|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-532 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 573.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQEFKASEHETVGA 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 IFTAAFQDLIEMEGQIQSLQQRIDTAQAteqqrLVHQLAELQEQYADRGGFEYHSRIRGVTIGLGFQLKDLEKAFGTFSG 164
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDE-----DLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 165 GEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSYTGNYT 244
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 245 QYLDKKAKRDRALDAAYNKQMKELTRQQKIVDRLRdyNSVQSSRRAASREKAIERITPIERRQDRRSLHFSFSPKVLSGN 324
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFR--AKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 325 DVLMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDEalLA 404
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDrigligpngagKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEE--LD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 405 PNETLIDAIRDIDSHLTDGDIRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREIL 484
Cdd:COG0488 392 PDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1222187810 485 EDALCGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETIGNYDDYAR 532
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-534 |
1.23e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 275.23 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQEFKASEHET 81
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 VgaiftaafQDLIEMeG-----QIQSLQQRI-DTAQATEQQRLvhQLAELQEQYADRGGFEYHSRIRGVTIGLGFqlkDL 155
Cdd:PRK15064 81 V--------LDTVIM-GhtelwEVKQERDRIyALPEMSEEDGM--KVADLEVKFAEMDGYTAEARAGELLLGVGI---PE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 156 EKAFGTFSG---GEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCkriceie 232
Cdd:PRK15064 147 EQHYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVC------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 233 nTHMVS--------YTGNYTQYLDKKAK-RDRAL-DAAYNK-QMKELtrqQKIVDRLRDYNSvqSSRRAASREKAIERIT 301
Cdd:PRK15064 220 -THMADldygelrvYPGNYDEYMTAATQaRERLLaDNAKKKaQIAEL---QSFVSRFSANAS--KAKQATSRAKQIDKIK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 302 PIERRQDRR---SLHFSFSPKVLsgNDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKS 378
Cdd:PRK15064 294 LEEVKPSSRqnpFIRFEQDKKLH--RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 379 DSGRIVFGRKVYPGYYAQEPdEALLAPNETLIDAIRDidsHLTDGD----IRNILASFLFTGESVFKHSGDLSGGEKARL 454
Cdd:PRK15064 372 DSGTVKWSENANIGYYAQDH-AYDFENDLTLFDWMSQ---WRQEGDdeqaVRGTLGRLLFSQDDIKKSVKVLSGGEKGRM 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 455 NMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETIGNYDDYARTK 534
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-635 |
7.16e-83 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 273.36 E-value: 7.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQEFKASEHET 81
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 VGAIFTAAFQDLIEMEGQIQSLQQRIDTAQateQQRLVHQLAELQEQYADRGGFEYHSRIRGVTIGLGFqlkDLEKAFGT 161
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETDP---SEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL---DPDAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 162 FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSYTG 241
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 242 NYTQYLDKKAK--RDRAL-DAAYNKQMKE---LTRQQKIVDRLRDYNSVqssrRA--ASREkaiERItpiERRQDRRSLH 313
Cdd:PRK11147 237 NYDQYLLEKEEalRVEELqNAEFDRKLAQeevWIRQGIKARRTRNEGRV----RAlkALRR---ERS---ERREVMGTAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 314 FSFSPKVLSGNDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGY 393
Cdd:PRK11147 307 MQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 394 YAQEpdEALLAPNETLIDAIRDIDSHLT-DGDIRNILA---SFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLM 469
Cdd:PRK11147 387 FDQH--RAELDPEKTVMDNLAEGKQEVMvNGRPRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLIL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 470 DEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANR--IFEltPEG-IEETIGNYDDyarTKQNQSdreallaq 546
Cdd:PRK11147 465 DEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFE--GNGkIGRYVGGYHD---ARQQQA-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 547 NHAPQINKTRRKQERQQAKALESERRRQKK-------ALAQLEEQMESNDQRIAAYEADMCQPSFY-DDMVYAQKITDDY 618
Cdd:PRK11147 532 QYLALKQPAVKKKEEAAAPKAETVKRSSKKlsyklqrELEQLPQLLEDLEAEIEALQAQVADADFFsQPHEQTQKVLADL 611
|
650
....*....|....*..
gi 1222187810 619 HALKADNENIIQQWEDL 635
Cdd:PRK11147 612 ADAEQELEVAFERWEEL 628
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-530 |
2.30e-82 |
|
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: 269.88 E-value: 2.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININeLSFSYGVHsifnnldfriddaehLGLIGRNGCGKSTFFKLLTGechhdtgtLDK--------KNGLTLGLLSQE 73
Cdd:TIGR03719 21 LKDIS-LSFFPGAK---------------IGVLGLNGAGKSTLLRIMAG--------VDKdfngearpQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 74 FKASEHETVGAIFTAAFQDliemegqIQSLQQRIDTAQA------TEQQRLVHQLAELQEQYADRGGFEYHSRIRGVTIG 147
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAE-------IKDALDRFNEISAkyaepdADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 148 LgfQLKDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKR 227
Cdd:TIGR03719 150 L--RCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 228 ICEIENTHMVSYTGNYTQYLDKKAKR----DRAlDAAYNKQMK-EL--------TRQQKIVDRLRDYNSVQSSRRAASRE 294
Cdd:TIGR03719 228 ILELDRGRGIPWEGNYSSWLEQKQKRleqeEKE-ESARQKTLKrELewvrqspkGRQAKSKARLARYEELLSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 295 KAIERITPIERRqdrrslhfsfspkvlsGNDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMK 374
Cdd:TIGR03719 307 TAEIYIPPGPRL----------------GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 375 QIKSDSGRIVFGRKVYPGYYAQEPDEalLAPNETLIDAIRDIDSHLTDGDI----RNILASFLFTGESVFKHSGDLSGGE 450
Cdd:TIGR03719 371 QEQPDSGTIEIGETVKLAYVDQSRDA--LDPNKTVWEEISGGLDIIKLGKReipsRAYVGRFNFKGSDQQKKVGQLSGGE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 451 KARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIfeLTPEG---IEETIGNY 527
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFEGdshVEWFEGNF 526
|
...
gi 1222187810 528 DDY 530
Cdd:TIGR03719 527 SEY 529
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-641 |
1.98e-81 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 269.73 E-value: 1.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQEFKASEhet 81
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 vgaifTAAFQDLIEMEGQIQSLQQRIDTAQATEQQrlvHQLAELQEQYADRGGFEYHSRIRGVTIGLGFQLKDLEKAFGT 161
Cdd:PRK10636 78 -----QPALEYVIDGDREYRQLEAQLHDANERNDG---HAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 162 FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSYTG 241
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 242 NYTQYLDKKAKRDRALDAAYNKQMKELTRQQKIVDRLRDYNSvqSSRRAASREKAIERITPIERRQDRRSLHFSF-SPKV 320
Cdd:PRK10636 230 NYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKAT--KAKQAQSRIKMLERMELIAPAHVDNPFHFSFrAPES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 321 LSgNDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDE 400
Cdd:PRK10636 308 LP-NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 401 ALLApNETLIDAIRDIDSHLTDGDIRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST 480
Cdd:PRK10636 387 FLRA-DESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 481 REILEDALCGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETIGNYDDYARTKQNQSDREAllAQNHAPQINKTRRKQE 560
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQEN--QTDEAPKENNANSAQA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 561 RQQAKALESERRRQ----KKALAQLEEQMESNDQRIAAYEADMCQPSFYDDMVYAQkITDDYH---ALKADNENIIQQWE 633
Cdd:PRK10636 544 RKDQKRREAELRTQtqplRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAE-LTACLQqqaSAKSGLEECEMAWL 622
|
....*...
gi 1222187810 634 DLALQLEE 641
Cdd:PRK10636 623 EAQEQLEQ 630
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-530 |
8.79e-74 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 246.95 E-value: 8.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 32 GLIGRNGCGKSTFFKLLTGechhdtgtLDKKN--------GLTLGLLSQEFKASEHETVGAIFTAAFQDliemegqIQSL 103
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAG--------VDKEFegearpapGIKVGYLPQEPQLDPEKTVRENVEEGVAE-------VKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 104 QQR---IDTAQATEQ---QRLVHQLAELQEQYADRGGFEYHSRIRGVTIGLgfQLKDLEKAFGTFSGGEKTRIALGCLLL 177
Cdd:PRK11819 102 LDRfneIYAAYAEPDadfDALAAEQGELQEIIDAADAWDLDSQLEIAMDAL--RCPPWDAKVTKLSGGERRRVALCRLLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 178 QSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSYTGNYTQYLDKKAKR---- 253
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRlaqe 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 254 DRAlDAAYNKQMK-EL--------TRQQKIVDRLRDYNSVQSSRRAASREKAIERITPIERrqdrrsLhfsfspkvlsGN 324
Cdd:PRK11819 260 EKQ-EAARQKALKrELewvrqspkARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPR------L----------GD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 325 DVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDEalLA 404
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDA--LD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 405 PNETLIDAIRDIDSHLTDGDI----RNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST 480
Cdd:PRK11819 401 PNKTVWEEISGGLDIIKVGNReipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 481 REILEDALCGYEGTLLFISHDRYFLNRVANRIfeLTPEGIEETI---GNYDDY 530
Cdd:PRK11819 481 LRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFEGDSQVEwfeGNFQEY 531
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
329-584 |
6.40e-51 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 184.50 E-value: 6.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDealLAPNET 408
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDriglvgrngagKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP---LDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 409 LIDAIRDIDSHLT--------------------------------------DGDIRNILASFLFTGESVFKHSGDLSGGE 450
Cdd:COG0488 78 VLDTVLDGDAELRaleaeleeleaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 451 KARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETIGNYDDY 530
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 531 ARTKQnqsDREALLAQNHAPQINKTRRKQE---RQQAKAleSERRRQK---KALAQLEEQ 584
Cdd:COG0488 238 LEQRA---ERLEQEAAAYAKQQKKIAKEEEfirRFRAKA--RKAKQAQsriKALEKLERE 292
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
327-519 |
2.07e-43 |
|
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: 152.60 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQepdeallapn 406
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 407 etlidairdidshltdgdirnilasflftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILED 486
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 1222187810 487 ALCGYEGTLLFISHDRYFLNRVANRIFELTPEG 519
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-535 |
2.75e-42 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 163.11 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTgeCHHDTGTldKKNGLTLGLlsqefkasEHETV 82
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGI--PKNCQILHV--------EQEVV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 GAIfTAAFQ----------DLIEMEGQIQSLQQRIDTAQATEQQR-----------LVHQLAELQEQYADRGGFEYHSRI 141
Cdd:PLN03073 246 GDD-TTALQcvlntdiertQLLEEEAQLVAQQRELEFETETGKGKgankdgvdkdaVSQRLEEIYKRLELIDAYTAEARA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 142 RGVTIGLGFQLKDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFL 221
Cdd:PLN03073 325 ASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 222 DRVCKRICEIENTHMVSYTGNYTQYLDKKAKRDRALDAAYNKQMKELTRQQKIVDRLRdYNSVQSSrRAASREKAIERIT 301
Cdd:PLN03073 405 NTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFR-YNAKRAS-LVQSRIKALDRLG 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 302 PIERRQDRRSLHFSF-------SPKVLSGNDVlmveglekSF---GDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQI 371
Cdd:PLN03073 483 HVDAVVNDPDYKFEFptpddrpGPPIISFSDA--------SFgypGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 372 LMKQIKSDSGRIVFGRKVYPGYYAQEPDEALLAPNETLIDAIRDIDShLTDGDIRNILASFLFTGESVFKHSGDLSGGEK 451
Cdd:PLN03073 555 ISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPG-VPEQKLRAHLGSFGVTGNLALQPMYTLSGGQK 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 452 ARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETIGNYDDYA 531
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYK 713
|
....
gi 1222187810 532 RTKQ 535
Cdd:PLN03073 714 KTLQ 717
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-249 |
2.02e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 157.53 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQEfkasehet 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 vgaiftaafqdliemegqiqslQQRIDtaqatEQQRLVHQLAELQEqyadrGGFEYHsrIRGVTIGLGFQLKDLEKAFGT 161
Cdd:COG0488 387 ----------------------QEELD-----PDKTVLDELRDGAP-----GGTEQE--VRGYLGRFLFSGDDAFKPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 162 FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSYTG 241
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPG 512
|
....*...
gi 1222187810 242 NYTQYLDK 249
Cdd:COG0488 513 GYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-235 |
1.65e-36 |
|
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: 133.34 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQefkasehetv 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 gaiftaafqdliemegqiqslqqridtaqateqqrlvhqlaelqeqyadrggfeyhsrirgvtiglgfqlkdlekafgtF 162
Cdd:cd03221 71 -------------------------------------------------------------------------------L 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 163 SGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTH 235
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-251 |
2.76e-23 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 103.82 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTldkkngltlgllsqeFKASEHETVGA 84
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT---------------VKWSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 I---FTAAF-QDLIEMEGQIQSLQQRIDtaqatEQQrlvhqlaelqeqyadrggfeyhsrIRGVTIGLGFQLKDLEKAFG 160
Cdd:PRK15064 387 YaqdHAYDFeNDLTLFDWMSQWRQEGDD-----EQA------------------------VRGTLGRLLFSQDDIKKSVK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 161 TFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSYT 240
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFS 517
|
250
....*....|.
gi 1222187810 241 GNYTQYLDKKA 251
Cdd:PRK15064 518 GTYEEYLRSQG 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
331-591 |
3.72e-20 |
|
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: 94.23 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 331 GLEKSF-GDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQIlMKQIKSD-SGRIVF--GRKVypGYYAQEPD------- 399
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-MAGVDKDfNGEARPqpGIKV--GYLPQEPQldptktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 400 --------------------------------EALLAPNETLIDAIRDIDSHLTDGDI-RNILASFLFTGESVFKHsgdL 446
Cdd:TIGR03719 86 renveegvaeikdaldrfneisakyaepdadfDKLAAEQAELQEIIDAADAWDLDSQLeIAMDALRCPPWDADVTK---L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 447 SGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIFELT-PEGIEETiG 525
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDrGRGIPWE-G 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 526 NYDDYARTKQNQSDREAllaqnhapqinktrrKQERQQAKALESE--------RRRQKKALAQLE--EQMESNDQR 591
Cdd:TIGR03719 242 NYSSWLEQKQKRLEQEE---------------KEESARQKTLKRElewvrqspKGRQAKSKARLAryEELLSQEFQ 302
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-261 |
4.31e-19 |
|
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: 86.84 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT-----LDKKNGLT-----LGLLS 71
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgEDVRKEPRearrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 72 QEFKASEHETVgaiftaafQDLIEMEGQIQSLQQRIDTAQAteqQRLVHQLaELQEqyadrggfeyhsrirgvtiglgfq 151
Cdd:COG4555 81 DERGLYDRLTV--------RENIRYFAELYGLFDEELKKRI---EELIELL-GLEE------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 152 lkDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLDRVCKRI 228
Cdd:COG4555 125 --FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRV 202
|
250 260 270
....*....|....*....|....*....|...
gi 1222187810 229 CEIENTHMVsYTGNYTQYLDKKAKRDraLDAAY 261
Cdd:COG4555 203 VILHKGKVV-AQGSLDELREEIGEEN--LEDAF 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-512 |
9.96e-19 |
|
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: 89.58 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSY--GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHD---TGTLdKKNGLTLGLLSQEFKA 76
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEV-LLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 77 SEhetVGAIFtaafQDlieMEGQIQSLqqridtaqateqqRLVHQLAE-LQEQYADRGgfEYHSRIRGVtiglgFQLKDL 155
Cdd:COG1123 83 RR---IGMVF----QD---PMTQLNPV-------------TVGDQIAEaLENLGLSRA--EARARVLEL-----LEAVGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 156 EKAFG----TFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD----FESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKR 227
Cdd:COG1123 133 ERRLDryphQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 228 IceienthMVSYTGnytqyldkkakrdraldaaynkqmkeltrqqKIVDRlrdynsvQSSRRAASREKAIERITPIERRQ 307
Cdd:COG1123 213 V-------VVMDDG-------------------------------RIVED-------GPPEEILAAPQALAAVPRLGAAR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 308 DRRSLHFSFSPKVLSgndvlmVEGLEKSF-----GDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGR 382
Cdd:COG1123 248 GRAAPAAAAAEPLLE------VRNLSKRYpvrgkGGVRAVDDVSLTLRRGEtlglvgesgsgKSTLARLLLGLLRPTSGS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 383 IVF-GRKVYP-------------GYYAQEPDEALLaPNETLIDAIRD-IDSH--LTDGDIRNILASFLftgESV------ 439
Cdd:COG1123 322 ILFdGKDLTKlsrrslrelrrrvQMVFQDPYSSLN-PRMTVGDIIAEpLRLHglLSRAERRERVAELL---ERVglppdl 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 440 -FKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-EILE--DALCGYEG-TLLFISHDRYFLNRVANRI 512
Cdd:COG1123 398 aDRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQaQILNllRDLQRELGlTYLFISHDLAVVRYIADRV 475
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
327-517 |
2.45e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 83.71 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYP-----------GYYA 395
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSampppewrrqvAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 QEPdeALLApnETLIDAIRDIDS----HLTDGDIRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDE 471
Cdd:COG4619 81 QEP--ALWG--GTVRDNLPFPFQlrerKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 472 PTNHIDMSTREILEDALCGY----EGTLLFISHDRYFLNRVANRIFELTP 517
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-233 |
2.81e-17 |
|
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: 80.97 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELSFSYGVHS--IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQEFkaseHETV 82
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 GAIFtaafQDlieMEGQIQSLQQRIDTAQATEQQRLV-HQLAELQEQYADRGGFEyhsrirgvtiglGFQLKDLEkafgT 161
Cdd:cd03225 78 GLVF----QN---PDDQFFGPTVEEEVAFGLENLGLPeEEIEERVEEALELVGLE------------GLRDRSPF----T 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 162 FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNA---FIIVSHDRFFLDRVCKRICEIEN 233
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
229-314 |
7.21e-17 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 75.69 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 229 CEIENTHMVSYTGNYTQYLDKKAKRDRALDAAYNKQMKELTRQQKIVDRLRDYNSvqSSRRAASREKAIERITPIER-RQ 307
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKAS--KAKQAQSRIKALEKMERIEKpER 78
|
....*..
