|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-531 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 1190.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEEFT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDTVIMGHAELWEIKQERERIYSLPEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTVHPGNYDEY 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 241 MLAATQARERLLADNAKKKAQISELQSFVSRFSANASKSRQATSRAKQIEKIQLTEVKASSRQNPFIRFEQEKKLFRNAL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDFEVDM 400
Cdd:PRK15064 321 EVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 401 TVFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNM 480
Cdd:PRK15064 400 TLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNM 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 481 ALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDEFLAKKGID 531
Cdd:PRK15064 480 ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-527 |
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: 754.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEEFTVLDT 84
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAELWEIKQERERIYSLPEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGWKLRV 164
Cdd:COG0488 82 VLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTVHPGNYDEYMLAA 244
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 245 TQARERLLADNAKKKAQISELQSFVSRFSANASKSRQATSRAKQIEKIQLTEVKASSRqNPFIRFEQEKKLFRNALEVEN 324
Cdd:COG0488 242 AERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 325 IAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATdFEVDMTVFD 404
Cdd:COG0488 321 LSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEE-LDPDKTVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 405 WMSLWMkPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALEL 484
Cdd:COG0488 399 ELRDGA-PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 490363216 485 YQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDEFLAK 527
Cdd:COG0488 478 FPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-524 |
2.00e-93 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 297.85 E-value: 2.00e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEEfT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDTVIMGHAELWEIKQEreriysLPEMSEE-EGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 160 WKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTVHPGNYD- 238
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 239 -EYMLAATQARERLLADNAKKKaqISELQSFVSRFSANASKSRQATSRAKQIEKIQLteVKASSRQNPF-IRFEQEKKLF 316
Cdd:PRK10636 234 fEVQRATRLAQQQAMYESQQER--VAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDF 396
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIIL-DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 397 EVDMTVFDWMSLwMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIE 476
Cdd:PRK10636 389 RADESPLQHLAR-LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 490363216 477 SLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDEF 524
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-499 |
9.60e-91 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 290.70 E-value: 9.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LIS-NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEEFT 80
Cdd:PRK11147 3 LISiHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDTVIMGHAELWEIKQERERIYSL--PEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQhngPMSEVAP 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLveTDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTVHPGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 239 EYMLAATQAReRLLAD-NA---KKKAQiSEL---QSFVSRFSANASKSRQAtsRAKQIEKIQLTEVKASSRqnpfIRFEQ 311
Cdd:PRK11147 240 QYLLEKEEAL-RVEELqNAefdRKLAQ-EEVwirQGIKARRTRNEGRVRAL--KALRRERSERREVMGTAK----MQVEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 312 EKKLFRNALEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQd 391
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQ- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 392 HATDFEVDMTVFDWMSlwmkpeDDEQSV------RSVLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:PRK11147 390 HRAELDPEKTVMDNLA------EGKQEVmvngrpRHVLGYLqdfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLI 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 490363216 463 MDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFV 499
Cdd:PRK11147 464 LDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-528 |
1.60e-83 |
|
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: 269.50 E-value: 1.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEEFTVLDTVIMGHAE 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIKQERERIYSLpeMSEEEglrvADLEVKFGEM----------DGYTVESR---AGELLlnvgiPLEQHNGPMSEVAP 158
Cdd:TIGR03719 96 IKDALDRFNEISAK--YAEPD----ADFDKLAAEQaelqeiidaaDAWDLDSQleiAMDAL-----RCPPWDADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTVHPGNYD 238
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 239 EYMlaaTQARERLL----ADNAKKKAQISELQsfvsrFSANASKSRQATSRAKqIEKIQLTEVKASSRQNPF--IRFEQE 312
Cdd:TIGR03719 245 SWL---EQKQKRLEqeekEESARQKTLKRELE-----WVRQSPKGRQAKSKAR-LARYEELLSQEFQKRNETaeIYIPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 313 KKLFRNALEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDH 392
Cdd:TIGR03719 316 PRLGDKVIEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 393 AtDFEVDMTVFDWMS---LWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNH 469
Cdd:TIGR03719 395 D-ALDPNKTVWEEISgglDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 470 LDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPE-KVTNFQGTYDEFLAKK 528
Cdd:TIGR03719 474 LDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEYEEDK 533
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-524 |
1.63e-78 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 260.56 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG---DLAPTSGNVFLDPNERLGklkqdqfayEEFTVL 82
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaiDGIPKNCQILHVEQEVVG---------DDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 83 DTVIMGHAELWEIKQERERIYSLPEMSEEEGL-------------------RVADLEVKFGEMDGYTVESRAGELLLNVG 143
Cdd:PLN03073 253 QCVLNTDIERTQLLEEEAQLVAQQRELEFETEtgkgkgankdgvdkdavsqRLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 144 IPLEQHNGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMA 223
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 224 DLDYGGLTVHPGNYDEY-MLAATQARERLLADNAKKKAQiSELQSFVSRFSANASKSRQATSRAKQIEKIQLTEVKASsr 302
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFeRTREEQLKNQQKAFESNERSR-SHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVN-- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 303 qNPFIRFE---QEKKLFRNALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW 379
Cdd:PLN03073 490 -DPDYKFEfptPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 380 SENATIGYYAQDHATDFEVDMTVFDWMSLWMkPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 459
