHDIRSLNIRwlrdqI 498
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkefeGEARPAPGIK-----V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPVLFST-TIAENIrlgrEEAtMEDIVQAAKDANAYNFIMALPQ-QFDTLVGEGGGQMSGGQKQ----------- 565
Cdd:PRK11819 73 GYLPQEPQLDPEkTVRENV----EEG-VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGELQEIIDAAdawdldsqlei 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 566 -----------------------RVAIARALIRKPKILLLDMATSALDNESEAKVQgalnkiQHGH----TIISVAH 615
Cdd:PRK11819 148 amdalrcppwdakvtklsggerrRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE------QFLHdypgTVVAVTH 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1095-1275 |
2.46e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1095 VLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSkkvnvqflrsnIGIVSQEPVLFDCSIMDNI 1174
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ-----------LAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1175 KYGDNT-KEISVERAIAAAKQ-----AQLHD--------FVMSLPEKYETNVGIQGSQLSR-------GEKQRIAIARAI 1233
Cdd:PRK10636 85 IDGDREyRQLEAQLHDANERNdghaiATIHGkldaidawTIRSRAASLLHGLGFSNEQLERpvsdfsgGWRMRLNLAQAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390249242 1234 VRDPKILLLDEATSALDTES----EKTVqlaldKAREGrTCIVIAH 1275
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAviwlEKWL-----KSYQG-TLILISH 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
420-652 |
2.60e-05 |
|
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: 48.65 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRF--YDPCEGMVTLdgHDIRSLNIRWLRDQ 497
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--HVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 498 IGIVEQEPVLFST-------------TIAENIR------------LGREEATMEDIVQAAKDAnAYNFIMALPQQFDTL- 551
Cdd:TIGR03269 76 SKVGEPCPVCGGTlepeevdfwnlsdKLRRRIRkriaimlqrtfaLYGDDTVLDNVLEALEEI-GYEGKEAVGRAVDLIe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 552 -------VGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNK--IQHGHTIISVAHRLSTVRS 622
Cdd:TIGR03269 155 mvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIED 234
|
250 260 270
....*....|....*....|....*....|.
gi 1390249242 623 -ADVIIGFEHGTAVERGTHEELLERkgvyFM 652
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVAV----FM 261
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
435-646 |
2.86e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 435 VKILNNLSMVIKPGETTAFVGSSGAGKSTALQLI------------QRFydpcegmvTLDGHDIRSLNIR----WLRDQI 498
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdnwhvtaDRF--------RWNGIDLLKLSPRerrkIIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 GIVEQEPvlfSTTIAENIRLGREeaTMEDI-------------VQAAKDANA---------YNFIM-ALPQQFdtlvgeg 555
Cdd:COG4170 92 AMIFQEP---SSCLDPSAKIGDQ--LIEAIpswtfkgkwwqrfKWRKKRAIEllhrvgikdHKDIMnSYPHEL------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 556 ggqmSGGQKQRVAIARALIRKPKILLLDMATSALdnESEAKVQ-----GALNKIQhGHTIISVAHRLSTV-RSADVIIGF 629
Cdd:COG4170 160 ----TEGECQKVMIAMAIANQPRLLIADEPTNAM--ESTTQAQifrllARLNQLQ-GTSILLISHDLESIsQWADTITVL 232
|
250
....*....|....*..
gi 1390249242 630 EHGTAVERGTHEELLER 646
Cdd:COG4170 233 YCGQTVESGPTEQILKS 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
419-501 |
2.93e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 419 EIEFHNVTFHYPSRP-EVKILNnlsMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQ 497
Cdd:PRK10522 322 TLELRNVTFAYQDNGfSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
....