gi 1222187810 308 DRRSLHF 314
Cdd:pfam12848 79 DKPKLRF 85
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
329-515 |
7.81e-17 |
|
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: 78.06 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKvypgyyaqepdeallapnet 408
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 409 lidairDIDSHLTDGDIRNIlaSFLFtgesvfkhsgDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDAL 488
Cdd:cd00267 62 ------DIAKLPLEELRRRI--GYVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|
gi 1222187810 489 CGY--EG-TLLFISHDRYFLNRVANRIFEL 515
Cdd:cd00267 124 RELaeEGrTVIIVTHDPELAELAADRVIVL 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
416-574 |
1.66e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 83.37 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 416 IDSHLTDGDIRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTL 495
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTF 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 496 LFISHDRYFLNRVANRIFELTPEGIEETIGNYDDYARtkqnqsdreallaqnhapqinkTRRKQERQQAKALES-ERRRQ 574
Cdd:PLN03073 395 IVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFER----------------------TREEQLKNQQKAFESnERSRS 452
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-236 |
1.68e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 78.70 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 8 LSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT--LDKKNGLTL---------GLLSQE--- 73
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEiyLDGKPLSAMpppewrrqvAYVPQEpal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 74 FkaseHETVGAIFTAAFQdliemegqiqSLQQRIDtaqateQQRLVHQLAELqeqyadrggfeyhsrirgvtiglGFQLK 153
Cdd:COG4619 86 W----GGTVRDNLPFPFQ----------LRERKFD------RERALELLERL-----------------------GLPPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 154 DLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFES----LNWLESFLNNYKNAFIIVSHDRFFLDRVCKRIC 229
Cdd:COG4619 123 ILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVL 202
|
....*..
gi 1222187810 230 EIENTHM 236
Cdd:COG4619 203 TLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
329-515 |
1.75e-16 |
|
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: 77.44 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFGRKVYP---------GYYaqeP 398
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEiygllgpngagKTTLIKIILGLLKPDSGEIkVLGKDIKKepeevkrriGYL---P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 DEALLAPNETLIDAIRdidshltdgdirnilasflftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHIDM 478
Cdd:cd03230 80 EEPSLYENLTVRENLK-------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1222187810 479 STREILEDALCGY---EGTLLFISHDRYFLNRVANRIFEL 515
Cdd:cd03230 129 ESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAIL 168
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
326-517 |
1.96e-16 |
|
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: 78.29 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFGRKVY--PGYYAQE----P 398
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEalaltgpngsgKTTLLRILAGLLPPSAGEVlWNGEPIRdaREDYRRRlaylG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 DEALLAPNETLIDAIR---DID-SHLTDGDIRNILASFLFTGesvFKHS--GDLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:COG4133 82 HADGLKPELTVRENLRfwaALYgLRADREAIDEALEAVGLAG---LADLpvRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1222187810 473 TNHIDMSTREILEDAL---CGYEGTLLFISHDRYFLNrvANRIFELTP 517
Cdd:COG4133 159 FTALDAAGVALLAELIaahLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
326-512 |
3.81e-16 |
|
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: 78.36 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGR-KVYPGYYAQE-----P 398
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlIDGEdVRKEPREARRqigvlP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 DEALLAPNETLID------AIRDIDSHLTDGDIRNILASFLFTGESVFKhSGDLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:COG4555 81 DERGLYDRLTVREniryfaELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1222187810 473 TNHID-MSTREILED--ALCGYEGTLLFISHDRYFLNRVANRI 512
Cdd:COG4555 160 TNGLDvMARRLLREIlrALKKEGKTVLFSSHIMQEVEALCDRV 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
361-596 |
5.87e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.32 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 361 NGIGKTTLFQILMKQIKSDSGRIVF--GRKVypGYYAQEP--DE------------------------------------ 400
Cdd:PRK11819 42 NGAGKSTLLRIMAGVDKEFEGEARPapGIKV--GYLPQEPqlDPektvrenveegvaevkaaldrfneiyaayaepdadf 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 401 -ALLAPNETLIDAIR-----DIDSHLT-----------DGDIRNilasflftgesvfkhsgdLSGGEKARLNMARLMVSE 463
Cdd:PRK11819 120 dALAAEQGELQEIIDaadawDLDSQLEiamdalrcppwDAKVTK------------------LSGGERRRVALCRLLLEK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 464 SNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIFELT-PEGI--EetiGNYDDYARTKQNQSDR 540
Cdd:PRK11819 182 PDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDrGRGIpwE---GNYSSWLEQKAKRLAQ 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222187810 541 EAllaqnhapqinktrrKQERQQAKALESE--------RRRQKKALAqleeqmesndqRIAAYE 596
Cdd:PRK11819 259 EE---------------KQEAARQKALKRElewvrqspKARQAKSKA-----------RLARYE 296
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-217 |
8.80e-16 |
|
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: 77.39 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT--LDKKN--GLT-------LGLL 70
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlLDGRDlaSLSrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 71 SQEFKASEHETVgaiftaafQDLIEMeGQI--QSLQQRIDtaqaTEQQRLVHQ-LAELQ-EQYADRggfeyhsrirgvti 146
Cdd:COG1120 81 PQEPPAPFGLTV--------RELVAL-GRYphLGLFGRPS----AEDREAVEEaLERTGlEHLADR-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 147 glgfqlkdlekAFGTFSGGEKTR--IA-----------LgclllqspdllllDEPTNYLDF----ESLNWLESFLNNYKN 209
Cdd:COG1120 134 -----------PVDELSGGERQRvlIAralaqepplllL-------------DEPTSHLDLahqlEVLELLRRLARERGR 189
|
....*...
gi 1222187810 210 AFIIVSHD 217
Cdd:COG1120 190 TVVMVLHD 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-233 |
2.24e-15 |
|
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: 73.82 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTldkkngltlgllsqefkasehetvga 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 iftaafqdlIEMEGQiqslqqriDTAQATEQQRLVHqlaelqeqyadrggfeyhsrirgvtIGLGFQLkdlekafgtfSG 164
Cdd:cd00267 56 ---------ILIDGK--------DIAKLPLEELRRR-------------------------IGYVPQL----------SG 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 165 GEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLDRVCKRICEIEN 233
Cdd:cd00267 84 GQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
337-515 |
9.31e-15 |
|
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: 72.42 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 337 GDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGrkvypGYYAQEPDEALLAPNETLIDAirdi 416
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-----GVDLRDLDLESLRKNIAYVPQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 417 DSHLTDGDIR-NIlasflftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEG-- 493
Cdd:cd03228 84 DPFLFSGTIReNI-----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgk 146
|
170 180
....*....|....*....|..
gi 1222187810 494 TLLFISHdRYFLNRVANRIFEL 515
Cdd:cd03228 147 TVIVIAH-RLSTIRDADRIIVL 167
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-525 |
1.08e-14 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 73.97 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFGRKVYP-----GYYAQEPD 399
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEfvaivgpngagKSTLLKAILGLLPPTSGTVrLFGKPPRRarrriGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 400 eallapnetlIDA-----IRDI-----DSH------LTDGDIRNILASFLFTGESVFKHS--GDLSGGEKARLNMARLMV 461
Cdd:COG1121 86 ----------VDWdfpitVRDVvlmgrYGRrglfrrPSRADREAVDEALERVGLEDLADRpiGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 462 SESNFLLMDEPTNHIDMSTREILEDALCGY--EG-TLLFISHD-----RYFlNRVA--NR--IFE------LTPEGIEET 523
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDlgavrEYF-DRVLllNRglVAHgppeevLTPENLSRA 234
|
..
gi 1222187810 524 IG 525
Cdd:COG1121 235 YG 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
329-512 |
1.18e-14 |
|
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: 73.06 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQ-LFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYP--------GYYAQEPD 399
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksiGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 400 EALLApnETLIDAIR--DIDSHLTDGDIRNILASF-LFTGESvfKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHI 476
Cdd:cd03226 82 YQLFT--DSVREELLlgLKELDAGNEQAETVLKDLdLYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1222187810 477 DMSTREILEDA---LCGYEGTLLFISHDRYFLNRVANRI 512
Cdd:cd03226 158 DYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
329-512 |
1.43e-14 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 73.56 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFGRKVYP---------GYYaqeP 398
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEifgllgpngagKTTTIRMLLGLLRPTSGEVrVLGEDVARdpaevrrriGYV---P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 DEALLAPNETLID------AIRDIDSHLTDGDIRNILASFLFTGesvFKHS--GDLSGGEKARLNMARLMVSESNFLLMD 470
Cdd:COG1131 80 QEPALYPDLTVREnlrffaRLYGLPRKEARERIDELLELFGLTD---AADRkvGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1222187810 471 EPTNHIDMSTR----EILEDaLCGYEGTLLFISHDRYFLNRVANRI 512
Cdd:COG1131 157 EPTSGLDPEARrelwELLRE-LAAEGKTVLLSTHYLEEAERLCDRV 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
329-515 |
1.78e-14 |
|
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: 72.95 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVYP-----GYYAQEPDEAL 402
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKerkriGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 LAPnetlIDaIRDI-----DSH------LTDGDIRNILASFLFTGESVFKHS--GDLSGGEKARLNMARLMVSESNFLLM 469
Cdd:cd03235 82 DFP----IS-VRDVvlmglYGHkglfrrLSKADKAKVDEALERVGLSELADRqiGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1222187810 470 DEPTNHIDMSTREILEDA---LCGYEGTLLFISHDRYFLNRVANRIFEL 515
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
327-509 |
2.04e-14 |
|
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: 73.14 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLfKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRK--------------VYPG 392
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdisyVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 393 YYaqepdealLAPNETLIDAI------RDIDSHLTDGDIRNIlASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNF 466
Cdd:cd03299 80 YA--------LFPHMTVYKNIayglkkRKVDKKEIERKVLEI-AEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 467 LLMDEPTNHIDMST----REILEDALCGYEGTLLFISHD----RYFLNRVA 509
Cdd:cd03299 151 LLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
326-509 |
4.22e-14 |
|
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: 72.15 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLF----KNVGFEIHRGDRigiigrngigKTTLFQILMKQIKSDSGRIVF-GRKVYP--------- 391
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETlglvgesgsgKSTLARAILGLLKPTSGSIIFdGKDLLKlsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 392 ----GYYAQEPDEAlLAPNETLIDAIRDIDSHLTDGD---IRNILASFLFTG----ESVFK---HsgDLSGGEKARLNMA 457
Cdd:cd03257 81 rkeiQMVFQDPMSS-LNPRMTIGEQIAEPLRIHGKLSkkeARKEAVLLLLVGvglpEEVLNrypH--ELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 458 RLMVSESNFLLMDEPTNHIDMSTR-EILE--DALC-GYEGTLLFISHD----RYFLNRVA 509
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQaQILDllKKLQeELGLTLLFITHDlgvvAKIADRVA 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
327-512 |
6.26e-14 |
|
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: 70.29 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFgrkvypgyyaqepDEALLAPN 406
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-------------DGEDLTDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 407 ETLIDAIRDidshltdgDIRNILASF-LFTGESVFKHSG-DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREIL 484
Cdd:cd03229 68 EDELPPLRR--------RIGMVFQDFaLFPHLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....
gi 1222187810 485 EDAL------CGYegTLLFISHDRYFLNRVANRI 512
Cdd:cd03229 140 RALLkslqaqLGI--TVVLVTHDLDEAARLADRV 171
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-524 |
1.24e-13 |
|
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: 70.99 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFG----DRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVYPGYYA------ 395
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtFDGRPVTRRRRKafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 ----QEPdEALLAPNETLIDAIRDIDSHLTDGDIRNILASFLftgESV-------FKHSGDLSGGEKARLNMARLMVSES 464
Cdd:COG1124 82 qmvfQDP-YASLHPRHTVDRILAEPLRIHGLPDREERIAELL---EQVglppsflDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 465 NFLLMDEPTNHIDMSTR-EIL--------EDALcgyegTLLFISHDRYFLNRVANRIFELtPEG-IEETI 524
Cdd:COG1124 158 ELLLLDEPTSALDVSVQaEILnllkdlreERGL-----TYLFVSHDLAVVAHLCDRVAVM-QNGrIVEEL 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-233 |
1.46e-13 |
|
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: 70.44 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT-------LDKKNGLTL----GLL 70
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkdITKKNLRELrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 71 sqeFKASEH----ETVgaiftaaFQDLI-----------EMEgqiqslqQRIDTAqateqqrlvhqLAELQ-EQYADRgg 134
Cdd:COG1122 81 ---FQNPDDqlfaPTV-------EEDVAfgpenlglpreEIR-------ERVEEA-----------LELVGlEHLADR-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 135 feyhsRIrgvtiglgFQLkdlekafgtfSGGEKTRIA-------------LgclllqspdllllDEPTNYLDFESLNWLE 201
Cdd:COG1122 131 -----PP--------HEL----------SGGQKQRVAiagvlamepevlvL-------------DEPTAGLDPRGRRELL 174
|
250 260 270
....*....|....*....|....*....|....*
gi 1222187810 202 SFLNNYKNA---FIIVSHDRFFLDRVCKRICEIEN 233
Cdd:COG1122 175 ELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-233 |
3.84e-13 |
|
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: 67.81 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLtgechhdtgtldkkngltLGLLSQEfkasehetv 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII------------------LGLLKPD--------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 gaiftaafqdliemEGQIQSLQQRIDTAQATEQQRL--VHQLAELqeqYADRGGFEYhsrirgvtiglgfqLKdlekafg 160
Cdd:cd03230 54 --------------SGEIKVLGKDIKKEPEEVKRRIgyLPEEPSL---YENLTVREN--------------LK------- 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 161 tFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLDRVCKRICEIEN 233
Cdd:cd03230 96 -LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-190 |
7.48e-13 |
|
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: 66.52 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 18 FNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT--LDKKNgltlglLSQEFKASEHETVGAIFTAAF----- 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilLDGQD------LTDDERKSLRKEIGYVFQDPQlfprl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 91 --QDLIEMEGQIQSLQQRIDTAQATEQQRLVhqlaelqeqyadrggfeyhsrirgvtiGLGFQLKD-LEKAFGTFSGGEK 167
Cdd:pfam00005 75 tvRENLRLGLLLKGLSKREKDARAEEALEKL---------------------------GLGDLADRpVGERPGTLSGGQR 127
|
170 180
....*....|....*....|...
gi 1222187810 168 TRIALGCLLLQSPDLLLLDEPTN 190
Cdd:pfam00005 128 QRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
329-515 |
7.57e-13 |
|
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: 67.88 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGD--RQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVYP----------GYYA 395
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlVDGKDLTKlslkelrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 QEPDEALLAP-----------NETL--IDAIRDIDSHLTDGDIRNILASFLFTgesvfkhsgdLSGGEKARLNMARLMVS 462
Cdd:cd03225 82 QNPDDQFFGPtveeevafgleNLGLpeEEIEERVEEALELVGLEGLRDRSPFT----------LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 463 ESNFLLMDEPTNHID-MSTREILE--DALCGYEGTLLFISHDRYFLNRVANRIFEL 515
Cdd:cd03225 152 DPDILLLDEPTAGLDpAGRRELLEllKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
1.13e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 68.19 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLD------KKNGLTLGLLSQef 74
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 75 kaseHETVGAIFTAAFQDLIEME--GQIqSLQQRIDtaqATEQQRLVHQLAELQ-EQYADRggfeyhsrirgvtiglgfq 151
Cdd:COG1121 83 ----RAEVDWDFPITVRDVVLMGryGRR-GLFRRPS---RADREAVDEALERVGlEDLADR------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 152 lkdlekAFGTFSGGEKTR--IA-----------LgclllqspdllllDEPTNYLDFESLNWLESFLNNYKN---AFIIVS 215
Cdd:COG1121 136 ------PIGELSGGQQQRvlLAralaqdpdlllL-------------DEPFAGVDAATEEALYELLRELRRegkTILVVT 196
|
250
....*....|....
gi 1222187810 216 HD-----RFFlDRV 224
Cdd:COG1121 197 HDlgavrEYF-DRV 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
326-512 |
1.36e-12 |
|
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: 68.15 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRIVFG-------------RKVypG 392
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEvtallgpngsgKSTLLRALAGLLKPSSGEVLLDgrdlaslsrrelaRRI--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 393 YYAQEPDealLAPNETLIDAI-------RDIDSHLTDGDIRNILASFLFTGESVFKHS--GDLSGGEKARLNMARLMVSE 463
Cdd:COG1120 79 YVPQEPP---APFGLTVRELValgryphLGLFGRPSAEDREAVEEALERTGLEHLADRpvDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 464 SNFLLMDEPTNHIDMSTR-EILE--DALCGYEG-TLLFISHDryfLN---RVANRI 512
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQlEVLEllRRLARERGrTVVMVLHD---LNlaaRYADRL 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
1.40e-12 |
|
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: 67.80 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT----LDKKNGLT--------LG 68
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlFGERRGGEdvwelrkrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 69 LLSQEFKA--SEHETVG-AIFTAAFqdliemeGQIQsLQQRIDtaqaTEQQRLVHQLAELqeqyadrggfeyhsrirgvt 145
Cdd:COG1119 82 LVSPALQLrfPRDETVLdVVLSGFF-------DSIG-LYREPT----DEQRERARELLEL-------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 146 iglgFQLKDL-EKAFGTFSGGEKTR--IA-----------LgclllqspdllllDEPTNYLDFES----LNWLESFLNNY 207
Cdd:COG1119 130 ----LGLAHLaDRPFGTLSQGEQRRvlIAralvkdpelliL-------------DEPTAGLDLGArellLALLDKLAAEG 192
|
....*....
gi 1222187810 208 KNAFIIVSH 216
Cdd:COG1119 193 APTLVLVTH 201
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-233 |
1.91e-12 |
|
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: 66.51 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELSFSYG-VHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGechhdtgtldkkngltlglLSQEFKASehetvg 83
Cdd:cd03226 2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-------------------LIKESSGS------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 84 aiftaafqdlIEMEGQIQSLQQRIDTAqATEQQRLVHQL------AELQeqYADRGGFEYHSRIRGV--TIGLgFQLKDL 155
Cdd:cd03226 57 ----------ILLNGKPIKAKERRKSI-GYVMQDVDYQLftdsvrEELL--LGLKELDAGNEQAETVlkDLDL-YALKER 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 156 EKAfgTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWL-ESF--LNNYKNAFIIVSHDRFFLDRVCKRICEIE 232
Cdd:cd03226 123 HPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVgELIreLAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
.
gi 1222187810 233 N 233
Cdd:cd03226 201 N 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
327-500 |
3.18e-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: 66.09 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKV---------------Y 390
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYqkniealrrigalieA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 391 PGYYaqepdeallaPNETLIDAIRdIDSHLTDGDIRNILASFLFTGESVFKHS--GDLSGGEKARLNMARLMVSESNFLL 468
Cdd:cd03268 81 PGFY----------PNLTARENLR-LLARLLGIRKKRIDEVLDVVGLKDSAKKkvKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1222187810 469 MDEPTNHID----MSTREILEDaLCGYEGTLLFISH 500
Cdd:cd03268 150 LDEPTNGLDpdgiKELRELILS-LRDQGITVLISSH 184
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
326-477 |
3.66e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 66.53 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKV--YP---------GY 393
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIthLPmherarlgiGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 394 YAQEP--------DEALLAPNETLIDAIRDIDSHLTDgdirNILASFlftGESVFKHS--GDLSGGEKARLNMARLMVSE 463
Cdd:TIGR04406 81 LPQEAsifrkltvEENIMAVLEIRKDLDRAEREERLE----ALLEEF---QISHLRDNkaMSLSGGERRRVEIARALATN 153
|
170
....*....|....