Cdd:PLN03073 569 SAKVRMAVFSQHHVDGLDLSSNPLLYMMRCF-PGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPH 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 460 VLIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDEF 524
Cdd:PLN03073 648 ILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-528 |
4.06e-77 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 252.73 E-value: 4.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEEFTVLDTVIMGHAE 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIKQERERIYSlpEMSEEEGL------RVADLEVKFGEMDGYTVESRagelllnvgipLEQH---------NGPMSEV 156
Cdd:PRK11819 98 VKAALDRFNEIYA--AYAEPDADfdalaaEQGELQEIIDAADAWDLDSQ-----------LEIAmdalrcppwDAKVTKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTVHPGN 236
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 237 YDEYMlaaTQARERLL----ADNAKKKAQISELQsFVsRFSAnasKSRQATSRAKqIEKIQLTEVKASSRQNPF--IRFE 310
Cdd:PRK11819 245 YSSWL---EQKAKRLAqeekQEAARQKALKRELE-WV-RQSP---KARQAKSKAR-LARYEELLSEEYQKRNETneIFIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 311 QEKKLFRNALEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQ 390
Cdd:PRK11819 316 PGPRLGDKVIEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHAtDFEVDMTVFDWMS---LWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:PRK11819 395 SRD-ALDPNKTVWEEISgglDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 468 NHLDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPE-KVTNFQGTYDEFLAKK 528
Cdd:PRK11819 474 NDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDsQVEWFEGNFQEYEEDK 535
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-528 |
9.06e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 197.98 E-value: 9.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 322 VENIAKGYEAnTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHatDFEVDMT 401
Cdd:COG0488 1 LENLSKSFGG-RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP--PLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 402 VFDWM---------------SLWMKPEDD----------------------EQSVRSVLGRLLFSQDDIKKSVKVLSGGE 444
Cdd:COG0488 78 VLDTVldgdaelraleaeleELEAKLAEPdedlerlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDEF 524
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY 237
|
....
gi 490363216 525 LAKK 528
Cdd:COG0488 238 LEQR 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-513 |
3.30e-56 |
|
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: 184.57 E-value: 3.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANtPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQdhatdfevd 399
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 mtvfdwmslwmkpeddeqsvrsvlgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLN 479
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 490363216 480 MALELYQGTLIFVSHDREFVSSLANRIIEITPEK 513
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-229 |
4.36e-44 |
|
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: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQdqfayeeftvldt 84
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimghaelweikqereriyslpemseeeglrvadlevkfgemdgytvesragelllnvgipleqhngpMSevaPGWKLRV 164
Cdd:cd03221 71 --------------------------------------------------------------------LS---GGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGG 229
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-525 |
4.44e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 4.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------SENATIGYYAQDH 392
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 393 ATDFEVDMTVFD--------WMSLWMKP-EDDEQSVRSVLGRL-LfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:COG1121 85 EVDWDFPITVRDvvlmgrygRRGLFRRPsRADREAVDEALERVgL--EDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 463 MDEPTNHLDMESIESLnMAL--ELYQG--TLIFVSHDREFVSSLANRIIEITPEKVtnFQGTYDEFL 525
Cdd:COG1121 163 LDEPFAGVDAATEEAL-YELlrELRREgkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-507 |
2.38e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.50 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAPTSGNVFldpnerlGKLKqdqFAYEEFTVLDTVIMGhAE 91
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIS-------GEVL---LDGRDLLELSEALRG-RR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIKQEreriyslpEMSEEEGLRVADlEVKFG----EMDGYTVESRAGELLLNVGIPLEQHNGPmSEVAPGWKLRVLLA 167
Cdd:COG1123 85 IGMVFQD--------PMTQLNPVTVGD-QIAEAlenlGLSRAEARARVLELLEAVGLERRLDRYP-HQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 168 QALFADPDILLLDEPTNNLD-------IDTIRWLEQtlnERNSTMIIISHDRHFLNMVCTHMADLDYGgltvhpgnydey 240
Cdd:COG1123 155 MALALDPDLLIADEPTTALDvttqaeiLDLLRELQR---ERGTTVLLITHDLGVVAEIADRVVVMDDG------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 241 MLAATQARERLLADNAKKKAqiselqsfVSRFSANASKSRQATSRAKQIekiqltevkassrqnpfirfeqekklfrnaL 320
Cdd:COG1123 220 RIVEDGPPEEILAAPQALAA--------VPRLGAARGRAAPAAAAAEPL------------------------------L 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEAN----TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENAT---- 384
Cdd:COG1123 262 EVRNLSKRYPVRgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltKLSRRSLrelr 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 --IGYYAQDHATDFEVDMTVFDWMSLWMK------PEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:COG1123 342 rrVQMVFQDPYSSLNPRMTVGDIIAEPLRlhgllsRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALAL 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 457 KPNVLIMDEPTNHLDMeSIES--LNMALEL---YQGTLIFVSHDREFVSSLANRII 507
Cdd:COG1123 422 EPKLLILDEPTSALDV-SVQAqiLNLLRDLqreLGLTYLFISHDLAVVRYIADRVA 476
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-507 |
2.64e-35 |
|
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: 132.47 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENA---TIGY 387
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHATDFevDMTVFD--------WMSLWMKP-EDDEQSVRSVLGRLlfsqdDIK----KSVKVLSGGEKGRMLFGKLM 454
Cdd:COG1120 80 VPQEPPAPF--GLTVRElvalgrypHLGLFGRPsAEDREAVEEALERT-----GLEhladRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 455 MQKPNVLIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREFVSSLANRII 507
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDlahqlevLELLRRLA---RERGRTVVMVLHDLNLAARYADRLV 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-223 |
4.10e-33 |
|
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: 126.70 E-value: 4.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE---RLGKL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslsRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDTVIMG---HAELWEI--KQERERIYSLPEMseeegLRVADL-EVKFGEMDGytvesraGELllnvg 143
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrypHLGLFGRpsAEDREAVEEALER-----TGLEHLaDRPVDELSG-------GER----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 144 ipleQhngpmsevapgwklRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDrhfLNM-- 217
Cdd:COG1120 144 ----Q--------------RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNLaa 202
|
....*..