gi 1390249242 498 IGIV 501
Cdd:PRK10522 399 FSAV 402
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
416-620 |
2.95e-05 |
|
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: 48.28 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 416 IKGEI-EFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-PCEGMVTLDGH--DIRSLnI 491
Cdd:TIGR02633 253 IGDVIlEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNP-A 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 492 RWLRDQIGIVEQE-------PVLfstTIAENIRLG-----------REEATMEDIVQAAKDANAYNFIMALP-------- 545
Cdd:TIGR02633 332 QAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSvlksfcfkmriDAAAELQIIGSAIQRLKVKTASPFLPigrlsggn 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 546 QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV 620
Cdd:TIGR02633 409 QQ------------------KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEV 466
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
143-261 |
3.22e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging 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: 350047 [Multi-domain] Cd Length: 296 Bit Score: 47.47 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQ 222
Cdd:cd18603 45 GVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLN 124
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1390249242 223 RLSTALSglllgfyrgwklTLVILAVS-PLIGIGAAVIGL 261
Cdd:cd18603 125 CLFQVIS------------TLVVISIStPIFLVVIIPLAI 152
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1092-1306 |
3.86e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1092 DIQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL---------ERFYDPDQGTVMIDGHDSKKVNVQFLRSNIGIVSQe 1162
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALagelpllsgERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1163 pvlfdcsimDNIKYGDNTKEIsveraIaaakQAQLHDfvMSLPEKYETNVGIQG------SQLSRGEKQRIAIARAIVRD 1236
Cdd:PRK10938 94 ---------GEDDTGRTTAEI-----I----QDEVKD--PARCEQLAQQFGITAlldrrfKYLSTGETRKTLLCQALMSE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 1237 PKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQGVVIEKGTHKKLMDQ 1306
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1208-1294 |
5.04e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1208 YETNVGiqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QLALDKAREGRTCIVIAHRLSTIQN-SDI 1285
Cdd:PRK10982 385 HRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDR 460
|
....*....
gi 1390249242 1286 IAVMSQGVV 1294
Cdd:PRK10982 461 ILVMSNGLV 469
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
438-644 |
6.60e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 45.99 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 438 LNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdPCEGMVTLDGHDIRSLNIR-------WLRDQigiveQEPVLF-- 508
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQ-----QSPPFAmp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 -----STTIAENIRLGREEATMEDIVQAAKDANAYN-FIMALP---QQfdtlvgegggqmsggqkqRVAIARALIR---- 575
Cdd:COG4138 86 vfqylALHQPAGASSEAVEQLLAQLAEALGLEDKLSrPLTQLSggeWQ------------------RVRLAAVLLQvwpt 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 576 ---KPKILLLDMATSALDneseakV--QGALNKI-----QHGHTIISVAHRLS-TVRSADVIIGFEHGTAVERGTHEELL 644
Cdd:COG4138 148 inpEGQLLLLDEPMNSLD------VaqQAALDRLlrelcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
451-590 |
6.66e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 451 TAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGH---DIRSlNIrWL---RDQIGIVEQEPVLFS-TTIAENIRLGreea 523
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK-GI-CLppeKRRIGYVFQDARLFPhYKVRGNLRYG---- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 524 tMedivqAAKDanaynfimalPQQFDTLVGEGGGQMSGG---------QKQRVAIARALIRKPKILLLDMATSALD 590
Cdd:PRK11144 101 -M-----AKSM----------VAQFDKIVALLGIEPLLDrypgslsggEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
430-613 |
7.81e-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: 45.33 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 430 PSRPEVKILNNLSMVIKPGETTAFVGSSGAGKST---ALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIgIVEQEPV 506
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 507 LFSTTiaenirlgreeaTMEDIVQAAKDANAYNFIMALP--QQfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDM 584
Cdd:cd03233 94 HFPTL------------TVRETLDFALRCKGNEFVRGISggER-----------------KRVSIAEALVSRASVLCWDN 144
|
170 180 190
....*....|....*....|....*....|..
gi 1390249242 585 ATSALDNESE---AKVQGALNKIQHGHTIISV 613
Cdd:cd03233 145 STRGLDSSTAleiLKCIRTMADVLKTTTFVSL 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
434-619 |
8.89e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQ-RFYDPC-EGMVTLDGHDIRSLNIRwlrdQIGIVEQEPVLFS-T 510
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 511 TIAEN------IRLGReEATMEDIVQAAKDANAYnfiMALPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRKPKILLLD 583
Cdd:PLN03211 156 TVRETlvfcslLRLPK-SLTKQEKILVAESVISE---LGLTKCENTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 1390249242 584 MATSALDNESEAKVQGALNKIQH-GHTIISVAHRLST 619
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSS 268
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1217-1253 |
9.03e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 9.03e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1390249242 1217 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
431-520 |
1.05e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIR-WLRDQIGIVEQE-PVLF 508
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQElNLVL 86
|
90
....*....|..