gi 1222187810 464 SNFLLMDEPTNHID 477
Cdd:TIGR04406 154 PKFILLDEPFAGVD 167
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-237 |
4.22e-12 |
|
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: 66.37 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHS----IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdkknglTLG--LLSQEFK 75
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEV------TFDgrPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 76 ASEHETVGAIF---TAAF------QDLIEMEGQIQSLQQRidtaqateQQRLVHQLAE--LQEQYADRggfeY-Hsrirg 143
Cdd:COG1124 75 KAFRRRVQMVFqdpYASLhprhtvDRILAEPLRIHGLPDR--------EERIAELLEQvgLPPSFLDR----YpH----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 144 vtiglgfQLkdlekafgtfSGGEKTRIALG-----------ClllqspdllllDEPTNYLD----FESLNWLESFLNNYK 208
Cdd:COG1124 138 -------QL----------SGGQRQRVAIAralilepelllL-----------DEPTSALDvsvqAEILNLLKDLREERG 189
|
250 260
....*....|....*....|....*....
gi 1222187810 209 NAFIIVSHDRFFLDRVCKRICEIENTHMV 237
Cdd:COG1124 190 LTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
287-515 |
4.46e-12 |
|
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: 69.02 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 287 SRRAASREkAIERITPIERRQDRRSlhFSFSPKVLSGNDVLMVEGLekSFG----DRQLFKNVGFEIHRGDrigiigrng 362
Cdd:COG4987 297 QHLGRVRA-AARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDV--SFRypgaGRPVLDGLSLTLPPGErvaivgpsg 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 363 igKTTLFQILMKQIKSDSGRIVFGrkvypGYYAQEPDEALLAPNETLIDAirdiDSHLTDGDIR-NI------------- 428
Cdd:COG4987 372 sgKSTLLALLLRFLDPQSGSITLG-----GVDLRDLDEDDLRRRIAVVPQ----RPHLFDTTLReNLrlarpdatdeelw 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 429 -------LASFLFT---------GEsvfkHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALCGY 491
Cdd:COG4987 443 aalervgLGDWLAAlpdgldtwlGE----GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEAL 518
|
250 260
....*....|....*....|....*
gi 1222187810 492 EG-TLLFISHDRYFLNRvANRIFEL 515
Cdd:COG4987 519 AGrTVLLITHRLAGLER-MDRILVL 542
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
447-517 |
6.26e-12 |
|
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: 65.53 E-value: 6.26e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 447 SGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR----EILEDALCgyEGT-LLFISHDRYFLNRVANRIFELTP 517
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKA--RGTaIIGIFHDEEVREAVADRVVDVTP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-228 |
7.85e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 65.47 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLT-----------LGLLS 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV-RVLGEDvardpaevrrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 72 QEFKASEHETVgaiftaafQDLIEMEGQIQSLQQRidtaqatEQQRLVHQLAELqeqyadrggfeyhsrirgvtiglgFQ 151
Cdd:COG1131 80 QEPALYPDLTV--------RENLRFFARLYGLPRK-------EARERIDELLEL------------------------FG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 152 LKD-LEKAFGTFSGGEKTRIALGClllqspdllllDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLDRVCKR 227
Cdd:COG1131 121 LTDaADRKVGTLSGGMKQRLGLALallhdpellilDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDR 200
|
.
gi 1222187810 228 I 228
Cdd:COG1131 201 V 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
296-537 |
7.92e-12 |
|
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: 68.32 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 296 AIERI-----TPIERRQDRRSLHfsfsPKVLSGNdvLMVEGLekSFG----DRQLFKNVGFEIHRGDRigiigrngigKT 366
Cdd:COG2274 444 ALERLddildLPPEREEGRSKLS----LPRLKGD--IELENV--SFRypgdSPPVLDNISLTIKPGERvaivgrsgsgKS 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 367 TLFQILMKQIKSDSGRIVFG-------------RKVypGYYAQEPDeaLLapNETLIDAIRDIDSHLTDGDIRNI----- 428
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDgidlrqidpaslrRQI--GVVLQDVF--LF--SGTIRENITLGDPDATDEEIIEAarlag 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 429 LASF-------LFT--GEsvfkHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEG--TLLF 497
Cdd:COG2274 590 LHDFiealpmgYDTvvGE----GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVII 665
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1222187810 498 ISHDRYFLnRVANRIFELTPEGIEEtIGNYDD-------YARTKQNQ 537
Cdd:COG2274 666 IAHRLSTI-RLADRIIVLDKGRIVE-DGTHEEllarkglYAELVQQQ 710
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
327-483 |
9.02e-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: 65.26 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKV--YP---------GYY 394
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdGQDItkLPmhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 395 AQEP--------DEALLAPNETLidairdidsHLTDGDIRNILASFL--FTGESVFKHSGD-LSGGEKARLNMARLMVSE 463
Cdd:cd03218 81 PQEAsifrkltvEENILAVLEIR---------GLSKKEREEKLEELLeeFHITHLRKSKASsLSGGERRRVEIARALATN 151
|
170 180
....*....|....*....|.
gi 1222187810 464 SNFLLMDEPTNHID-MSTREI 483
Cdd:cd03218 152 PKFLLLDEPFAGVDpIAVQDI 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
326-472 |
1.25e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHR------------GdrigiigrngigKTTLFQILMKQIKSDSGRIVF-GRKV--Y 390
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQgeivgllgpngaG------------KTTTFYMIVGLVKPDSGRIFLdGEDIthL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 391 P---------GYYAQEP--------DEALLAPNETLidairdidsHLTDGDIRNILASFL--FTGESVFKHSGD-LSGGE 450
Cdd:COG1137 71 PmhkrarlgiGYLPQEAsifrkltvEDNILAVLELR---------KLSKKEREERLEELLeeFGITHLRKSKAYsLSGGE 141
|
170 180
....*....|....*....|..
gi 1222187810 451 KARLNMARLMVSESNFLLMDEP 472
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEP 163
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-63 |
1.27e-11 |
|
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: 63.61 E-value: 1.27e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTG--TLDKKN 63
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeiLLDGKD 62
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-511 |
1.44e-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: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG--ECHHDTGTLDKKNGLT---LGLLSQEFKAS 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCekcGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 78 EHETVGAIFTAAFQDLIEMEGQI-QSLQQRI-----DTAQATEQQRLVHQLAELQEQYadrgGFEYHSRI-RGV----TI 146
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWNLSDKLrRRIRKRIaimlqRTFALYGDDTVLDNVLEALEEI----GYEGKEAVgRAVdlieMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 147 GLGFQLKDLEKafgTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNW----LESFLNNYKNAFIIVSHdrffld 222
Cdd:TIGR03269 157 QLSHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSH------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 223 rvckriceienthmvsytgnYTQYLDKKAKRDRALDaayNKQMKELTRQQKIVdrlrdynsvqssrraasrEKAIERITP 302
Cdd:TIGR03269 228 --------------------WPEVIEDLSDKAIWLE---NGEIKEEGTPDEVV------------------AVFMEGVSE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 303 IERRQDrrslhfsfspkVLSGNDVLMVEGLEKSFG--DRQLFK---NVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIK 377
Cdd:TIGR03269 267 VEKECE-----------VEVGEPIIKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 378 SDSGRIVF-----------------GR-KVYPGYYAQEPDealLAPNETLIDAIRD-IDSHLTD--GDIRNI--LASFLF 434
Cdd:TIGR03269 336 PTSGEVNVrvgdewvdmtkpgpdgrGRaKRYIGILHQEYD---LYPHRTVLDNLTEaIGLELPDelARMKAVitLKMVGF 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 435 T---GESVF-KHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG----YEGTLLFISHDRYFLN 506
Cdd:TIGR03269 413 DeekAEEILdKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKareeMEQTFIIVSHDMDFVL 492
|
....*
gi 1222187810 507 RVANR 511
Cdd:TIGR03269 493 DVCDR 497
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
364-474 |
2.31e-11 |
|
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: 62.28 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 364 GKTTLFQILMKQIKSDSGRIVF-------------GRKVypGYYAQEPdeaLLAPNETLIDAIR------DIDSHLTDGD 424
Cdd:pfam00005 23 GKSTLLKLIAGLLSPTEGTILLdgqdltdderkslRKEI--GYVFQDP---QLFPRLTVRENLRlglllkGLSKREKDAR 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 425 IRNILASF---LFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTN 474
Cdd:pfam00005 98 AEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-216 |
2.55e-11 |
|
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: 63.39 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTldkkngltlgllsQEFKASEhetv 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE-------------ITFDGKS---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 gaiftaaFQDLIEMEGQIQSLqqridtaqateqqrlvhqlAELQEQYADRGGFE---YHSRIRGV----------TIGLG 149
Cdd:cd03268 64 -------YQKNIEALRRIGAL-------------------IEAPGFYPNLTAREnlrLLARLLGIrkkridevldVVGLK 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 150 FQLKdleKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSH 216
Cdd:cd03268 118 DSAK---KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSH 184
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
365-529 |
4.29e-11 |
|
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: 65.93 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 365 KTTLFQILMKQIKSDSGRIVFG-------------RKVypGYYAQEPdeALLApnETLIDAIRDIDSHLTDGDIRNIL-- 429
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINgvdlsdldpaswrRQI--AWVPQNP--YLFA--GTIRENLRLGRPDASDEELEAALea 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 430 ---ASFLFT---------GEsvfkHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY-EG-TL 495
Cdd:COG4988 450 aglDEFVAAlpdgldtplGE----GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTV 525
|
170 180 190
....*....|....*....|....*....|....
gi 1222187810 496 LFISHDRYFLNRvANRIFELTPEGIEETiGNYDD 529
Cdd:COG4988 526 ILITHRLALLAQ-ADRILVLDDGRIVEQ-GTHEE 557
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
329-509 |
4.40e-11 |
|
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: 62.07 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVypgyyaQEPDEALLAPN- 406
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlLDGKDL------ASLSPKELARKi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 407 ---ETLIDAIrDIDsHLTDgdiRNIlasflftgesvfkhsGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-E 482
Cdd:cd03214 76 ayvPQALELL-GLA-HLAD---RPF---------------NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQiE 135
|
170 180 190
....*....|....*....|....*....|
gi 1222187810 483 ILE--DALCGYEG-TLLFISHDryfLNRVA 509
Cdd:cd03214 136 LLEllRRLARERGkTVVMVLHD---LNLAA 162
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
365-525 |
1.06e-10 |
|
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: 61.93 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 365 KTTLFQILMKQIKSDSGRIVFG-----------------RKVypGYYAQEpdeALLAPNETLIDAI-----RDIDSHLTD 422
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppqqRKI--GLVFQQ---YALFPHLNVRENLafglkRKRNREDRI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 423 gDIRNILASFLFTgESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREI----LEDALCGYEGTLLFI 498
Cdd:cd03297 111 -SVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQllpeLKQIKKNLNIPVIFV 188
|
170 180
....*....|....*....|....*..
gi 1222187810 499 SHDRYFLNRVANRIFELTpEGIEETIG 525
Cdd:cd03297 189 THDLSEAEYLADRIVVME-DGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
327-501 |
1.49e-10 |
|
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: 61.12 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDEAL---- 402
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 --LAPNETLIDAI-----------RDIDSHLTDgdirniLASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLM 469
Cdd:cd03301 81 yaLYPHMTVYDNIafglklrkvpkDEIDERVRE------VAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1222187810 470 DEPTNHIDMSTR-----EI--LEDALcgyEGTLLFISHD 501
Cdd:cd03301 155 DEPLSNLDAKLRvqmraELkrLQQRL---GTTTIYVTHD 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-224 |
2.41e-10 |
|
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: 60.57 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGechhdtgtldkkngltlgLLSQEfkasehe 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG------------------LLPPS------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 81 tvgaiftaafqdliemEGQIQSLQQRIDTAQATEQQRLV---HQLAelqeQYADRGGFEY---HSRIRGVTIGLG----- 149
Cdd:COG4133 56 ----------------AGEVLWNGEPIRDAREDYRRRLAylgHADG----LKPELTVRENlrfWAALYGLRADREaidea 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 150 ---FQLKDLE-KAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLD 222
Cdd:COG4133 116 leaVGLAGLAdLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELA 195
|
..
gi 1222187810 223 RV 224
Cdd:COG4133 196 AA 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
326-578 |
3.42e-10 |
|
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: 62.61 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSF--GDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSD---SGRIVF-------------GR 387
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLdgrdllelsealrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 388 KVypGYYAQEPD-------------EALLAPNETLIDAIRDIDSHLTDGDIRNILASFLFTgesvfkhsgdLSGGEKARL 454
Cdd:COG1123 84 RI--GMVFQDPMtqlnpvtvgdqiaEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQ----------LSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 455 NMARLMVSESNFLLMDEPTNHIDMST-REILE--DALCGYEG-TLLFISHDRYFLNRVANRIFELTPEGIEETignyddy 530
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTqAEILDllRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVED------- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 531 ARTKQNQSDREALLAQNHAPQINKTRRKQERQQAKALE---------SERRRQKKAL 578
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEvrnlskrypVRGKGGVRAV 281
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-233 |
3.46e-10 |
|
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: 60.20 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYG----VHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLTLGLLSQEFKASE 78
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-RVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 79 -HETVGAIFtaafqdliemegqiqslQQR--IDTAQATEQqrlvhqlAELQEQYADRGGFEYHSRIRGVTIGLGfqLKDL 155
Cdd:cd03255 80 rRRHIGFVF-----------------QSFnlLPDLTALEN-------VELPLLLAGVPKKERRERAEELLERVG--LGDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 156 EKAF-GTFSGGEKTRIA------------LGclllqspdllllDEPTNYLDFES----LNWLESFLNNYKNAFIIVSHDR 218
Cdd:cd03255 134 LNHYpSELSGGQQQRVAiaralandpkiiLA------------DEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
250
....*....|....*
gi 1222187810 219 FFLDRvCKRICEIEN 233
Cdd:cd03255 202 ELAEY-ADRIIELRD 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
338-500 |
3.65e-10 |
|
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: 59.25 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 338 DRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKvypgyyaqepdeallaPNETLIDAIRDID 417
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV----------------PVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 418 S------HLTDGDIRNILasflftGESvfkhsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALCG 490
Cdd:cd03247 78 SvlnqrpYLFDTTLRNNL------GRR-------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEV 144
|
170
....*....|.
gi 1222187810 491 YEG-TLLFISH 500
Cdd:cd03247 145 LKDkTLIWITH 155
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
365-515 |
4.35e-10 |
|
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: 60.04 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 365 KTTLFQILMKQIKSDSGRI-VFGRKVYP----------GYYAQEPDEALLAPneTLIDairDI-----DSHLTDGDIRNI 428
Cdd:COG1122 40 KSTLLRLLNGLLKPTSGEVlVDGKDITKknlrelrrkvGLVFQNPDDQLFAP--TVEE---DVafgpeNLGLPREEIRER 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 429 LASFL-------FTGESVFkhsgDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY--EG-TLLFI 498
Cdd:COG1122 115 VEEALelvglehLADRPPH----ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIV 190
|
170
....*....|....*..
gi 1222187810 499 SHDRYFLNRVANRIFEL 515
Cdd:COG1122 191 THDLDLVAELADRVIVL 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
329-512 |
5.02e-10 |
|
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: 60.08 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGR-IVFG-------RKVYP--GYYAQEP 398
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGhdvvrepREVRRriGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 --DEALLAPNETLIDA-IRDIDSHLTDGDIRNILAsFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNH 475
Cdd:cd03265 83 svDDELTGWENLYIHArLYGVPGAERRERIDELLD-FVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1222187810 476 IDMSTR----EILEDALCGYEGTLLFISHDRYFLNRVANRI 512
Cdd:cd03265 162 LDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
329-512 |
5.18e-10 |
|
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: 60.21 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVYPgyyaqepdealLAPNE 407
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDISG-----------LSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 408 tLIDAIRDI----------DS-------------H--LTDGDIRNILASFL-FTG--ESVFKHSGDLSGGEKARLNMARL 459
Cdd:cd03261 72 -LYRLRRRMgmlfqsgalfDSltvfenvafplreHtrLSEEEIREIVLEKLeAVGlrGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 460 MVSESNFLLMDEPTNHID-MSTREI------LEDALCgyeGTLLFISHDRYFLNRVANRI 512
Cdd:cd03261 151 LALDPELLLYDEPTAGLDpIASGVIddlirsLKKELG---LTSIMVTHDLDTAFAIADRI 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
329-501 |
5.51e-10 |
|
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: 59.79 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQL----FKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFGRKVYP-----GYYAQEP 398
Cdd:cd03293 3 VRNVSKTYGGGGGavtaLEDISLSVEEGEfvalvgpsgcgKSTLLRIIAGLERPTSGEVlVDGEPVTGpgpdrGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 deALLaPNETLID--AIRDIDSHLTDGDIRNILASFL-FTGESVFKHS--GDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:cd03293 83 --ALL-PWLTVLDnvALGLELQGVPKAEARERAEELLeLVGLSGFENAypHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 1222187810 474 NHIDMSTREILEDAL----CGYEGTLLFISHD 501
Cdd:cd03293 160 SALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-228 |
6.80e-10 |
|
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: 58.74 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGechhdtgtLDKKngltlgllsqefkaseheTV 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG--------LEEP------------------DS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 GAIFTAAfQDLIEMEGQIQSLQQRIdtaqateqqRLVHQLAELqeqyadrggFEYHSRIRGVTIGLgfqlkdlekafgtf 162
Cdd:cd03229 55 GSILIDG-EDLTDLEDELPPLRRRI---------GMVFQDFAL---------FPHLTVLENIALGL-------------- 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 163 SGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLN----NYKNAFIIVSHDRFFLDRVCKRI 228
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRV 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-59 |
6.85e-10 |
|
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: 59.47 E-value: 6.85e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI 56
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
329-512 |
6.99e-10 |
|
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: 58.21 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKVYPGyyaqEPDEALLAPNE 407
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFA----SPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 408 TlidairdidshltdgdirnilasflftgesVFKhsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILED- 486
Cdd:cd03216 79 M------------------------------VYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKv 124
|
170 180
....*....|....*....|....*...
gi 1222187810 487 --ALCGYEGTLLFISHDRYFLNRVANRI 512
Cdd:cd03216 125 irRLRAQGVAVIFISHRLDEVFEIADRV 152
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-237 |
7.56e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFK----LLT---GECHHDTGTL----DKKNGLTLGL 69
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKcfarLLTpqsGTVFLGDKPIsmlsSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 70 LSQEFKASEHETVgaiftaafQDLIE--------MEGQI-QSLQQRIDtaQATEQQRLVHqlaelqeqYADRggfeyhsr 140
Cdd:PRK11231 81 LPQHHLTPEGITV--------RELVAygrspwlsLWGRLsAEDNARVN--QAMEQTRINH--------LADR-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 141 irgvtiglgfQLKDLekafgtfSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDF----ESLNWLESfLNNYKNAFIIVSH 216
Cdd:PRK11231 135 ----------RLTDL-------SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMRLMRE-LNTQGKTVVTVLH 196
|
250 260
....*....|....*....|.
gi 1222187810 217 DrffLDRVCkRICEientHMV 237
Cdd:PRK11231 197 D---LNQAS-RYCD----HLV 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
326-517 |
7.73e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 60.10 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSF----GDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFGRKVYP-----GYYA 395
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEfvalvgpsgcgKSTLLRLIAGLEKPTSGEVlVDGKPVTGpgpdrGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 QEPdeALLaPNETLID------AIRDIDSHLTDGDIRNILASFLFTGesvFKHS--GDLSGGEKARLNMARLMVSESNFL 467
Cdd:COG1116 87 QEP--ALL-PWLTVLDnvalglELRGVPKAERRERARELLELVGLAG---FEDAypHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 468 LMDEPTNHIDMSTREILED---ALCGYEG-TLLFISHDRY---FLnrvANRIFELTP 517
Cdd:COG1116 161 LMDEPFGALDALTRERLQDellRLWQETGkTVLFVTHDVDeavFL---ADRVVVLSA 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-512 |
1.18e-09 |
|
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: 58.76 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 343 KNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG----RKVYP-------GYYAQEPdeallapneTLID 411
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdiRQLDPadlrrniGYVPQDV---------TLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 412 A-IRD-IDSHLTDGDIRNILASFLFTGESVF--KH----------SGD-LSGGEKARLNMARLMVSESNFLLMDEPTNHI 476
Cdd:cd03245 92 GtLRDnITLGAPLADDERILRAAELAGVTDFvnKHpngldlqigeRGRgLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1222187810 477 DMSTREILEDALCGYEG--TLLFISHdRYFLNRVANRI 512
Cdd:cd03245 172 DMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRI 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
327-515 |
1.27e-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: 58.45 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKVYP------GYYaqePD 399
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIaarnriGYL---PE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 400 EALLAPNETLID---------------AIRDIDSHLTDGDIRNILASFLFTgesvfkhsgdLSGGEKARLNMARLMVSES 464
Cdd:cd03269 78 ERGLYPKMKVIDqlvylaqlkglkkeeARRRIDEWLERLELSEYANKRVEE----------LSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1222187810 465 NFLLMDEPTNHIDMSTREILEDALCGYEG---TLLFISHDRYFLNRVANRIFEL 515
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-247 |
1.80e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL-------TGECH---HD---TGTLDKKNGLTL 67
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNiagHQfdfSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 68 ----GLLSQEFKASEHETVgaiftaaFQDLIEMEGQIQSLQQRIDTAQAteqQRLVHQLaELQEqYADRggFEYHsrirg 143
Cdd:COG4161 81 rqkvGMVFQQYNLWPHLTV-------MENLIEAPCKVLGLSKEQAREKA---MKLLARL-RLTD-KADR--FPLH----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 144 vtiglgfqlkdlekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFI---IVSHDRFF 220
Cdd:COG4161 142 ------------------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEF 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 1222187810 221 LDRVCKRICEIENTHMVSY----------TGNYTQYL 247
Cdd:COG4161 204 ARKVASQVVYMEKGRIIEQgdashftqpqTEAFAHYL 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
446-519 |
1.88e-09 |
|
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: 57.16 E-value: 1.88e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST----REILEDALCgyegTLLFISHdRYFLNRVANRIFELTPEG 519
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESedrlYQLLKELGI----TVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
327-512 |
2.55e-09 |
|
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: 58.22 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRIVF------------------GRK 388
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEihgligpngagKTTLFNLISGFLRPTSGSVLFdgeditglppheiarlgiGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 389 -----VYP----------GYYAQEPDEALLAPNETLIDAIRDIDSHLTD----GDIRNILAsflftgesvfkhsGDLSGG 449
Cdd:cd03219 81 fqiprLFPeltvlenvmvAAQARTGSGLLLARARREEREARERAEELLErvglADLADRPA-------------GELSYG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 450 EKARLNMARLMVSESNFLLMDEPTNhiDMSTREIleDALCGY------EG-TLLFISHDRYFLNRVANRI 512
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAA--GLNPEET--EELAELirelreRGiTVLLVEHDMDVVMSLADRV 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
329-515 |
2.99e-09 |
|
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: 57.50 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGD----RQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVYpgyyaqEPDEALL 403
Cdd:cd03255 3 LKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDIS------KLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 404 AP--NET---------LIdairdidSHLTDGDirNILASFLFTG----------ESVFKHSG----------DLSGGEKA 452
Cdd:cd03255 77 AAfrRRHigfvfqsfnLL-------PDLTALE--NVELPLLLAGvpkkerreraEELLERVGlgdrlnhypsELSGGQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 453 RLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG----YEGTLLFISHDRYFLNRvANRIFEL 515
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnkeAGTTIVVVTHDPELAEY-ADRIIEL 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-235 |
3.53e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIF-----NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTG-TLDKKNGLTLGLLS-QEFK 75
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 76 ASEHEtVGAIFT----AAFQDLIEMEGQIQSLQQRIDTAQATEQQRLVHQLAELQEQYADRGGFEyhsrirgvtiglgfq 151
Cdd:PRK13645 87 RLRKE-IGLVFQfpeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFE--------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 152 lkdlekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFES----LNWLESFLNNYKNAFIIVSHDrffLDRVCKR 227
Cdd:PRK13645 151 ----------LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHN---MDQVLRI 217
|
....*...
gi 1222187810 228 ICEIENTH 235
Cdd:PRK13645 218 ADEVIVMH 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-60 |
3.96e-09 |
|
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: 57.16 E-value: 3.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLD 60
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
327-502 |
4.87e-09 |
|
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: 59.22 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDR-QLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKVYP----------GYY 394
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLADadadswrdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 395 AQEP--------DEALL----APNETLIDAIRDIDSHLTDGDIRNILASFLftGEsvfkHSGDLSGGEKARLNMARLMVS 462
Cdd:TIGR02857 402 PQHPflfagtiaENIRLarpdASDAEIREALERAGLDEFVAALPQGLDTPI--GE----GGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1222187810 463 ESNFLLMDEPTNHIDMSTREILEDAL-CGYEG-TLLFISHDR 502
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALrALAQGrTVLLVTHRL 517
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-50 |
5.33e-09 |
|
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: 55.85 E-value: 5.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYG--VHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR 50
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-87 |
8.22e-09 |
|
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: 55.40 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHS--IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTG--TLDKKNGLTL--------GLL 70
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGeiTLDGVPVSDLekalssliSVL 80
|
90 100
....*....|....*....|
gi 1222187810 71 SQE---FKASEHETVGAIFT 87
Cdd:cd03247 81 NQRpylFDTTLRNNLGRRFS 100
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-247 |
9.79e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL-------TGEC-----HHD-TGTLDKKNGLTL 67
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLniagnHFDfSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 68 ----GLLSQEFKASEHETVgaiftaaFQDLIEMEGQIQSLQQRIDTAQATEQ-QRLvhQLAElqeqYADRggFEYHsrir 142
Cdd:PRK11124 81 rrnvGMVFQQYNLWPHLTV-------QQNLIEAPCRVLGLSKDQALARAEKLlERL--RLKP----YADR--FPLH---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 143 gvtiglgfqlkdlekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAFI---IVSHDRF 219
Cdd:PRK11124 142 -------------------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVE 202
|
250 260 270
....*....|....*....|....*....|....*...
gi 1222187810 220 FLDRVCKRICEIENTHMVSY----------TGNYTQYL 247
Cdd:PRK11124 203 VARKTASRVVYMENGHIVEQgdascftqpqTEAFKNYL 240
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-224 |
1.05e-08 |
|
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: 55.97 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSY----GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT--LDKKNGLTlglLSQEFK 75
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiiFDGKDLLK---LSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 76 ASEHETVGAIftaaFQDliemegQIQSLQQRIdtaqateqqRLVHQLAE-LQEQYADRGgfeyhSRIRGVTIGLGFQLKD 154
Cdd:cd03257 78 KIRRKEIQMV----FQD------PMSSLNPRM---------TIGEQIAEpLRIHGKLSK-----KEARKEAVLLLLVGVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 155 LEKAFGT-----FSGGEKTRIALG-----------ClllqspdllllDEPTNYLD----FESLNWLESFLNNYKNAFIIV 214
Cdd:cd03257 134 LPEEVLNrypheLSGGQRQRVAIAralalnpklliA-----------DEPTSALDvsvqAQILDLLKKLQEELGLTLLFI 202
|
250
....*....|....
gi 1222187810 215 SHD----RFFLDRV 224
Cdd:cd03257 203 THDlgvvAKIADRV 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-233 |
1.29e-08 |
|
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: 55.49 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 19 NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLD---------KKNGL-----TLGLLSQEFKASEHETVGA 84
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlRGRAIpylrrKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 ifTAAFQDLIEMEGQiQSLQQRIdtAQATEQQRLVHQLAELQEQyadrggfeyhsrirgvtiglgfqlkdlekafgtFSG 164
Cdd:cd03292 98 --NVAFALEVTGVPP-REIRKRV--PAALELVGLSHKHRALPAE---------------------------------LSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222187810 165 GEKTRIALGCLLLQSPDLLLLDEPTNYLD----FESLNWLESFlnNYKNAFIIVS-HDRFFLDRVCKRICEIEN 233
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDpdttWEIMNLLKKI--NKAGTTVVVAtHAKELVDTTRHRVIALER 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-237 |
1.36e-08 |
|
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: 56.35 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIF---------NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLtgechhdtgtldkkngltLGLlsq 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgakqrapvlTNVSLSIEEGETVGLLGRSGCGKSTLARLL------------------LGL--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 73 efkasEHETVGAIFTAAfQDLIEMEG-QIQSLQQRI-----DTAQATEQQRLVHQ-LAELQEQYADRGGFEYHSRIRGVT 145
Cdd:TIGR02769 61 -----EKPAQGTVSFRG-QDLYQLDRkQRRAFRRDVqlvfqDSPSAVNPRMTVRQiIGEPLRHLTSLDESEQKARIAELL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 146 IGLGFQLKDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDF----ESLNWLESFLNNYKNAFIIVSHDRFFL 221
Cdd:TIGR02769 135 DMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLV 214
|
250
....*....|....*.
gi 1222187810 222 DRVCKRICEIENTHMV 237
Cdd:TIGR02769 215 QSFCQRVAVMDKGQIV 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
327-512 |
2.15e-08 |
|
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: 54.83 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDEAL---- 402
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMvfqd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 --LAPNETLIDAI----RDidSHLTDGDIR-NILASFLFTGESVFKHS--GDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:cd03259 81 yaLFPHLTVAENIafglKL--RGVPKAEIRaRVRELLELVGLEGLLNRypHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1222187810 474 NHIDMSTREILEDAL------CGYegTLLFISHDRYFLNRVANRI 512
Cdd:cd03259 159 SALDAKLREELREELkelqreLGI--TTIYVTHDQEEALALADRI 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-193 |
2.44e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.39 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL----DKKNGLTLGLLSQEFKA 76
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 77 SEHETVGAiFTAAFQDLIEMeGQIQSLqQRIDTAQATEqQRLVHQLAELQE--QYADRggfeyhsrirgvtiglgfqlkd 154
Cdd:PRK09536 82 VPQDTSLS-FEFDVRQVVEM-GRTPHR-SRFDTWTETD-RAAVERAMERTGvaQFADR---------------------- 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1222187810 155 lekAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD 193
Cdd:PRK09536 136 ---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
327-500 |
2.59e-08 |
|
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: 54.29 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPgYYAQEPDEAL---- 402
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-EQRDEPHENIlylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 --------LAPNETLidairDIDSHLTDGDIRNILASFLFTGESVFKH--SGDLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:TIGR01189 80 hlpglkpeLSALENL-----HFWAAIHGGAQRTIEDALAAVGLTGFEDlpAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 1222187810 473 TNHIDMSTREILE---DALCGYEGTLLFISH 500
Cdd:TIGR01189 155 TTALDKAGVALLAgllRAHLARGGIVLLTTH 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
365-501 |
3.15e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.16 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 365 KTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQ--EPDEALLApneTLIDAI-------RDIDSHLTDGDiRNILASFL-- 433
Cdd:NF040873 31 KSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPL---TVRDLVamgrwarRGLWRRLTRDD-RAAVDDALer 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 434 -----FTGESVfkhsGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDAL---CGYEGTLLFISHD 501
Cdd:NF040873 107 vgladLAGRQL----GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLaeeHARGATVVVVTHD 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-50 |
3.24e-08 |
|
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: 56.77 E-value: 3.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHS--IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-172 |
3.27e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.16 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTG--TLDKKN---------GLTLGL 69
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGevRLNGRPladwspaelARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 70 LSQefkaseHETVGAIFTAafQDLIEMeGQIQSLQQRIDTAQATEQqrlVHQLAELQEqYADRggfEYHsrirgvtiglg 149
Cdd:PRK13548 81 LPQ------HSSLSFPFTV--EEVVAM-GRAPHGLSRAEDDALVAA---ALAQVDLAH-LAGR---DYP----------- 133
|
170 180
....*....|....*....|...
gi 1222187810 150 fqlkdlekafgTFSGGEKTRIAL 172
Cdd:PRK13548 134 -----------QLSGGEQQRVQL 145
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
326-488 |
3.47e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.58 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQE-------P 398
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqrvgvvP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 399 DEALLAPNETLIDAIRDIDSH--LTDGDIRNILASFLFTGESVFKHS---GDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYfgLSAAAARALVPPLLEFAKLENKADakvGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170
....*....|....*
gi 1222187810 474 NHIDMSTREILEDAL 488
Cdd:PRK13537 167 TGLDPQARHLMWERL 181
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-237 |
4.00e-08 |
|
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: 56.31 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSY--GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdkknglTLGllSQEFKASEHE 80
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI------TLG--GVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 81 TVGAIFTAAFQD--LIEMegqiqSLQQ--RIDTAQATEQQ-----RLVhQLAELQEQYADRggfeYHSRI--RGVTiglg 149
Cdd:COG4987 406 DLRRRIAVVPQRphLFDT-----TLREnlRLARPDATDEElwaalERV-GLGDWLAALPDG----LDTWLgeGGRR---- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 150 fqlkdlekafgtFSGGEKTRIA-------------LgclllqspdllllDEPTNYLDFES-LNWLESFLNNYKN-AFIIV 214
Cdd:COG4987 472 ------------LSGGERRRLAlarallrdapillL-------------DEPTEGLDAATeQALLADLLEALAGrTVLLI 526
|
250 260
....*....|....*....|...
gi 1222187810 215 SHDRFFLDRVCkRICEIENTHMV 237
Cdd:COG4987 527 THRLAGLERMD-RILVLEDGRIV 548
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
365-501 |
4.86e-08 |
|
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: 55.83 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 365 KTTLFQILMKQIKSDSGRIVFGrkvypGYYAQEPDEALLAPNETLIDAirdiDSHLTDGDIRN--ILASFLFTGESVFK- 441
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLD-----GVPVSSLDQDEVRRRVSVCAQ----DAHLFDTTVREnlRLARPDATDEELWAa 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 442 -----------------------HSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALCGYEG-TLL 496
Cdd:TIGR02868 445 lervgladwlralpdgldtvlgeGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAALSGrTVV 524
|
....*
gi 1222187810 497 FISHD 501
Cdd:TIGR02868 525 LITHH 529
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
572-636 |
6.77e-08 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 49.77 E-value: 6.77e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 572 RRQKKALAQLEEQMESNDQRIAAYEADMCQPSFYDDMVYAQKITDDYHALKADNENIIQQWEDLA 636
Cdd:pfam16326 4 YKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDYEKLQELSAELEELEAELEELYERWEELE 68
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-232 |
7.99e-08 |
|
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: 53.07 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 20 NLDFRIDdAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL--------DKKNGLTL-------GLLSQEFKASEHETV-- 82
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfDSRKKINLppqqrkiGLVFQQYALFPHLNVre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 ----GAIFTAAFQDLIEMEGQIQSLQqridtaqateqqrlvhqLAELQEQYADrggfeyhsrirgvtiglgfqlkdleka 158
Cdd:cd03297 95 nlafGLKRKRNREDRISVDELLDLLG-----------------LDHLLNRYPA--------------------------- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 159 fgTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNAF----IIVSHDRFFLDRVCKRICEIE 232
Cdd:cd03297 131 --QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVME 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
365-534 |
1.05e-07 |
|
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: 54.35 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 365 KTTLFQILMKQIKSDSGRIVFG-----------------RKVypGYYAQEpdeALLAPN----ETLIDAIRDidshlTDG 423
Cdd:TIGR02142 36 KTTLIRLIAGLTRPDEGEIVLNgrtlfdsrkgiflppekRRI--GYVFQE---ARLFPHlsvrGNLRYGMKR-----ARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 424 DIRNI----LASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-EI---LEDALCGYEGTL 495
Cdd:TIGR02142 106 SERRIsferVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKyEIlpyLERLHAEFGIPI 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1222187810 496 LFISHDRYFLNRVANRIFeLTPEGIEETIGNYDDYARTK 534
Cdd:TIGR02142 186 LYVSHSLQEVLRLADRVV-VLEDGRVAAAGPIAEVWASP 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-238 |
1.09e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.13 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGEchhdtgtldkkngltlgllsqefkasEHET 81
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE--------------------------ERPT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 VGAIFTAAfQDLIEM-EGQIQSLQQRIDtaqateqqrLVHQ---------------LAeLQEQYADRGgfEYHSRIRGV- 144
Cdd:COG2884 56 SGQVLVNG-QDLSRLkRREIPYLRRRIG---------VVFQdfrllpdrtvyenvaLP-LRVTGKSRK--EIRRRVREVl 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 145 -TIGLGfqlkDLEKAF-GTFSGGEKTRIA-----------LgclllqspdllLLDEPTNYLDFES----LNWLESFlNNY 207
Cdd:COG2884 123 dLVGLS----DKAKALpHELSGGEQQRVAiaralvnrpelL-----------LADEPTGNLDPETsweiMELLEEI-NRR 186
|
250 260 270
....*....|....*....|....*....|.
gi 1222187810 208 KNAFIIVSHDRFFLDRVCKRICEIENTHMVS 238
Cdd:COG2884 187 GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
2-228 |
1.10e-07 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 53.16 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVH-------SIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT-LDKKNGLTLGLLsqe 73
Cdd:TIGR02324 1 LLEVEDLSKTFTLHqqggvrlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRiLVRHEGAWVDLA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 74 fKASEHE-------TVGaiFTAAFQDLI----EMEGQIQSLQQR---IDTAQAtEQQRLVHQLaELQEQyadrggfeyhs 139
Cdd:TIGR02324 78 -QASPREvlevrrkTIG--YVSQFLRVIprvsALEVVAEPLLERgvpREAARA-RARELLARL-NIPER----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 140 rirgvtiglgfqLKDLEKAfgTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSH 216
Cdd:TIGR02324 142 ------------LWHLPPA--TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKArgaALIGIFH 207
|
250
....*....|..