gi 1390249242 509 STTIAENIRLGR 520
Cdd:PRK10982 87 QRSVMDNMWLGR 98
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1093-1278 |
1.07e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1093 IQVLNGLSVSVDPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGTVMIDGHdsKKVNVQFLR-------SNI---GIVS 1160
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGF--PKKQETFARisgyceqNDIhspQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1161 QEPVLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPekyetnvGIQGsqLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:PLN03140 971 RESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*....
gi 1390249242 1241 LLDEATSALDTESEKTVQLAL-DKAREGRTCIVIAHRLS 1278
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
771-1037 |
1.21e-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: 45.58 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 771 IYSLLFSQILKTFSL------------VDKEQQRSEIYSMCLFFVILGCVSLFTQFLQGYNFAKSGELLTKRLRKFGFKA 838
Cdd:cd18555 5 ISILLLSLLLQLLTLlipiltqyvidnVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 839 MLRQDIGWFDdlKNNPGVLTTRlATDASQVQGATGSQV-GMMVNSFTNIFVAVLIaFLFNWKLSLVISVFFPFLALSGAV 917
Cdd:cd18555 85 LLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQILSNQViSLIIDLLLLVIYLIYM-LYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 918 QTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLCYAFSQGISFLANS 997
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 998 AAYRYGGYLIVYEDLNF----------SYVFRVVSSIAMSATAVGRTFSY 1037
Cdd:cd18555 241 LILWIGAYLVINGELTLgeliafsslaGSFLTPIVSLINSYNQFILLKSY 290
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1215-1288 |
1.43e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1215 QGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKARE--GRTCIVIAHRLSTIQN-SDIIAV 1288
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHV 144
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
423-638 |
1.45e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.92 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 423 HNVTFHYPSRpevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNI--------RWL 494
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 495 -RDQIGIVEQEP-------VLFSTTIAEniRL--------GREEATMEDIVQAAK-DANAynfIMALPQQFdtlvgeggg 557
Cdd:PRK11701 87 lRTEWGFVHQHPrdglrmqVSAGGNIGE--RLmavgarhyGDIRATAGDWLERVEiDAAR---IDDLPTTF--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 558 qmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGTA 634
Cdd:PRK11701 153 --SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGRV 230
|
....
gi 1390249242 635 VERG 638
Cdd:PRK11701 231 VESG 234
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
441-463 |
1.99e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 45.31 E-value: 1.99e-04
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
114-261 |
2.00e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), 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: 350045 [Multi-domain] Cd Length: 314 Bit Score: 45.00 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 114 WINSSFNQNMT----NGTSCGLVDINSEVIKFS-GIYAGVGVAVLILGYFQIRL---WVITGARQIR-KMrkfyFRRIMR 184
Cdd:cd18601 29 WANLEEKLNDTtdrvQGENSTNVDIEDLDRDFNlGIYAGLTAATFVFGFLRSLLffhVAVSASKNLHnKM----FASVLR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 185 MEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLllgfyrgwkltLVILAVSPLIGIGAAVIGL 261
Cdd:cd18601 105 APIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVV-----------LLAVVVNPWVLIPVIPLVI 170
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
193-339 |
2.68e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 44.79 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 193 TSVGELNSRFSDDINKIDEAIADQMALFLQRLSTALSGLLLgfYRgwkltlvILAVSPLIGIGAAVIGLSV-AKFTELEL 271
Cdd:cd18596 112 ASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFL--YR-------LLGWSALVGLAVMVLLLPLnGYLAKRYS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 272 KAYAKAGSIAD-------EVLSSIRTVAAFGGENKEVERyeknlMFAQR----WGIWKGMVMGFFTGYMWCLI------- 333
Cdd:cd18596 183 RAQKELMKARDarvqlvtEVLQGIRMIKFFAWERKWEER-----ILEAReeelKWLRKRFLLDLLLSLLWFLIpilvtvv 257
|
....*..
gi 1390249242 334 -FFCYAL 339
Cdd:cd18596 258 tFATYTL 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1100-1294 |
2.92e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1100 SVSVDPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGhdsKKVNVQFLRSNI--GIV------SQEPVLFDCSIM 1171
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1172 DNIKygdntkeISVERA-------IAAAKQAQLHD-FVMSLPEKY---ETNVGiqgsQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:PRK11288 350 DNIN-------ISARRHhlragclINNRWEAENADrFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249242 1241 LLDEATSALD--TESEkTVQLALDKAREGRTCIVIAHRLSTIQN-SDIIAVMSQGVV 1294
Cdd:PRK11288 419 LLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
883-1013 |
3.91e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 44.13 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 883 FTNIFVAVLiaFLFNWKLSLVISVFFPFLALSGAVQTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKA 962
Cdd:cd18586 125 WAPLFLAVI--FLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRR 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 963 FEVELEKSYKTAIRKANVYGLCYAFSQGISFLANSAAYRYGGYLIVYEDLN 1013
Cdd:cd18586 203 WEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELT 253
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
433-590 |
4.01e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 433 PEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLI----QRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLF 508
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 509 STTIAEN----IRL----GREEATMEDiVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGG-QKQRVAIARALIRKPKI 579
Cdd:TIGR00956 152 HLTVGETldfaARCktpqNRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGgERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 1390249242 580 LLLDMATSALD 590
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
434-501 |
4.30e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 4.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQ----LIQrfydPCEGMVTLDGHDIRSLNIRWLRdQIGIV 501
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgILV----PTSGEVRVLGYVPFKRRKEFAR-RIGVV 100
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1217-1286 |
4.96e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 4.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 1217 SQLSRGEKQRIAIARAIVRDPK--ILLLDEATSALDTESEKTVQLALDKAR-EGRTCIVIAHRLSTIQNSDII 1286
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWI 158
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
420-615 |
5.49e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYPSRPevKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVtldghdIRSLNIRwlrdqIG 499
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 IVEQEPV----LFSTTIAENIRLgrEEATMEDIVQAAKDANAYNFIMALpQQFDTLvgegggqmSGGQKQRVAIARALIR 575
Cdd:PLN03073 576 VFSQHHVdgldLSSNPLLYMMRC--FPGVPEQKLRAHLGSFGVTGNLAL-QPMYTL--------SGGQKSRVAFAKITFK 644
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390249242 576 KPKILLLDMATSALDNES-EAKVQGaLNKIQHGhtIISVAH 615
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAvEALIQG-LVLFQGG--VLMVSH 682
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1218-1304 |
6.97e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1218 QLSRGEKQRIAIARAIVRDPKILLLDEATSALdtesEKTVQ------LALDKAREGRTCIVIAHRLSTI-QNSDIIAVMS 1290
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAM----EPTTQaqifrlLTRLNQNNNTTILLISHDLQMLsQWADKINVLY 233
|
90
....*....|....
gi 1390249242 1291 QGVVIEKGTHKKLM 1304
Cdd:PRK15093 234 CGQTVETAPSKELV 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1218-1298 |
7.78e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1218 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQLALDKARegRTCIVIAHR---LSTIQnSDIIAVMSQGVV 1294
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHArefLNTVV-TDILHLHGQKLV 420
|
....