gi 1222187810 217 DRFFLDRVCKRI 228
Cdd:TIGR02324 208 DEEVRELVADRV 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-59 |
1.44e-07 |
|
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: 51.28 E-value: 1.44e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 11 SYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:cd03216 9 RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI 57
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
326-512 |
1.68e-07 |
|
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: 52.73 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRIVF-GRKVypgyyAQEPDEAL-- 402
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEivgligpngagKTTLFNLITGFYRPTSGRILFdGRDI-----TGLPPHRIar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 -----------LAPNETLIDAIRdIDSHLTDGdiRNILASFLFTGESVFKH-----------------------SGDLSG 448
Cdd:COG0411 79 lgiartfqnprLFPELTVLENVL-VAAHARLG--RGLLAALLRLPRARREEreareraeellervgladradepAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 449 GEKARLNMARLMVSESNFLLMDEPT---NHIDmsTREILE--DALCGYEG-TLLFISHDRYFLNRVANRI 512
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAaglNPEE--TEELAEliRRLRDERGiTILLIEHDMDLVMGLADRI 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-517 |
1.74e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 31 LGLIGRNGCGKSTFFKLLTGE-----CHHDtGTLDKKNGLtlgllsQEFKASEHETVgaiftaaFQDLIEmeGQIQSLQ- 104
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGElipnlGDYE-EEPSWDEVL------KRFRGTELQNY-------FKKLYN--GEIKVVHk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 105 -QRIDTAQateqQRLVHQLAELQEQYADRGGF-EYHSRIrgvtiGLGfqlKDLEKAFGTFSGGEKTRIALGCLLLQSPDL 182
Cdd:PRK13409 166 pQYVDLIP----KVFKGKVRELLKKVDERGKLdEVVERL-----GLE---NILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 183 LLLDEPTNYLD-FESLN---WLESFLNNykNAFIIVSHDRFFLDRVCkriceiENTHmVSY--TGNYTQYLDKKAKRdra 256
Cdd:PRK13409 234 YFFDEPTSYLDiRQRLNvarLIRELAEG--KYVLVVEHDLAVLDYLA------DNVH-IAYgePGAYGVVSKPKGVR--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 257 ldAAYNKQMKELTRQQKIvdRLRDYnsvqssrraasrekAIE-RITPIERRQDRRSLhFSFSPkvlsgndvlmvegLEKS 335
Cdd:PRK13409 302 --VGINEYLKGYLPEENM--RIRPE--------------PIEfEERPPRDESERETL-VEYPD-------------LTKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 336 FGDRQLFKNVGfEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKV-Y-PGYYAQEPD---EALLApnetli 410
Cdd:PRK13409 350 LGDFSLEVEGG-EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsYkPQYIKPDYDgtvEDLLR------ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 411 DAIRDIDSHLTDGDIRNILASflftgESVFKHS-GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALC 489
Cdd:PRK13409 423 SITDDLGSSYYKSEIIKPLQL-----ERLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
490 500 510
....*....|....*....|....*....|....
gi 1222187810 490 GY----EGTLLFISHDRYFLNRVANRI--FELTP 517
Cdd:PRK13409 498 RIaeerEATALVVDHDIYMIDYISDRLmvFEGEP 531
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
446-479 |
1.77e-07 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 52.89 E-value: 1.77e-07
10 20 30
....*....|....*....|....*....|....
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMS 479
Cdd:TIGR03873 138 LSGGERQRVHVARALAQEPKLLLLDEPTNHLDVR 171
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
327-488 |
1.92e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.62 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF---GRKVYPGYYAQEPDEALL 403
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 404 A----------PNETL---IDAIRDIDSHLTD------GDIRNILASFLFTGESVFKHSGDL----SGGEKARLNMARLM 460
Cdd:PRK11701 87 LrtewgfvhqhPRDGLrmqVSAGGNIGERLMAvgarhyGDIRATAGDWLERVEIDAARIDDLpttfSGGMQQRLQIARNL 166
|
170 180
....*....|....*....|....*...
gi 1222187810 461 VSESNFLLMDEPTNHIDMSTREILEDAL 488
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLL 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-50 |
1.98e-07 |
|
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: 52.29 E-value: 1.98e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG 53
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-50 |
2.12e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.39 E-value: 2.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1222187810 11 SYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-50 |
2.22e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 52.40 E-value: 2.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1222187810 1 MLININELSFSY----GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG 59
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-238 |
2.28e-07 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 51.97 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHS----IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLtgechhdtGTLDKK-------NGLTLGLL 70
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL--------GGLDRPtsgevliDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 71 SQ----EFKAsehETVGAIF---------TAAFQdlIEMEGQIQSLQQRIDTAQATEQQRLVHqLAELQEQYADrggfey 137
Cdd:COG1136 76 SErelaRLRR---RHIGFVFqffnllpelTALEN--VALPLLLAGVSRKERRERARELLERVG-LGDRLDHRPS------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 138 hsrirgvtiglgfQLkdlekafgtfSGGEKTRIA------------LGclllqspdllllDEPTNYLDFES----LNWLE 201
Cdd:COG1136 144 -------------QL----------SGGQQQRVAiaralvnrpkliLA------------DEPTGNLDSKTgeevLELLR 188
|
250 260 270
....*....|....*....|....*....|....*..
gi 1222187810 202 SFLNNYKNAFIIVSHDRFFLDRvCKRICEIENTHMVS 238
Cdd:COG1136 189 ELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
329-536 |
2.55e-07 |
|
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: 51.96 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDEAL------ 402
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFvfqhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 LAPNETLID------AIRDIDSHLTDGDIRNILASFL-FTGESVF--KHSGDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:cd03296 85 LFRHMTVFDnvafglRVKPRSERPPEAEIRAKVHELLkLVQLDWLadRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 474 NHIDMSTREILEDALCGYEG----TLLFISHDRYFLNRVANRIFELTpEGIEETIGNYDDYARTKQN 536
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMN-KGRIEQVGTPDEVYDHPAS 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
442-501 |
2.67e-07 |
|
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: 51.80 E-value: 2.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 442 HSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID-MSTREIlEDALCGY--EGTLLFISHD 501
Cdd:cd03260 138 HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELkkEYTIVIVTHN 199
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-512 |
2.75e-07 |
|
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: 51.92 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 330 EGLEKSFGDRQ-LFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG-------------RKVypGYYA 395
Cdd:cd03295 4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgedireqdpvelrRKI--GYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 QEpdeALLAP------NETLIDAIRDIDSHLTDGDIRNILASF-LFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLL 468
Cdd:cd03295 82 QQ---IGLFPhmtveeNIALVPKLLKWPKEKIRERADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1222187810 469 MDEPTNHIDMSTREILEDALCGYE----GTLLFISHDRYFLNRVANRI 512
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDIDEAFRLADRI 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
336-547 |
3.62e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 336 FGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIvfgrkvypgyyAQEPDEAL--LAPNE------ 407
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLgkLRQDQfafeef 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 408 TLIDAI-------------RD-IDS--HLTDGD---IRNILASFL----FTGES------------VFKHSGDLSG---G 449
Cdd:PRK15064 80 TVLDTVimghtelwevkqeRDrIYAlpEMSEEDgmkVADLEVKFAemdgYTAEAragelllgvgipEEQHYGLMSEvapG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 450 EKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETIGNYDD 529
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260
....*....|....*....|
gi 1222187810 530 Y--ARTKQnqsdREALLAQN 547
Cdd:PRK15064 240 YmtAATQA----RERLLADN 255
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-196 |
3.91e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 50.70 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 11 SYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQefkaseHETVGAIFTAAF 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ------RSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 91 QDLIEMeGQiqslqqridtaqateqqrlvhqlaelqeqYADRGGFEYHSRI--RGVTIGL-GFQLKDLEK-AFGTFSGGE 166
Cdd:NF040873 75 RDLVAM-GR-----------------------------WARRGLWRRLTRDdrAAVDDALeRVGLADLAGrQLGELSGGQ 124
|
170 180 190
....*....|....*....|....*....|
gi 1222187810 167 KTRIALGCLLLQSPDLLLLDEPTNYLDFES 196
Cdd:NF040873 125 RQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
329-500 |
6.62e-07 |
|
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: 50.49 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDR--QLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKvypgyyaqepDEALLaPN 406
Cdd:cd03369 9 VENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----------DISTI-PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 407 ETLIDAIRDI--DSHLTDGDIRNILASF-------LFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID 477
Cdd:cd03369 78 EDLRSSLTIIpqDPTLFSGTIRSNLDPFdeysdeeIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190
....*....|....*....|....*....|.
gi 1222187810 478 MST--------REILEDAlcgyegTLLFISH 500
Cdd:cd03369 158 YATdaliqktiREEFTNS------TILTIAH 182
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
327-512 |
6.64e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 51.69 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHR------------GdrigiigrngigKTTLFQILMKQIKSDSGRIVFG-------- 386
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASgelvallgpsgsG------------KTTLLRIIAGLETPDSGRIVLNgrdlftnl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 387 ----RKVypGYYAQEPdeaLLAPNETLID----AIRDIDshLTDGDIRNILASFLftgESVF-KHSGD-----LSGGEKA 452
Cdd:COG1118 71 ppreRRV--GFVFQHY---ALFPHMTVAEniafGLRVRP--PSKAEIRARVEELL---ELVQlEGLADrypsqLSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 453 RLNMARLMVSESNFLLMDEPTNHIDMSTR--------EILEDalcgYEGTLLFISHDR---YflnRVANRI 512
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRkelrrwlrRLHDE----LGGTTVFVTHDQeeaL---ELADRV 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
330-515 |
8.07e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.44 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 330 EGLEKSF-GDRQLFKNVGFEIHRGDrigiigrngigKTTLFQILMKQIKSDSGRI-VFG---------------RKVypG 392
Cdd:COG2884 5 ENVSKRYpGGREALSDVSLEIEKGEfvfltgpsgagKSTLLKLLYGEERPTSGQVlVNGqdlsrlkrreipylrRRI--G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 393 YYAQepDEALLaPNETLID------AIRDIDSHLTDGDIRNILASF-LFTGESVFKHSgdLSGGEKARLNMARLMVSESN 465
Cdd:COG2884 83 VVFQ--DFRLL-PDRTVYEnvalplRVTGKSRKEIRRRVREVLDLVgLSDKAKALPHE--LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 466 FLLMDEPTNHIDMST-REILE--DALCGYEGTLLFISHDRYFLNRVANRIFEL 515
Cdd:COG2884 158 LLLADEPTGNLDPETsWEIMEllEEINRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-193 |
8.41e-07 |
|
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: 50.27 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHlGLIGRNGCGKSTFFKLLTGECHHDTGTL--------DKKNGL--TLGLLSQ 72
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlKQPQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 73 EFKASEHETVgaiftAAFQDLIEMEGQIQSLQQRidtaqateqQRLVHQLAELQ-EQYADrggfeyhsrirgvtiglgfq 151
Cdd:cd03264 80 EFGVYPNFTV-----REFLDYIAWLKGIPSKEVK---------ARVDEVLELVNlGDRAK-------------------- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1222187810 152 lkdleKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD 193
Cdd:cd03264 126 -----KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-50 |
8.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.76 E-value: 8.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHS--IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTG 57
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-535 |
9.30e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.81 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 439 VFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID----MSTREILEDALCGYEGTLLFISHDRYFLNRVA----- 509
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSdftaf 223
|
90 100 110
....*....|....*....|....*....|.
gi 1222187810 510 -----NRIFELTPEGIEETIGNYDDYARTKQ 535
Cdd:PRK14258 224 fkgneNRIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
310-512 |
9.55e-07 |
|
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: 49.78 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 310 RSLHFSFSPKVLSGNDVLmvegleksfgdrqlfKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKV 389
Cdd:cd03250 4 EDASFTWDSGEQETSFTL---------------KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 390 ypGYYAQEPdealLAPNETLIDAI---------------------RDIDShLTDGDIRNIlasflftGEsvfkhSG-DLS 447
Cdd:cd03250 69 --AYVSQEP----WIQNGTIRENIlfgkpfdeeryekvikacalePDLEI-LPDGDLTEI-------GE-----KGiNLS 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 448 GGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALCGY---EGTLLFISHDRYFLNRvANRI 512
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLllnNKTRILVTHQLQLLPH-ADQI 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
327-500 |
1.01e-06 |
|
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: 49.80 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIV-------FGRKVYPG---YYAQ 396
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggpldFQRDSIARgllYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 397 EPD-EALLAPNETLIDAIRDidsHLTDGdIRNILASFLFTGesvFKH--SGDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:cd03231 81 APGiKTTLSVLENLRFWHAD---HSDEQ-VEEALARVGLNG---FEDrpVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 1222187810 474 NHIDMSTREILEDAL---CGYEGTLLFISH 500
Cdd:cd03231 154 TALDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-227 |
1.09e-06 |
|
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: 51.73 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSY-----GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNG-----LT----- 66
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdMTkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 67 --------LGLLSQEFKASEHETVgaiftaaFQDLIEMEGqiqslqqrIDTAQATEQQRLVHQL--AELQEQYAdrggfe 136
Cdd:TIGR03269 359 grgrakryIGILHQEYDLYPHRTV-------LDNLTEAIG--------LELPDELARMKAVITLkmVGFDEEKA------ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 137 yhsrirgVTIglgfqlkdLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWL-ESFLNNYK---NAFI 212
Cdd:TIGR03269 418 -------EEI--------LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREemeQTFI 482
|
250
....*....|....*
gi 1222187810 213 IVSHDRFFLDRVCKR 227
Cdd:TIGR03269 483 IVSHDMDFVLDVCDR 497
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
329-529 |
1.29e-06 |
|
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: 49.93 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKV---YPGY----------YA 395
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHkrpvntvfqnYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 qepdealLAPNETLIDAI------RDIDSHLTDGDIRNILaSFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLM 469
Cdd:cd03300 83 -------LFPHLTVFENIafglrlKKLPKAEIKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222187810 470 DEPTNHIDMSTREILE---DALCGYEG-TLLFISHDRYFLNRVANRIFELTpEGIEETIGNYDD 529
Cdd:cd03300 155 DEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHDQEEALTMSDRIAVMN-KGKIQQIGTPEE 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-525 |
1.76e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.60 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 331 GLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGrkvypgyyAQEPDEALLAPNET- 408
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLG--------VPVPARARLARARIg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 409 LIDAIRDIDSHLT---------------DGDIRNILASFLFTGESVFKHS---GDLSGGEKARLNMARLMVSESNFLLMD 470
Cdd:PRK13536 118 VVPQFDNLDLEFTvrenllvfgryfgmsTREIEAVIPSLLEFARLESKADarvSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 471 EPTNHIDMSTREILED---ALCGYEGTLLFISH---------DRYFLNRVANRIFELTPEG-IEETIG 525
Cdd:PRK13536 198 EPTTGLDPHARHLIWErlrSLLARGKTILLTTHfmeeaerlcDRLCVLEAGRKIAEGRPHAlIDEHIG 265
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
326-486 |
1.90e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.10 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIvfgrkVYPGYYAQEPDEALLA- 404
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-----KLDGGDIDDPDVAEACh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 405 ---------PNETLIDAIRdIDSHLTDGDIRNILASFLFTGESVFKH--SGDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:PRK13539 77 ylghrnamkPALTVAENLE-FWAAFLGGEELDIAAALEAVGLAPLAHlpFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170
....*....|...
gi 1222187810 474 NHIDMSTREILED 486
Cdd:PRK13539 156 AALDAAAVALFAE 168
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-49 |
1.98e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.98 E-value: 1.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSY--GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLT 49
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-58 |
2.00e-06 |
|
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: 49.01 E-value: 2.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYG----VHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT 58
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE 60
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
2.17e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.21 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDkknglTLGllsqefkasehe 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT-----VLG------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 81 tvgaiftaafqdlIEMEGQIQSLQQRIDtaqateqqrLVHQLAELQEQYADRGG-------FEYHSR-IRGVTIGLgFQL 152
Cdd:PRK13536 103 -------------VPVPARARLARARIG---------VVPQFDNLDLEFTVRENllvfgryFGMSTReIEAVIPSL-LEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 153 KDLEKAFGT----FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFES--LNW--LESFLNNYKnAFIIVSHDRFFLDRV 224
Cdd:PRK13536 160 ARLESKADArvsdLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLARGK-TILLTTHFMEEAERL 238
|
250
....*....|....
gi 1222187810 225 CKRICEIENTHMVS 238
Cdd:PRK13536 239 CDRLCVLEAGRKIA 252
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
444-515 |
2.20e-06 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 49.27 E-value: 2.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILE--DALCGYEG-TLLFISHDRYFLNRvANRIFEL 515
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNRELGtTIVMVTHDPELAAR-ADRVIRL 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-229 |
2.21e-06 |
|
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: 49.04 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELS--FSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGE----------CHHDTGTLDKKNGLTLGLLSQ 72
Cdd:cd03263 3 IRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGElrptsgtayiNGYSIRTDRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 73 ------EFKASEHetvgaiftaafqdlIEMEGQIQSLQQRidtaQATEQQRLVHQLAELqEQYADRggfeyhsRIRgvti 146
Cdd:cd03263 83 fdalfdELTVREH--------------LRFYARLKGLPKS----EIKEEVELLLRVLGL-TDKANK-------RAR---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 147 glgfqlkdlekafgTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN--AFIIVSHDRFFLDRV 224
Cdd:cd03263 133 --------------TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEAL 198
|
....*
gi 1222187810 225 CKRIC 229
Cdd:cd03263 199 CDRIA 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.35e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHS-----IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL--------DKKNGLTL 67
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 68 GLLSQEF-----------KASE-HETVGAIFTAA----FQDLIEMEGQIQSLQQRIDTAQATEQQRLVHQLAELQEQYAD 131
Cdd:PRK13651 81 EKVLEKLviqktrfkkikKIKEiRRRVGVVFQFAeyqlFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 132 RGGFEyhsrirgvtiglgfqlkdlekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFE-SLNWLESFLNNYKNA 210
Cdd:PRK13651 161 RSPFE-------------------------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQG 215
|
250
....*....|....*....
gi 1222187810 211 --FIIVSHDrffLDRVCKR 227
Cdd:PRK13651 216 ktIILVTHD---LDNVLEW 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-58 |
2.58e-06 |
|
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: 49.04 E-value: 2.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT 58
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE 56
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
446-500 |
2.92e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.21 E-value: 2.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALCGYEG-TLLFISH 500
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITH 532
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-237 |
3.49e-06 |
|
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: 48.48 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVH-----------SIFN----------NLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdK 61
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslkSLFKrkyrevealkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 62 KNGLTLGLLSQEFKASehetVGAIFtaafqdliemeGQIQSLQQRIDTAQATEQQRLVHQLAElqeqyadrggFEYHSRI 141
Cdd:cd03267 80 VAGLVPWKRRKKFLRR----IGVVF-----------GQKTQLWWDLPVIDSFYLLAAIYDLPP----------ARFKKRL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 142 RGVTiglgfQLKDLEKAFGT----FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNY----KNAFII 213
Cdd:cd03267 135 DELS-----ELLDLEELLDTpvrqLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLL 209
|
250 260
....*....|....*....|....
gi 1222187810 214 VSHDRFFLDRVCKRICEIENTHMV 237
Cdd:cd03267 210 TSHYMKDIEALARRVLVIDKGRLL 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-58 |
3.61e-06 |
|
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: 48.88 E-value: 3.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1222187810 19 NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT 58
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR 60
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
329-523 |
3.63e-06 |
|
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: 48.82 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngIGKTTLFQILMKQIKSDSGRI-VFGRKVypgyyAQEPDEALlapne 407
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEilaiiggsgSGKSVLLKLIIGLLRPDSGEIlVDGQDI-----TGLSEKEL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 408 tliDAIRD-----------IDS---------------HLTDGDIRNI---------LASF--LFTGEsvfkhsgdLSGGE 450
Cdd:COG1127 78 ---YELRRrigmlfqggalFDSltvfenvafplrehtDLSEAEIRELvleklelvgLPGAadKMPSE--------LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 451 KARLNMARLMVSESNFLLMDEPTNHID-MSTREILE------DALcgyEGTLLFISHDRYFLNRVANRI---------FE 514
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpITSAVIDElirelrDEL---GLTSVVVTHDLDSAFAIADRVavladgkiiAE 223
|
....*....
gi 1222187810 515 LTPEGIEET 523
Cdd:COG1127 224 GTPEELLAS 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
415-500 |
4.41e-06 |
|
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: 48.26 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 415 DIDSHLTDGDIRNIL---------ASFLFTGESVFKHSGD-LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREIL 484
Cdd:cd03244 99 DPFGEYSDEELWQALervglkefvESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI 178
|
90 100
....*....|....*....|..
gi 1222187810 485 EDAL------CgyegTLLFISH 500
Cdd:cd03244 179 QKTIreafkdC----TVLTIAH 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-50 |
4.86e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.52 E-value: 4.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG 60
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
343-525 |
4.97e-06 |
|
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: 48.23 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 343 KNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKVY-PGyyaqePDEALLAPNETLID--------- 411
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITePG-----PDRMVVFQNYSLLPwltvrenia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 412 -AIRDIDSHLTDGDIRNILASFLFT---GESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDA 487
Cdd:TIGR01184 77 lAVDRVLPDLSKSERRAIVEEHIALvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1222187810 488 LCG----YEGTLLFISHDRYFLNRVANRIFELTpEGIEETIG 525
Cdd:TIGR01184 157 LMQiweeHRVTVLMVTHDVDEALLLSDRVVMLT-NGPAANIG 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-512 |
5.87e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 322 SGNDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMK-------QIKSDSGRIVFGRKVYP--- 391
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiydsKIKVDGKVLYFGKDIFQida 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 392 -------GYYAQEPDEAllaPNETLIDAIR-DIDSH--LTDGDIRNILASFLF-------TGESVFKHSGDLSGGEKARL 454
Cdd:PRK14246 86 iklrkevGMVFQQPNPF---PHLSIYDNIAyPLKSHgiKEKREIKKIVEECLRkvglwkeVYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 455 NMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY--EGTLLFISHDRYFLNRVANRI 512
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYV 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
5.92e-06 |
|
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: 48.13 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 31 LGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLlsQEFKASEhetvgaiftaaFQDLIE--MEGQIQSLQ--QR 106
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEIL--DEFRGSE-----------LQNYFTklLEGDVKVIVkpQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 107 IDTAQATEQQRLVhqlaELQEQYADRGGFEY---HSRIRGVtiglgfqlkdLEKAFGTFSGGEKTRIALGCLLLQSPDLL 183
Cdd:cd03236 96 VDLIPKAVKGKVG----ELLKKKDERGKLDElvdQLELRHV----------LDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1222187810 184 LLDEPTNYLDF-ESLNW--LESFLNNYKNAFIIVSHDRFFLDRVCKRIC 229
Cdd:cd03236 162 FFDEPSSYLDIkQRLNAarLIRELAEDDNYVLVVEHDLAVLDYLSDYIH 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
339-573 |
6.24e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 339 RQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVypGYYAQEP-----------------DEA 401
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQAwimnatvrgnilffdeeDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 402 LLApnetliDAIRdiDSHLtDGDIRNiLASFLFT--GESvfkhSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMS 479
Cdd:PTZ00243 751 RLA------DAVR--VSQL-EADLAQ-LGGGLETeiGEK----GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 480 TRE-ILEDALCGYEG--TLLFISHDRYFLNRvANRIFELTPEGIEETiGNYDDYART----------------KQNQSDR 540
Cdd:PTZ00243 817 VGErVVEECFLGALAgkTRVLATHQVHVVPR-ADYVVALGDGRVEFS-GSSADFMRTslyatlaaelkenkdsKEGDADA 894
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1222187810 541 EAL-------LAQNHAPQINKTRRKQERQQAKALESERRR 573
Cdd:PTZ00243 895 EVAevdaapgGAVDHEPPVAKQEGNAEGGDGAALDAAAGR 934
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-50 |
6.43e-06 |
|
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: 47.51 E-value: 6.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG 48
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-227 |
6.70e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 16 SIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGechhdtgtLDKKNGLTLGLLSQEFKASEHE--------TVGAIFt 87
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAG--------LDDGSSGEVSLVGQPLHQMDEEaraklrakHVGFVF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 88 aafqdliemegqiQSLQQrIDTAQATEQQRLVHQLaelqeqyadRGGFEYHSRIRGVT----IGLGFQLKDLEkafGTFS 163
Cdd:PRK10584 95 -------------QSFML-IPTLNALENVELPALL---------RGESSRQSRNGAKAlleqLGLGKRLDHLP---AQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 164 GGEKTRIALGCLLLQSPDLLLLDEPTNYLDFES----LNWLESFLNNYKNAFIIVSHDRFFLDRvCKR 227
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHDLQLAAR-CDR 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-59 |
7.47e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.26 E-value: 7.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI 64
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
376-601 |
7.53e-06 |
|
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: 49.56 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 376 IKSDSGR--IVFGRKVYPGYYAQEPDEALLAPNETLidairdidshLTDGDIRNIlasflftGESvfkhSGDLSGGEKAR 453
Cdd:TIGR00957 710 IQNDSLRenILFGKALNEKYYQQVLEACALLPDLEI----------LPSGDRTEI-------GEK----GVNLSGGQKQR 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 454 LNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTL-----LFISHDRYFLNRVaNRIFELTPEGIEEtIGNYD 528
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQV-DVIIVMSGGKISE-MGSYQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 529 D--------------YARTKQNQ------------SDREALLAQNhAPQINKTRRKQERQQAKALESERRRQKKALAQLE 582
Cdd:TIGR00957 847 EllqrdgafaeflrtYAPDEQQGhledswtalvsgEGKEAKLIEN-GMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSA 925
|
250 260
....*....|....*....|.
gi 1222187810 583 E--QMESNDQRIAAYEADMCQ 601
Cdd:TIGR00957 926 ElqKAEAKEETWKLMEADKAQ 946
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-218 |
7.98e-06 |
|
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: 48.82 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLTLGLLSQefkASEHET 81
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-AVNGVPLADADA---DSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 VGAIFTAAFQdlieMEGQI-QSLQQRIDTAQATEQQRLVHQlAELQEQYADRGGfEYHSRI--RGVtiGLgfqlkdleka 158
Cdd:TIGR02857 398 IAWVPQHPFL----FAGTIaENIRLARPDASDAEIREALER-AGLDEFVAALPQ-GLDTPIgeGGA--GL---------- 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 159 fgtfSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN--AFIIVSHDR 218
Cdd:TIGR02857 460 ----SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-50 |
8.88e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.62 E-value: 8.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 3 ININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-217 |
9.19e-06 |
|
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: 48.18 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 7 ELSFS--YGVHSIfnNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLTLgllsqefkasehetvga 84
Cdd:TIGR02142 2 SARFSkrLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-VLNGRTL----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 iftaafqdliemegqiQSLQQRIDTAqaTEQQRL--VHQLAELQEQYADRGGFEY-HSRIRG---------VTIGLGFQl 152
Cdd:TIGR02142 62 ----------------FDSRKGIFLP--PEKRRIgyVFQEARLFPHLSVRGNLRYgMKRARPserrisferVIELLGIG- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 153 KDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD----FESLNWLESFLNNYKNAFIIVSHD 217
Cdd:TIGR02142 123 HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-50 |
9.57e-06 |
|
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: 47.43 E-value: 9.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1222187810 8 LSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG 48
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-48 |
9.76e-06 |
|
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: 47.18 E-value: 9.76e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL 46
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-216 |
1.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIF-----NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL--------DKKNGLT- 66
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditDKKVKLSd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 67 ----LGLLSQ--EFKASEhETVGAIFTAAFQDLIEMEGQIQslqQRIDTAQateqqrlvhQLAELQ-EQYADRGGFEyhs 139
Cdd:PRK13637 81 irkkVGLVFQypEYQLFE-ETIEKDIAFGPINLGLSEEEIE---NRVKRAM---------NIVGLDyEDYKDKSPFE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 140 rirgvtiglgfqlkdlekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD----FESLNWLESFLNNYKNAFIIVS 215
Cdd:PRK13637 145 ----------------------LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrDEILNKIKELHKEYNMTIILVS 202
|
.
gi 1222187810 216 H 216
Cdd:PRK13637 203 H 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-228 |
1.06e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.37 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIF---------NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLTLGLLSQ 72
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV-SWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 73 EFKASEHETVGAIftaaFQDLIEMEGQIQSLQQRIDtaqatEQQRlvhQLAELQEqyADRggfeyHSRIRGVTIGLGFQL 152
Cdd:PRK10419 82 AQRKAFRRDIQMV----FQDSISAVNPRKTVREIIR-----EPLR---HLLSLDK--AER-----LARASEMLRAVDLDD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 153 KDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDF----ESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRI 228
Cdd:PRK10419 143 SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRV 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
327-501 |
1.07e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.36 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKvyPGYYAQEP-----DEA 401
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA--PLAEAREDtrlmfQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 402 LLAPNETLIDairDIDSHLTdGDIRNILASFLftgESV--FKHSGD----LSGGEKARLNMARLMVSESNFLLMDEPTNH 475
Cdd:PRK11247 91 RLLPWKKVID---NVGLGLK-GQWRDAALQAL---AAVglADRANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190
....*....|....*....|....*....|
gi 1222187810 476 IDMSTR----EILEDALCGYEGTLLFISHD 501
Cdd:PRK11247 164 LDALTRiemqDLIESLWQQHGFTVLLVTHD 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
443-488 |
1.15e-05 |
|
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: 46.83 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 443 SGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDAL 488
Cdd:cd03254 137 GGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEAL 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-228 |
1.20e-05 |
|
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: 47.02 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 25 IDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGlTLGLLSQEFKAsehetvgaiftaafqdliEMEGQIQSLQ 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKA------------------DYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 105 QRIDTAQATEQQRLVHQLAELQ-EQYADRggfeyhsrirgvtiglgfQLKDLekafgtfSGGEKTRIALGCLLLQSPDLL 183
Cdd:cd03237 83 SSITKDFYTHPYFKTEIAKPLQiEQILDR------------------EVPEL-------SGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 184 LLDEPTNYLDFE----SLNWLESF-LNNYKNAFiIVSHDRFFLDRVCKRI 228
Cdd:cd03237 138 LLDEPSAYLDVEqrlmASKVIRRFaENNEKTAF-VVEHDIIMIDYLADRL 186
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-50 |
1.59e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 47.40 E-value: 1.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG 53
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-512 |
1.59e-05 |
|
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: 46.34 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLF--KNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGR-------KVYP--GYY 394
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYsirtdrkAARQslGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 395 AQepDEAL---LAPNETLI-----------DAIRDIDSHLTDGDI---RNilasflftgesvfKHSGDLSGGEKARLNMA 457
Cdd:cd03263 81 PQ--FDALfdeLTVREHLRfyarlkglpksEIKEEVELLLRVLGLtdkAN-------------KRARTLSGGMKRKLSLA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 458 RLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEG--TLLFISHDRYFLNRVANRI 512
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-60 |
1.69e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLD 60
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQ 69
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
326-501 |
1.87e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.76 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGD-RQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKvyPGYYA--------- 395
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK--PIDYSrkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 396 ------QEPDEALLAPNETLIDAIRDIDSHLTDGDIR----NILASflfTGESVFKHSGD--LSGGEKARLNMARLMVSE 463
Cdd:PRK13636 83 svgmvfQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRkrvdNALKR---TGIEHLKDKPThcLSFGQKKRVAIAGVLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1222187810 464 SNFLLMDEPTNHID-MSTREILEDALCGYEG---TLLFISHD 501
Cdd:PRK13636 160 PKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElglTIIIATHD 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
338-500 |
1.96e-05 |
|
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: 46.31 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 338 DRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGY-----------YAQEPdeALLA-- 404
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkylhskvslVGQEP--VLFArs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 405 ------------PNETLIDAIRDIDSHltdgDIRNILASFLFTGesVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:cd03248 104 lqdniayglqscSFECVKEAAQKAHAH----SFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190
....*....|....*....|....*....|
gi 1222187810 473 TNHIDMSTREILEDAL--CGYEGTLLFISH 500
Cdd:cd03248 178 TSALDAESEQQVQQALydWPERRTVLVIAH 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-73 |
2.00e-05 |
|
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: 47.45 E-value: 2.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 3 ININELSFSYGVHS-IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLTLGLLSQE 73
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI-LINGVDLSDLDPA 407
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-528 |
2.02e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.25 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 324 NDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVY----PGYYAQEPD 399
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 400 EALLAP---NETLID------AIRDIdsHLTDGDIRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMD 470
Cdd:PRK10247 85 YCAQTPtlfGDTVYDnlifpwQIRNQ--QPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 471 EPTNHIDMSTREILEDALCGY----EGTLLFISHDRYFLNRvANRIFELTPEGIEETIGNYD 528
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKDEINH-ADKVITLQPHAGEMQEARYE 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-50 |
3.08e-05 |
|
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: 45.66 E-value: 3.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSI--FNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG 52
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-61 |
3.43e-05 |
|
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: 44.45 E-value: 3.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1222187810 20 NLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDK 61
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM 60
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
341-489 |
3.44e-05 |
|
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: 47.21 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 341 LFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVfgrkvYPGYYAQEPDEALLAP---NETLI-----DA 412
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----HSGRISFSPQTSWIMPgtiKDNIIfglsyDE 515
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 413 IRdIDSHLTDGDIRNILASFLFTGESVFKHSG-DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALC 489
Cdd:TIGR01271 516 YR-YTSVIKACQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFESCLC 593
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-50 |
3.45e-05 |
|
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: 44.90 E-value: 3.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYG--VHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG 50
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-217 |
3.71e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGV-----------HSIFNNLDFRIDDAEHLGLIGRNGCGKST----FFKLLT--GECHHDTGTLDKKN 63
Cdd:PRK15134 274 PLLDVEQLQVAFPIrkgilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 64 GLTLGLLSQEFKAsehetvgaiftaAFQDliemegQIQSLQQRIDTAQATEQQRLVHQ---LAELQEQyadrggfeyhsR 140
Cdd:PRK15134 354 RRQLLPVRHRIQV------------VFQD------PNSSLNPRLNVLQIIEEGLRVHQptlSAAQREQ-----------Q 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 141 IRGVTIGLGFQLKDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD----FESLNWLESFLNNYKNAFIIVSH 216
Cdd:PRK15134 405 VIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISH 484
|
.
gi 1222187810 217 D 217
Cdd:PRK15134 485 D 485
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
444-500 |
3.72e-05 |
|
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: 45.18 E-value: 3.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILED---ALCGYEG-TLLFISH 500
Cdd:cd03298 127 GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlvlDLHAETKmTVLMVTH 187
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-48 |
3.74e-05 |
|
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: 45.10 E-value: 3.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1222187810 3 ININELSFSYGVH--SIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL 54
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-43 |
3.74e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.22 E-value: 3.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKST 43
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKST 44
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
446-501 |
3.98e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 45.62 E-value: 3.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTRE----ILEDALCGYEGTLLFISHD 501
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREqmqeLLLDVWQRTGKGVFLITHS 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-50 |
4.54e-05 |
|
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: 45.36 E-value: 4.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG 51
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
446-519 |
4.57e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.34 E-value: 4.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG--YEGTLLFISHdRYFLNRVANRIFELTPEG 519
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
446-515 |
5.27e-05 |
|
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: 44.71 E-value: 5.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILE--DALCGYEGTLLFISHDRYFLNRVANRIFEL 515
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtWEIMNllKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
446-509 |
5.34e-05 |
|
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: 46.22 E-value: 5.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-EILE--DALCGYEG-TLLFISHD----RYFLNRVA 509
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQaQILDllRDLQREHGlAYLFISHDlavvRALAHRVM 497
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-229 |
5.98e-05 |
|
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: 44.83 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL---------DKKNGLTL----GL 69
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltdDKKNINELrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 70 LSQEFKASEHETVgaiftaaFQDLieMEGQIQSLQQRIDTAQATeqqrlvhqlaelQEQYADRGGfeyhsrirgvtiglg 149
Cdd:cd03262 81 VFQQFNLFPHLTV-------LENI--TLAPIKVKGMSKAEAEER------------ALELLEKVG--------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 150 fqLKDLEKAF-GTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFEslnWLESFLNNYKN------AFIIVSHDRFFLD 222
Cdd:cd03262 125 --LADKADAYpAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMKDlaeegmTMVVVTHEMGFAR 199
|
....*..
gi 1222187810 223 RVCKRIC 229
Cdd:cd03262 200 EVADRVI 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
327-522 |
6.08e-05 |
|
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: 44.87 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGD-RQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG----------------RKV 389
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklkgkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 390 ypGYYAQEPDealLAPNETLIDAI-----------RDIDSHLTDGDIRNILASFLFTG--ESVFKHSGDLSGGEKARLNM 456
Cdd:cd03256 81 --GMIFQQFN---LIERLSVLENVlsgrlgrrstwRSLFGLFPKEEKQRALAALERVGllDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 457 ARLMVSESNFLLMDEPTNHID-MSTREILED--ALCGYEGTLLFIS-HD----RYFLNRV----ANRI-FELTPEGIEE 522
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDpASSRQVMDLlkRINREEGITVIVSlHQvdlaREYADRIvglkDGRIvFDGPPAELTD 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
329-533 |
6.18e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.46 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG-----------RKVypGY---- 393
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhardRKV--GFvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 394 YA---------------------QEPDEALLAPNET-LIDAIRDidSHLTDgdirnilasflftgesvfKHSGDLSGGEK 451
Cdd:PRK10851 83 YAlfrhmtvfdniafgltvlprrERPNAAAIKAKVTqLLEMVQL--AHLAD------------------RYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 452 ARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG----YEGTLLFISHDRYFLNRVANRIFELTpEGIEETIGNY 527
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVVMS-QGNIEQAGTP 221
|
....*.