gi 1390249242 1295 IEKG 1298
Cdd:PLN03073 421 TYKG 424
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
424-487 |
9.49e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.86 E-value: 9.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249242 424 NVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIR 487
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1089-1292 |
1.09e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1089 SRPDIQVLNGLSVSVDPGQTLAFVGSSGCGKStsiQLLERFYDPDQ---GTVMIDGHD-SKKVNVQFLRSNIGIVSQ--- 1161
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKragGEIRLNGKDiSPRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 1162 EPVLF-DCSIMDNIKYGDNTK-----------EISVERAIAAAKQAQLHDFVMSLpekyETNVGiqgsQLSRGEKQRIAI 1229
Cdd:PRK09700 349 DNGFFpNFSIAQNMAISRSLKdggykgamglfHEVDEQRTAENQRELLALKCHSV----NQNIT----ELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249242 1230 ARAIVRDPKILLLDEATSALDTESEKTVQLALDK-AREGRTCIVIAHRLSTIQN-SDIIAVMSQG 1292
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEG 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
418-590 |
1.13e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 418 GEI--EFHNVTFHYPSRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYdP--CEGMVTLDGhdiRSLNIRW 493
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDG---KPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 494 LRDQI--------------GIVeqePVLfstTIAENIRL--------------GREEATMEDIVQ--AAKDANAYNFIMA 543
Cdd:PRK13549 332 PQQAIaqgiamvpedrkrdGIV---PVM---GVGKNITLaaldrftggsriddAAELKTILESIQrlKVKTASPELAIAR 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 544 LP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALD 590
Cdd:PRK13549 406 LSggnQQ------------------KAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
235-360 |
1.62e-03 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 42.10 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 235 FYRGWKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLM----- 309
Cdd:cd18588 137 FYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAryvka 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1390249242 310 -F-AQRWGIWKGMVMGFFTGYMWCLIffcyalaFWYGSRLVLDeGEYTPGTLI 360
Cdd:cd18588 217 sFkTANLSNLASQIVQLIQKLTTLAI-------LWFGAYLVMD-GELTIGQLI 261
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
437-590 |
1.63e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 437 ILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHdirslnirWlrdQIGIVEQE-PVLFSTTIAEN 515
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN--------W---QLAWVNQEtPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 516 IRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTL----------------------VGEGGGQMSGGQKQRVAIARAL 573
Cdd:PRK10636 85 IDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIdawtirsraasllhglgfsneqLERPVSDFSGGWRMRLNLAQAL 164
|
170
....*....|....*..
gi 1390249242 574 IRKPKILLLDMATSALD 590
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD 181
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
431-625 |
1.72e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.33 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSL------NIRWLRDQIGIveqE 504
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 505 PVLfstTIAENIRL---GREEATMEDIVQAAKDANAYNFiMALP-------QQfdtlvgegggqmsggqkQRVAIARALI 574
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPvrqlsagQQ-----------------RRVALARLWL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390249242 575 RKPKILLLDMATSALDNESEAKVQGAL-NKIQHGHTIISVAHRLSTVRSADV 625
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLaQHAEQGGMVILTTHQDLPVASDKV 197
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
566-633 |
1.84e-03 |
|
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: 40.77 E-value: 1.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 566 RVAIARALIRKPK--ILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTVRSADVIIGFEHGT 633
Cdd:cd03238 95 RVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
431-583 |
2.21e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 431 SRPEVkiLNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRwlrDQI------------ 498
Cdd:COG1129 263 SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR---DAIragiayvpedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 499 --GIVEQEPVLFSTTIAeN---------IRLGREEATMEDIVQA--AKDANAYNFIMALP---QQfdtlvgegggqmsgg 562
Cdd:COG1129 338 geGLVLDLSIRENITLA-SldrlsrgglLDRRRERALAEEYIKRlrIKTPSPEQPVGNLSggnQQ--------------- 401
|
170 180
....*....|....*....|.