gi 1222187810 528 DDYART 533
Cdd:PRK10851 222 DQVWRE 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-226 |
6.46e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 6 NELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLT-------------GEchHDTGTLDKKNGLTLGLLSQ 72
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldGE--HIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 73 efkasEHETVGAIftaafqdliemegQIQSLQQRidtaqateqQRLVHQLAELQEQYADRGGFEYHSRIRGVTiGLGFQL 152
Cdd:PRK10253 89 -----NATTPGDI-------------TVQELVAR---------GRYPHQPLFTRWRKEDEEAVTKAMQATGIT-HLADQS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 153 KDlekafgTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDF-ESLNWLE--SFLNNYKN-AFIIVSHDrffLDRVCK 226
Cdd:PRK10253 141 VD------TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNREKGyTLAAVLHD---LNQACR 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
440-512 |
6.88e-05 |
|
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: 44.94 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 440 FKHS--GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEG----TLLFISHDryfLN---RVAN 510
Cdd:cd03294 153 WEHKypDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAelqkTIVFITHD---LDealRLGD 229
|
..
gi 1222187810 511 RI 512
Cdd:cd03294 230 RI 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
338-480 |
7.10e-05 |
|
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: 44.57 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 338 DRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSD---SGRIVF-GRKVYP-------GYYAQepDEALLaPN 406
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPRKPdqfqkcvAYVRQ--DDILL-PG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 407 ----ETL---------------IDAIRDID---SHLTDGDIRNIlasfLFTGesvfkhsgdLSGGEKARLNMARLMVSES 464
Cdd:cd03234 96 ltvrETLtytailrlprkssdaIRKKRVEDvllRDLALTRIGGN----LVKG---------ISGGERRRVSIAVQLLWDP 162
|
170
....*....|....*.
gi 1222187810 465 NFLLMDEPTNHIDMST 480
Cdd:cd03234 163 KVLILDEPTSGLDSFT 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
324-522 |
7.19e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.96 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 324 NDVLMVEGLEKSFGDRQLFKNVGFEIHRGDrigiigrngigkttLFQILMKqikSDSGRIVFGRKVYpgyYAQEPDEALL 403
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGD--------------VISIIGS---SGSGKSTFLRCIN---FLEKPSEGSI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 404 APNETLIDAIRDIDSHLTDGDIRNI---------------LASFLFTGESVF---------------------------- 440
Cdd:PRK10619 63 VVNGQTINLVRDKDGQLKVADKNQLrllrtrltmvfqhfnLWSHMTVLENVMeapiqvlglskqeareravkylakvgid 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 441 -----KHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDmstREILEDAL-----CGYEG-TLLFISHDRYFLNRVA 509
Cdd:PRK10619 143 eraqgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD---PELVGEVLrimqqLAEEGkTMVVVTHEMGFARHVS 219
|
250
....*....|...
gi 1222187810 510 NRIFELTPEGIEE 522
Cdd:PRK10619 220 SHVIFLHQGKIEE 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
326-477 |
7.51e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRK---VYP---------GY 393
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisLLPlhararrgiGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 394 YAQEPD-EALLAPNETLIdAIRDIDSHLTDgDIRNILASFLFTgESVFKHSGD-----LSGGEKARLNMARLMVSESNFL 467
Cdd:PRK10895 83 LPQEASiFRRLSVYDNLM-AVLQIRDDLSA-EQREDRANELME-EFHIEHLRDsmgqsLSGGERRRVEIARALAANPKFI 159
|
170
....*....|
gi 1222187810 468 LMDEPTNHID 477
Cdd:PRK10895 160 LLDEPFAGVD 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-59 |
7.78e-05 |
|
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: 44.00 E-value: 7.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 3 ININELSFSYG-----VHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV 62
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
446-500 |
7.86e-05 |
|
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: 44.53 E-value: 7.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILE--DALCGYEgTLLFISH 500
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTeREIQAalRDVSKGR-TTIVIAH 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-510 |
8.85e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 8.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 442 HSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID-MSTREILEDAL-CGYEGTLLFISHDRYFLNRVAN 510
Cdd:PRK14267 146 YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTAKIEELLFeLKKEYTIVLVTHSPAQAARVSD 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
446-480 |
8.89e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 8.89e-05
10 20 30
....*....|....*....|....*....|....*
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST 480
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
429-512 |
9.25e-05 |
|
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: 44.28 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 429 LASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID-MSTREILE--DALCGYEGTLLFISHDRYFL 505
Cdd:cd03266 120 LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREfiRQLRALGKCILFSTHIMQEV 199
|
....*..
gi 1222187810 506 NRVANRI 512
Cdd:cd03266 200 ERLCDRV 206
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
326-507 |
9.42e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEPDEALLAP 405
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 406 NETLID---AIRD---IDSHLTDGDIRNILASFLFTGESVFKHS-GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDM 478
Cdd:PRK13540 81 HRSGINpylTLREnclYDIHFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 1222187810 479 STREILEDALCGYE---GTLLFISHDRYFLNR 507
Cdd:PRK13540 161 LSLLTIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
446-517 |
9.66e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 44.72 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-------EILEDALcgyeG-TLLFISHD----RYFLNRVA---- 509
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQaqvlnllEDLQDEL----GlTYLFISHDlsvvRHISDRVAvmyl 233
|
....*...
gi 1222187810 510 NRIFELTP 517
Cdd:COG4608 234 GKIVEIAP 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-50 |
9.66e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 9.66e-05
10 20 30
....*....|....*....|....*....|..
gi 1222187810 19 NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG 70
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
327-473 |
1.03e-04 |
|
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: 43.72 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGdRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKV--YP-------GYYAQ 396
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVlkQPqklrrriGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 397 EPDealLAPNETLID------AIRDIDSHLTDGDIRNILASfLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMD 470
Cdd:cd03264 80 EFG---VYPNFTVREfldyiaWLKGIPSKEVKARVDEVLEL-VNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
...
gi 1222187810 471 EPT 473
Cdd:cd03264 156 EPT 158
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-58 |
1.04e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.94 E-value: 1.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT 58
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR 70
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
446-512 |
1.05e-04 |
|
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: 44.11 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHID-MSTREILE---DALCGYEGTLLFISHDRYFLNRVANRI 512
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDpETTQSILAllrDINRELGLTIVLITHEMEVVKRICDRV 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
446-480 |
1.08e-04 |
|
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: 43.69 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....*
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST 480
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
445-566 |
1.10e-04 |
|
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: 44.32 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 445 DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY----EGTLLFISHDRYFLNRVANR--IFELTP- 517
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRliVFEGEPs 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 518 ------------EGIEETIGNYDDYARTKQNqsdreallaqNHAPQINKTRRKQERQQAKA 566
Cdd:cd03237 195 vngvanppqslrSGMNRFLKNLDITFRRDPE----------TGRPRINKLGSVKDREQKES 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
331-480 |
1.28e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 331 GLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFgrkvypgyyaqEPDEALLAPNETLI 410
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------DVPDNQFGREASLI 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 411 DAIRDIDSHLtdgDIRNILAS------FLFTgeSVFKHsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST 480
Cdd:COG2401 104 DAIGRKGDFK---DAVELLNAvglsdaVLWL--RRFKE---LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2-51 |
1.29e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.05 E-value: 1.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGE 51
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGD 50
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
327-512 |
1.29e-04 |
|
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: 42.97 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQ--LFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG----RKVYP-------GY 393
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDgadiSQWDPnelgdhvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 394 YAQepdeallapnetlidairdiDSHLTDGDIR-NIlasflftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:cd03246 81 LPQ--------------------DDELFSGSIAeNI-----------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1222187810 473 TNHIDMSTREILEDA---LCGYEGTLLFISHDRYFLNRvANRI 512
Cdd:cd03246 124 NSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLAS-ADRI 165
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-489 |
1.41e-04 |
|
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: 44.08 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 341 LFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVfgrkvYPGYYAQEPDEALLAP---NETLI-----DA 412
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----HSGRISFSSQFSWIMPgtiKENIIfgvsyDE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 413 IRdIDSHLTDGDIRNILASFLFTGESVFKHSG-DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMST-REILEDALC 489
Cdd:cd03291 127 YR-YKSVVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeKEIFESCVC 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-239 |
1.43e-04 |
|
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: 43.42 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdkkngltlgllsqEFKasehetv 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-------------LFD------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 83 GAIFTAAFQDLI----EMEGQIQSLQQRidtaqatEQQRLVHQLAELQEQYADRGGFEYHSRirgvtiglgFQLKDL-EK 157
Cdd:cd03269 61 GKPLDIAARNRIgylpEERGLYPKMKVI-------DQLVYLAQLKGLKKEEARRRIDEWLER---------LELSEYaNK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 158 AFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKNA---FIIVSHDRFFLDRVCKRICEIENT 234
Cdd:cd03269 125 RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKG 204
|
....*
gi 1222187810 235 HMVSY 239
Cdd:cd03269 205 RAVLY 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
325-501 |
1.58e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.95 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 325 DVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFGRKVYPGYYAQEP--DEAL 402
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 ---------LAPN---ETLIDAIRDIDS-HLTDGDIRNilasflftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLM 469
Cdd:PRK09544 83 pltvnrflrLRPGtkkEDILPALKRVQAgHLIDAPMQK------------------LSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1222187810 470 DEPTNHIDMSTREILEDAL--------CGyegtLLFISHD 501
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIdqlrreldCA----VLMVSHD 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-50 |
1.65e-04 |
|
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: 43.58 E-value: 1.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG 48
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
343-513 |
1.71e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 343 KNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG---------------RKVypGYYAQEPDEALLapnE 407
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkkvklsdirKKV--GLVFQYPEYQLF---E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 408 TLIDaiRDI-----DSHLTDGDIRN-ILASFLFTGES--VFKHSG--DLSGGEKARLNMARLMVSESNFLLMDEPTNHID 477
Cdd:PRK13637 99 ETIE--KDIafgpiNLGLSEEEIENrVKRAMNIVGLDyeDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1222187810 478 MSTR-EILE---DALCGYEGTLLFISHDRYFLNRVANRIF 513
Cdd:PRK13637 177 PKGRdEILNkikELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
446-509 |
1.71e-04 |
|
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: 44.27 E-value: 1.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-EILE--DALCGYEG-TLLFISHD----RYFLNRVA 509
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQaQILNllKDLQRELGlAILFITHDlgvvAEIADRVA 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-73 |
1.76e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.56 E-value: 1.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTLGLLSQE 73
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK 75
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-193 |
2.16e-04 |
|
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: 44.35 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHS-IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG--ECHHDTGTLDKKN--GLTLGLLSQEFKAS 77
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGffQARSGEILLNGFSlkDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 78 EHETVgaIFTAAFQDLIEMEGQIQSLQQRIDTAQateqqrlvhQLAELQEQyadrggfeyhsrIRGVTIGLGfqlKDLEK 157
Cdd:TIGR01193 554 PQEPY--IFSGSILENLLLGAKENVSQDEIWAAC---------EIAEIKDD------------IENMPLGYQ---TELSE 607
|
170 180 190
....*....|....*....|....*....|....*.
gi 1222187810 158 AFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD 193
Cdd:TIGR01193 608 EGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
445-533 |
2.19e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.87 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 445 DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDAL----CGYEGTLLFISHDRYFLNRVANRIF-----EL 515
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHDLDEAMRIGDRIAimqngEV 243
|
90 100
....*....|....*....|
gi 1222187810 516 TPEGIEETIGN--YDDYART 533
Cdd:PRK10070 244 VQVGTPDEILNnpANDYVRT 263
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-58 |
2.38e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.56 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT 58
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE 57
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-59 |
2.51e-04 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 43.60 E-value: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI 59
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-50 |
2.71e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|..
gi 1222187810 19 NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTG 314
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
446-516 |
2.75e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.94 E-value: 2.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDmstREILEDALCGYEG------TLLFISHDRYFLNRVANRIFELT 516
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD---DALSEGILRLFEEfnrvgvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-67 |
2.89e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 2.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 15 HSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKNGLTL 67
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL 89
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-224 |
2.90e-04 |
|
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: 42.51 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 5 INELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGecHHDTgtldkkngltlgllsqefkaseHETVGA 84
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKY----------------------EVTEGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 IFtaaF--QDLIEMEgqiqslqqridtaqATEQQRLVHQLAelqeqyadrggFEYHSRIRGVTigLGFQLKDLEKafgTF 162
Cdd:cd03217 59 IL---FkgEDITDLP--------------PEERARLGIFLA-----------FQYPPEIPGVK--NADFLRYVNE---GF 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 163 SGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLDRV 224
Cdd:cd03217 106 SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYI 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-228 |
2.92e-04 |
|
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: 44.00 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 29 EHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKngLTLGLLSQEFKASEHETVgaiftaafQDLIEmegqiQSLQQRID 108
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--LKISYKPQYISPDYDGTV--------EEFLR-----SANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 109 TAQATEQ--QRLvhQLAELQEQYadrggfeyhsrirgvtiglgfqLKDLekafgtfSGGEKTRIALGCLLLQSPDLLLLD 186
Cdd:COG1245 432 SSYYKTEiiKPL--GLEKLLDKN----------------------VKDL-------SGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1222187810 187 EPTNYLDFES----LNWLESFLNNYKNAFIIVSHDRFFLDRVCKRI 228
Cdd:COG1245 481 EPSAHLDVEQrlavAKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-48 |
3.02e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.10 E-value: 3.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL 53
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-84 |
3.10e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 3.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 29 EHLGLIGRNGCGKSTFFKLLTGECHHDTGTLDKKngLTLGLLSQEFKASEHETVGA 84
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQYIKPDYDGTVED 419
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
444-500 |
3.20e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.65 E-value: 3.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-EILE--DALCGYEG-TLLFISH 500
Cdd:PRK10771 128 GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqEMLTlvSQVCQERQlTLLMVSH 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
446-500 |
3.41e-04 |
|
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: 43.58 E-value: 3.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISH 500
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-48 |
3.53e-04 |
|
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: 42.53 E-value: 3.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 3 ININELSFSYGV---HSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL 49
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
444-501 |
3.81e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 42.43 E-value: 3.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-EILE--DALCGYEG-TLLFISHD 501
Cdd:COG3840 128 GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRqEMLDlvDELCRERGlTVLMVTHD 189
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
446-512 |
3.93e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 3.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG----YEGTLLFISHDRYFLNRVANRI 512
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlnreHGTTLILVTHDLQLAARCDRRL 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-48 |
4.22e-04 |
|
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: 42.22 E-value: 4.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1222187810 3 ININELSFSYGVHS-IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL 47
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-48 |
4.27e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.33 E-value: 4.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1222187810 3 ININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-48 |
4.75e-04 |
|
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: 42.29 E-value: 4.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1222187810 3 ININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLL 48
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI 47
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-67 |
4.77e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 4.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGEchHDTGTldkKNGLTL 67
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD--HPQGY---SNDLTL 320
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-59 |
4.91e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 4.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1222187810 19 NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI 61
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
293-517 |
5.06e-04 |
|
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: 43.23 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 293 REKAIE-RITPIERRQDRRSLhFSFSpkvlsgndvlmveGLEKSFGDRQLFKNVGfEIHRGDRIGIIGRNGIGKTTLFQI 371
Cdd:COG1245 321 RDEPIEfEVHAPRREKEEETL-VEYP-------------DLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 372 LMKQIKSDSGRIVFGRKVypGYYAQ--EPDEallapNETLIDAIRDIdshltdgdIRNILASFLFTGEsVFKHSG----- 444
Cdd:COG1245 386 LAGVLKPDEGEVDEDLKI--SYKPQyiSPDY-----DGTVEEFLRSA--------NTDDFGSSYYKTE-IIKPLGlekll 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 445 -----DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALC----GYEGTLLFISHDRYFLNRVANRI--F 513
Cdd:COG1245 450 dknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLIDYISDRLmvF 529
|
....
gi 1222187810 514 ELTP 517
Cdd:COG1245 530 EGEP 533
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
444-500 |
5.30e-04 |
|
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: 41.99 E-value: 5.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTRE-ILE--DALCGYEG-TLLFISH 500
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARElLLAllDKLAAEGApTLVLVTH 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
446-535 |
5.34e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.07 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHID-MSTREIlEDALCGYEG--TLLFISHDRYFLNRVANRI-FELTPEGIE 521
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDpISAGKI-EETLLGLKDdyTMLLVTRSMQQASRISDRTgFFLDGDLIE 227
|
90
....*....|....
gi 1222187810 522 etignyddYARTKQ 535
Cdd:PRK14239 228 --------YNDTKQ 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-217 |
5.85e-04 |
|
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: 41.94 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdkknglTLGLLSQEFKASEHE 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI------LFGGEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 81 TVGAIFT--AAFQDLIEMEGQIQSL--QQRIDTAQATEQQRLVHQLAELQ--EQYADRggfeYHSrirgvtiglgfQLkd 154
Cdd:cd03296 75 NVGFVFQhyALFRHMTVFDNVAFGLrvKPRSERPPEAEIRAKVHELLKLVqlDWLADR----YPA-----------QL-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 155 lekafgtfSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDF----ESLNWLESFLNNYKNAFIIVSHD 217
Cdd:cd03296 138 --------SGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-196 |
7.42e-04 |
|
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: 41.70 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 3 ININELSFSYGVHS--IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGEC----------HHDTGTLDkKNGL--TLG 68
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYvpengrvlvdGHDLALAD-PAWLrrQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 69 LLSQEfkasehetvGAIFTAAFQDLIEMEGQIQSLQQRIDTAQATEQQRLVHQLAElqeqyadrgGFEYHSRIRGVtiGL 148
Cdd:cd03252 80 VVLQE---------NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPE---------GYDTIVGEQGA--GL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1222187810 149 gfqlkdlekafgtfSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFES 196
Cdd:cd03252 140 --------------SGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-512 |
7.54e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 20 NLDFRIDDAEHLGLIGRNGCGKS----TFFKLLT---GECHHDTGTLDKKNGLTLGLlsQEFKASEHETV-GAIFTAAFQ 91
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVQCDKMLLRRRSRQVIEL--SEQSAAQMRHVrGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 92 DLIEMEGQIQSLQQRIdtaqaTEQQRLvHQLAELQEQYADRGGFEYHSRIRGVTIGLGFQLKDLekafgtfSGGEKTRIA 171
Cdd:PRK10261 112 EPMTSLNPVFTVGEQI-----AESIRL-HQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQL-------SGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 172 LGCLLLQSPDLLLLDEPTNYLDF----ESLNWLESFLNNYKNAFIIVSHDRFFLDRVCKRICEIENTHMVSyTGNYTQYL 247
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE-TGSVEQIF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 248 DKKAK-RDRALDAAynkqmkeltrqqkiVDRLRDYNSVQSSRRAA--SREKAIERITPIErrQDrrslhfsfspKVLSGN 324
Cdd:PRK10261 258 HAPQHpYTRALLAA--------------VPQLGAMKGLDYPRRFPliSLEHPAKQEPPIE--QD----------TVVDGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 325 DVLMVEGLEKSFGDR-----------QLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKV--Y 390
Cdd:PRK10261 312 PILQVRNLVTRFPLRsgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRIdtL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 391 PGYYAQ----------EPDEALLAPNETLIDAIRD-IDSH-LTDGDIRNILASFLFT-----GESVFKHSGDLSGGEKAR 453
Cdd:PRK10261 392 SPGKLQalrrdiqfifQDPYASLDPRQTVGDSIMEpLRVHgLLPGKAAAARVAWLLErvgllPEHAWRYPHEFSGGQRQR 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222187810 454 LNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTL----LFISHDRYFLNRVANRI 512
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAVVERISHRV 534
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
446-501 |
8.13e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.61 E-value: 8.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG-YEGT---LLFISHD 501
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlWQETgkqVLLITHD 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-228 |
8.34e-04 |
|
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: 41.20 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYG-----VHSIfNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTG--TLDKKNGLT-------- 66
Cdd:cd03266 1 MITADALTKRFRdvkktVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfaTVDGFDVVKepaearrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 67 LGLLSQEFKASEHETVGAIFtAAFQDLIEMEGQiqSLQQRIDtaqateqqrlvhQLAELqeqyadrggfeyhsrirgvti 146
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENL-EYFAGLYGLKGD--ELTARLE------------ELADR--------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 147 glgFQLKD-LEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNYKN---AFIIVSHDRFFLD 222
Cdd:cd03266 124 ---LGMEElLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVE 200
|
....*.
gi 1222187810 223 RVCKRI 228
Cdd:cd03266 201 RLCDRV 206
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-59 |
8.51e-04 |
|
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: 42.48 E-value: 8.51e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1222187810 21 LDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-50 |
8.65e-04 |
|
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: 41.44 E-value: 8.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 3 ININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR 51
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
326-488 |
9.89e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.54 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDS---------GRIV--FGR------- 387
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVqrEGRlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 388 -KVYPGYYAQEPD--EALLAPNETLIDAI------RDIDSHLTDGDIRNILASFLFTGESVFKHS--GDLSGGEKARLNM 456
Cdd:PRK09984 84 sRANTGYIFQQFNlvNRLSVLENVLIGALgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQrvSTLSGGQQQRVAI 163
|
170 180 190
....*....|....*....|....*....|..
gi 1222187810 457 ARLMVSESNFLLMDEPTNHIDMSTREILEDAL 488
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
446-500 |
1.08e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.07 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY-EG-TLLFISH 500
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGrTTIVIAH 533
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-516 |
1.10e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 439 VFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILE---DALCGYEGTLLFISHDRYFLNRVANRIFEL 515
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQktiNNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
.
gi 1222187810 516 T 516
Cdd:PTZ00265 653 S 653
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
324-473 |
1.12e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.02 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 324 NDVLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKVYPGYYAQEPDEAL 402
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 403 -LAPNETLIDAIRDIDSHLTDGD-----------IRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMD 470
Cdd:PRK11614 83 aIVPEGRRVFSRMTVEENLAMGGffaerdqfqerIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
...
gi 1222187810 471 EPT 473
Cdd:PRK11614 163 EPS 165
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-246 |
1.12e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.15 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGEChhdtgTLDKKNGLTLGLLSQEfkasehet 81
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI-----TGDKSAGSHIELLGRT-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 82 vgaiftaafqdlIEMEGQIQS--LQQRIDTAQATEQQRLVHQLAELQEQYAD--------RGGFEYHSR------IRGVT 145
Cdd:PRK09984 71 ------------VQREGRLARdiRKSRANTGYIFQQFNLVNRLSVLENVLIGalgstpfwRTCFSWFTReqkqraLQALT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 146 -IGLGfqlKDLEKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFES----LNWLESFLNNYKNAFIIVSHDRFF 220
Cdd:PRK09984 139 rVGMV---HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDY 215
|
250 260
....*....|....*....|....*.
gi 1222187810 221 LDRVCKRICEIENTHmVSYTGNYTQY 246
Cdd:PRK09984 216 ALRYCERIVALRQGH-VFYDGSSQQF 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-50 |
1.37e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.54 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLInINELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:COG4136 1 MLS-LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG 49
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
329-512 |
1.39e-03 |
|
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: 40.59 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 329 VEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFgrkvypgyyaqepDEALLAPNET 408
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-------------DGLKLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 409 LIDAIR----------DIDSHLTdgDIRNI-LASFLFTGESV------------------FKHS--GDLSGGEKARLNMA 457
Cdd:cd03262 70 NINELRqkvgmvfqqfNLFPHLT--VLENItLAPIKVKGMSKaeaeeralellekvgladKADAypAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 458 RLMVSESNFLLMDEPTNHID--MsTREILE---DAlcGYEG-TLLFISHDRYFLNRVANRI 512
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDpeL-VGEVLDvmkDL--AEEGmTMVVVTHEMGFAREVADRV 205
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
326-515 |
1.40e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVFG--------RKVYPGYYAQE 397
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgktatrgdRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 398 PD-EALLAPNETL--IDAIRDIDSHLTDGdirNILASFLFTG--ESVFKHsgdLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:PRK13543 91 PGlKADLSTLENLhfLCGLHGRRAKQMPG---SALAIVGLAGyeDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1222187810 473 TNHIDMSTREILEDALCGY---EGTLLFISHDRYFLNRVANRIFEL 515
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
444-484 |
1.48e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDM-STREIL 484
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELL 168
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
446-482 |
1.56e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.16 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTRE 482
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
443-477 |
1.60e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.67 E-value: 1.60e-03
10 20 30
....*....|....*....|....*....|....*
gi 1222187810 443 SGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID 477
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
446-524 |
1.86e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 40.74 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALC------GYegTLLFISHD-----RYFLNRVANRIFE 514
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSelnrekGY--TLAAVLHDlnqacRYASHLIALREGK 221
|
90
....*....|
gi 1222187810 515 LTPEGIEETI 524
Cdd:PRK10253 222 IVAQGAPKEI 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-218 |
1.90e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 40.84 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 1 MLININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL-------------DKKngltL 67
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrlharDRK----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 68 GLLSQEFKASEHETVGaiftaafqDLIEMEGQIQSLQQRIDTA----QATEQQRLVhQLAELQEQYADrggfeyhsrirg 143
Cdd:PRK10851 77 GFVFQHYALFRHMTVF--------DNIAFGLTVLPRRERPNAAaikaKVTQLLEMV-QLAHLADRYPA------------ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 144 vtiglgfQLkdlekafgtfSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDF----ESLNWLESFLNNYKNAFIIVSHDR 218
Cdd:PRK10851 136 -------QL----------SGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
446-535 |
2.19e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEG--TLLFISHDRYFLNRVANR--IF---ELTPE 518
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRaaLFfdgRLVEE 243
|
90
....*....|....*..
gi 1222187810 519 GIEETIGNYDDYARTKQ 535
Cdd:PRK14271 244 GPTEQLFSSPKHAETAR 260
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
446-529 |
2.21e-03 |
|
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: 40.29 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG-YEG-TLLFISHdRYFLNRVANRIFELTPEGIEEt 523
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlMKNrTTFVIAH-RLSTIENADRIVVLEDGKIVE- 216
|
....*.
gi 1222187810 524 IGNYDD 529
Cdd:cd03251 217 RGTHEE 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
443-515 |
2.27e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.18 E-value: 2.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 443 SGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDM----STREILEDaLCGYEGT-LLFISHDRYFLNRVaNRIFEL 515
Cdd:PRK11629 143 PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnadSIFQLLGE-LNRLQGTaFLVVTHDLQLAKRM-SRQLEM 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
445-501 |
2.29e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.78 E-value: 2.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222187810 445 DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR-----EI--LEDALcgyEGTLLFISHD 501
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmriEIsrLHKRL---GRTMIYVTHD 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
144-223 |
2.49e-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: 39.23 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 144 VTIGLGFqLKdLEKAFGTFSGGEKTRIALGCLLLQSPDLLL--LDEPTNYLDFESLNWLESFLN---NYKNAFIIVSHDR 218
Cdd:cd03238 72 IDVGLGY-LT-LGQKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNL 149
|
....*
gi 1222187810 219 FFLDR 223
Cdd:cd03238 150 DVLSS 154
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
446-500 |
2.58e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY----EGTLLFISH 500
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
446-519 |
2.74e-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: 39.23 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSES--NFLLMDEPTNHIDMSTREILEDAL-----CGYegTLLFISHDRYFLNRvANRIFELTPE 518
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIkglidLGN--TVILIEHNLDVLSS-ADWIIDFGPG 164
|
.
gi 1222187810 519 G 519
Cdd:cd03238 165 S 165
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
2-224 |
2.83e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG--ECHHDTGTLDKKnGLTLGLLSQEFKASEh 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFK-GKDLLELSPEDRAGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 80 etvgAIFTAaFQDLIEMEGQIQS--LQQRIDTAQATEQQRLVHQL--AELQEQYADRGGFEYHSRIRGVTIGlgfqlkdl 155
Cdd:PRK09580 79 ----GIFMA-FQYPVEIPGVSNQffLQTALNAVRSYRGQEPLDRFdfQDLMEEKIALLKMPEDLLTRSVNVG-------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 156 ekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLN---NYKNAFIIVSHDRFFLDRV 224
Cdd:PRK09580 146 ------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNslrDGKRSFIIVTHYQRILDYI 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-207 |
2.95e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.17 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 2 LININELSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKlltgechHDTGTLDKKNGLTLGLLSQEFKASEHE 80
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFR-------HFNGILKPTSGSVLIRGEPITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 81 ---TVGAIFTAA----FQDLIEMEGQIQSLQQRIDTAqaTEQQRLVHQLAELQ-EQYADRggFEYHsrirgvtiglgfql 152
Cdd:PRK13652 76 vrkFVGLVFQNPddqiFSPTVEQDIAFGPINLGLDEE--TVAHRVSSALHMLGlEELRDR--VPHH-------------- 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 153 kdlekafgtFSGGEKTRIALGCLLLQSPDLLLLDEPTNYLDFESLNWLESFLNNY 207
Cdd:PRK13652 138 ---------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
446-501 |
2.95e-03 |
|
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: 39.72 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCG----YEGTLLFISHD 501
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElnreRGTTLVLVTHD 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
327-486 |
3.04e-03 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 40.21 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-------------GRKVypgy 393
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsaraaSRRV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 394 yAQEPDEALLAPN---ETLIDAIRdiDSHL------TDGDIRNILASFLFTGESVF--KHSGDLSGGEKARLNMARLMVS 462
Cdd:PRK09536 80 -ASVPQDTSLSFEfdvRQVVEMGR--TPHRsrfdtwTETDRAAVERAMERTGVAQFadRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190
....*....|....*....|....*....|..
gi 1222187810 463 ESNFLLMDEPTNHIDM--------STREILED 486
Cdd:PRK09536 157 ATPVLLLDEPTASLDInhqvrtleLVRRLVDD 188
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-512 |
3.22e-03 |
|
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: 38.95 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 323 GNDVLMVEGLekSFGDRqlFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRIVF-GRKVYP---------- 391
Cdd:cd03215 1 GEPVLEVRGL--SVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRrsprdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 392 -GYYAQEPDEALLAPNETLIDairdidshltdgdirNILASFLftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLMD 470
Cdd:cd03215 77 iAYVPEDRKREGLVLDLSVAE---------------NIALSSL------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1222187810 471 EPTNHIDMSTRE-----ILEDALCGyeGTLLFISHDRYFLNRVANRI 512
Cdd:cd03215 130 EPTRGVDVGAKAeiyrlIRELADAG--KAVLLISSELDELLGLCDRI 174
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
363-519 |
3.28e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 363 IGKTTLFQ-ILMkqiksdsgrIVFGRKVyPGYYAQEPDEALLAPNETLidAIRDID-SHLTDGDIR-----NILASFLFT 435
Cdd:cd03240 33 AGKTTIIEaLKY---------ALTGELP-PNSKGGAHDPKLIREGEVR--AQVKLAfENANGKKYTitrslAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 436 --GES---VFKHSGDLSGGEKA------RLNMARLMVSESNFLLMDEPT-----NHIDMSTREILEDALCGYEGTLLFIS 499
Cdd:cd03240 101 hqGESnwpLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTtnldeENIEESLAEIIEERKSQKNFQLIVIT 180
|
170 180
....*....|....*....|
gi 1222187810 500 HDRYFLNRvANRIFELTPEG 519
Cdd:cd03240 181 HDEELVDA-ADHIYRVEKDG 199
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
444-473 |
3.47e-03 |
|
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: 39.34 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|
gi 1222187810 444 GDLSGGEKARLNMARLMVSESNFLLMDEPT 473
Cdd:cd03224 131 GTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-67 |
3.79e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 39.61 E-value: 3.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 2 LININELSFSYGVHS--IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTLdKKNGLTL 67
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-TVGGMVL 71
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2-50 |
3.81e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 3.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG 49
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-49 |
4.04e-03 |
|
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: 39.14 E-value: 4.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 3 ININELSFSYGVH--SIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLT 49
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP 49
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
446-513 |
4.17e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 39.35 E-value: 4.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMS-TREILED--ALCGYEGTLLFISHDRYFLNRVANR-IF 513
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRaIF 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
446-529 |
4.17e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.33 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDAL-CGYEGTLLFISHDRYFLNRVANRIFELTPEGIEETi 524
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES- 550
|
....*
gi 1222187810 525 GNYDD 529
Cdd:PRK13657 551 GSFDE 555
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
446-500 |
4.28e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.09 E-value: 4.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY--EGTLLFISH 500
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
327-508 |
4.33e-03 |
|
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: 39.05 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 327 LMVEGLEKSFGDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILM--KQIKSDSGRIVFGRKVypgYYAQEPDE-ALL 403
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGED---ITDLPPEErARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 404 -------APNE----TLIDAIRDIDshltDGdirnilasflftgesvfkhsgdLSGGEKARLNMARLMVSESNFLLMDEP 472
Cdd:cd03217 78 giflafqYPPEipgvKNADFLRYVN----EG----------------------FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1222187810 473 TNHIDMSTREILEDALCGY--EGT-LLFISHDRYFLNRV 508
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYI 170
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-188 |
4.34e-03 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 39.18 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 8 LSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGT------------LDKKNGLTLGLLSQEfk 75
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgqdithlpMHERARLGIGYLPQE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 76 ASehetvgaiftaAFQDLIEMEGQIQSLQQRIDTAQATEQQRLVHQLAELQEQyadrggfeyHSRirgvtiglgfqlkdl 155
Cdd:TIGR04406 85 AS-----------IFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQIS---------HLR--------------- 129
|
170 180 190
....*....|....*....|....*....|...
gi 1222187810 156 EKAFGTFSGGEKTRIALGCLLLQSPDLLLLDEP 188
Cdd:TIGR04406 130 DNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-50 |
5.05e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 5.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 3 ININELSFSYGVHSI-FNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTG 371
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
439-515 |
5.07e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 40.09 E-value: 5.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222187810 439 VFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGYEGTLLFISHdRYFLNRVANRIFEL 515
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVL 686
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
445-501 |
5.08e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 39.30 E-value: 5.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 445 DLSGGEKARLNMARLMVSESNFLLMDEPTNHID-MSTREILE--DALCGYEGTLLFISHD 501
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-193 |
5.10e-03 |
|
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: 40.04 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 8 LSFSY-GVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG--ECHHDTGTLDkkngltlGLLSQEFKASEHETVGA 84
Cdd:TIGR02868 340 LSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGllDPLQGEVTLD-------GVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 85 IF--------TAAFQDLiemegqiqslqqRIDTAQATEQQrlvhqLAELQEQyadrggfeyhsrirgvtIGLGFQLKDLE 156
Cdd:TIGR02868 413 VCaqdahlfdTTVRENL------------RLARPDATDEE-----LWAALER-----------------VGLADWLRALP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1222187810 157 KAFGT--------FSGGEKTRIALGCLLLQSPDLLLLDEPTNYLD 193
Cdd:TIGR02868 459 DGLDTvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-59 |
5.28e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.14 E-value: 5.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDTGTL 59
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
337-529 |
5.30e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.40 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 337 GDRQLFKNVGFEIHRGDRIGIIGRNGIGKTTLFQILMKQIKSDSGRI-VFGRKV----------YPGYYAQEPDEALLAP 405
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlIRGEPItkenirevrkFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 406 NETLIDAIRDIDSHLTDGDIRNILASFLFT------GESVFKHsgdLSGGEKARLNMARLMVSESNFLLMDEPTNHID-M 478
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEETVAHRVSSALHMlgleelRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 479 STREI---LEDALCGYEGTLLFISHDRYFLNRVANRIF-----ELTPEGIEETIGNYDD 529
Cdd:PRK13652 172 GVKELidfLNDLPETYGMTVIFSTHQLDLVPEMADYIYvmdkgRIVAYGTVEEIFLQPD 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
405-519 |
5.40e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 39.28 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 405 PNETLIDAIRDIDSHLTDGD-------IRNILASFLFTGESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHID 477
Cdd:PRK10419 104 PRKTVREIIREPLRHLLSLDkaerlarASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 478 M----STREILEDaLCGYEGT-LLFISHD----RYFLNRVA----NRIFELTPEG 519
Cdd:PRK10419 184 LvlqaGVIRLLKK-LQQQFGTaCLFITHDlrlvERFCQRVMvmdnGQIVETQPVG 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-50 |
5.64e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 38.63 E-value: 5.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG 49
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-50 |
5.80e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 5.80e-03
10 20 30
....*....|....*....|....*....|..
gi 1222187810 19 NNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-56 |
6.37e-03 |
|
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: 39.42 E-value: 6.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1222187810 2 LININELSFSYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTGECHHDT 56
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT 55
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
446-502 |
6.58e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 39.31 E-value: 6.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222187810 446 LSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILEDALCGY----EGTLLFISHDR 502
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQ 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-501 |
7.07e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.30 E-value: 7.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222187810 437 ESVFKHSGDLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTR----EILEDALCGYEGTLLFISHD 501
Cdd:PRK15134 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQaqilALLKSLQQKHQLAYLFISHD 485
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-50 |
7.40e-03 |
|
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: 38.39 E-value: 7.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1222187810 11 SYGVHSIFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG 48
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
445-485 |
8.40e-03 |
|
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: 38.35 E-value: 8.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1222187810 445 DLSGGEKARLNMARLMVSESNFLLMDEPTNHIDMSTREILE 485
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
326-414 |
9.78e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.55 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222187810 326 VLMVEGLEKSFGDRQLFKNVGFEIHRGdrigiigrngiG-----------KTTLFQILMKQIKSDSGRI-VFGRKVYP-- 391
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKG-----------EifgllgpngagKTTTIRIILGILAPDSGEVlWDGEPLDPed 69
|
90 100
....*....|....*....|....*..
gi 1222187810 392 ----GYYaqePDEALLAPNETLIDAIR 414
Cdd:COG4152 70 rrriGYL---PEERGLYPKMKVGEQLV 93
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-50 |
9.80e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 37.93 E-value: 9.80e-03
10 20 30
....*....|....*....|....*....|....
gi 1222187810 17 IFNNLDFRIDDAEHLGLIGRNGCGKSTFFKLLTG 50
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG 50
|
|
| |