gi 1390249242 563 qkqRVAIARALIRKPKILLLD 583
Cdd:COG1129 402 ---KVVLAKWLATDPKVLILD 419
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
436-643 |
2.34e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 436 KILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYD-PCEGM---VTLDGHDIRSLNIRWLRDQIG----IVEQEP-- 505
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISEKERRNLVGaevaMIFQDPmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 506 -------VLFSTTIAENIRLG------REEA----TMEDIVQAAKDANAYnfimalPQQFDtlvgegggqmsGGQKQRVA 568
Cdd:PRK11022 101 slnpcytVGFQIMEAIKVHQGgnkktrRQRAidllNQVGIPDPASRLDVY------PHQLS-----------GGMSQRVM 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 569 IARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH--TIISVAHRLSTV-RSADVIIGFEHGTAVERGTHEEL 643
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1103-1145 |
2.62e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 2.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1390249242 1103 VDPGQTLAFVGSSGCGKSTSI-QLLErfyDPDQGTVMIDGHDSK 1145
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVnALLG---EEVQKTGAVREDDSK 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
434-500 |
2.66e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249242 434 EVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLI--QRFYDPCEGMVTLDGHDIRSLNIRwLRDQIGI 500
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGI 86
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
567-633 |
3.19e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249242 567 VAIARALIRKPK---ILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTVRSADVIIGFEHGT 633
Cdd:PRK00635 1708 IKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLIEMGPGS 1778
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
420-626 |
3.21e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 420 IEFHNVTFHYpsrpEVKILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMVTldghdIRSLNIRWLrdqig 499
Cdd:PRK13541 2 LSLHQLQFNI----EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNI----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 500 iveQEPvlFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRKP 577
Cdd:PRK13541 68 ---AKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390249242 578 KILLLDMATSALDNESEAKVQGALN-KIQHGHTIISVAHRLSTVRSADVI 626
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
412-479 |
3.49e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249242 412 KLDRIKGEIEfhNVTFHYPSRPevkILNNLSMVIKPGETTAFVGSSGAGKSTALQLIQRFYDPCEGMV 479
Cdd:PRK15064 314 KLHRNALEVE--NLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
839-1007 |
4.72e-03 |
|
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: 40.60 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 839 MLRQDIGWFDDLKNnpGVLTTRLATDASQVQGATGSQV-GMMVNSFTNIFVAVLIaFLFNWKLSLVISVFFPFLALSGAV 917
Cdd:cd18778 83 LQRLSLRYFDDRQT--GDLMSRVINDVANVERLIADGIpQGITNVLTLVGVAIIL-FSINPKLALLTLIPIPFLALGAWL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 918 QTKMLTGFASQDKEILEKAGQITNEALSNIRTVAGIGVEGRFIKAFEVELEKSYKTAIRKANVYGLcyaFSQGISFLANS 997
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAI---FHPLMEFLTSL 236
|
170
....*....|...
gi 1390249242 998 ---AAYRYGGYLI 1007
Cdd:cd18778 237 gtvLVLGFGGRLV 249
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
144-297 |
4.87e-03 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 40.66 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 144 IYAGVGV--AVLILGYFQIRLwvITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDINKIDEAIADQMALFL 221
Cdd:cd18559 43 VLGALAIlqGITVFQYSMAVS--IGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWM 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249242 222 QRLSTALSGLLLGFYRGwKLTLVILAVSPLIGIGAAVIGLSVAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGE 297
Cdd:cd18559 121 GPLQNVIGLYLLILLAG-PMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWE 195
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
143-303 |
5.87e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 40.47 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 143 GIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFDCTSVGELNSRFSDDInkidEAIADQMALFL- 221
Cdd:cd18584 41 LLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGV----DALDGYFARYLp 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 222 QRLSTALSGLLLG---FYRGWkLTLVILAVS-PLIGIGAAVIGLSVAKFTELELKAYAK-AGSIADeVLSSIRTVAAFGG 296
Cdd:cd18584 117 QLVLAAIVPLLILvavFPLDW-VSALILLVTaPLIPLFMILIGKAAQAASRRQWAALSRlSGHFLD-RLRGLPTLKLFGR 194
|
....*..
gi 1390249242 297 ENKEVER 303
Cdd:cd18584 195 ARAQAAR 201
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
121-309 |
7.26e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 39.90 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 121 QNMTNGTSCGLVDINSEVIKFSGIYAGVGVAVLILGYFQIRLWVITGARQIRKMRKFYFRRIMRMEIGWFdctsvgeLNS 200
Cdd:cd18560 20 GRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWH-------LSK 92
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249242 201 RFSDDINKID---EAIADQMALFLQRLSTALSGLLLgfyrgwklTLVILAVSPLIGIGAAVIgLSVA------------- 264
Cdd:cd18560 93 KTGEVVRIMDrgtESANTLLSYLVFYLVPTLLELIV--------VSVVFAFHFGAWLALIVF-LSVLlygvftikvtewr 163
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170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390249242 265 -KFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLM 309
Cdd:cd18560 164 tKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVK 209
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