gi 490363216 218 -VCTHMA 223
Cdd:COG1120 203 rYADRLV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-230 |
8.53e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 120.58 E-value: 8.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftvldt 84
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimGHAELWEIKQERERIYSLPEmseeeglrvadlevKFGEMDGYTVEsragELLLnvgipleqhngpMSEvapGWKLRV 164
Cdd:cd03230 61 ---GKDIKKEPEEVKRRIGYLPE--------------EPSLYENLTVR----ENLK------------LSG---GMKQRL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQ---TLNERNSTMIIISHDRHFLNMVCTHMADLDYGGL 230
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-233 |
3.49e-31 |
|
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: 121.12 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD----------PNERLGKLK 70
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkepreARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 71 QDQFAYEEFTVLDtVIMGHAELWEIKqereriyslpemSEEEGLRVADLEVKFGeMDGYtVESRAGELllnvgipleqhn 150
Cdd:COG4555 81 DERGLYDRLTVRE-NIRYFAELYGLF------------DEELKKRIEELIELLG-LEEF-LDRRVGEL------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 151 gpmsevAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQ---TLNERNSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:COG4555 134 ------STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
....*.
gi 490363216 228 GGLTVH 233
Cdd:COG4555 208 GKVVAQ 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-509 |
4.94e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.56 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK------WSENATIGYYAQDHAT 394
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 DFEVDMTVFDW--MSLWMK-------PEDDEQSVRSVLGRL-LFsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMD 464
Cdd:cd03235 80 DRDFPISVRDVvlMGLYGHkglfrrlSKADKAKVDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490363216 465 EPTNHLDMESIESLnMAL--ELYQ-G-TLIFVSHDREFVSSLANRIIEI 509
Cdd:cd03235 158 EPFAGVDPKTQEDI-YELlrELRReGmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-221 |
7.02e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.18 E-value: 7.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERlgKLKQDQFAY----EEF- 79
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--EKERKRIGYvpqrRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 -----TVLDTVIMGhaeLWeikqereriyslPEMSEEEGLRVADlevkfgemdgytvESRAGELLLNVGIpLEQHNGPMS 154
Cdd:cd03235 81 rdfpiSVRDVVLMG---LY------------GHKGLFRRLSKAD-------------KAKVDEALERVGL-SELADRQIG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQtLNERNSTMIIISHDrhfLNMVCTH 221
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHD---LGLVLEY 198
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-221 |
5.10e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLdpNERLGKLKQDQFAY----EEF- 79
Cdd:COG1121 10 ENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL--FGKPPRRARRRIGYvpqrAEVd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 -----TVLDTVIMG---HAELWEI--KQERERIyslpemseEEGLRVADLE----VKFGEMDGytvesraGELllnvgip 145
Cdd:COG1121 88 wdfpiTVRDVVLMGrygRRGLFRRpsRADREAV--------DEALERVGLEdladRPIGELSG-------GQQ------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 146 leQhngpmsevapgwklRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQT---LNERNSTMIIISHDrhfLNMVCTH 221
Cdd:COG1121 146 --Q--------------RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELlreLRREGKTILVVTHD---LGAVREY 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-228 |
5.74e-29 |
|
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: 111.95 E-value: 5.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKqdqfayeeftvldt 84
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLP-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimghaelweIKQERERIYSLPEMSeeeglrvadlevkfgemdgytvesragelllnvgipleqhngpmsevaPGWKLRV 164
Cdd:cd00267 68 ----------LEELRRRIGYVPQLS------------------------------------------------GGQRQRV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQT---LNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELlreLAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
8.35e-29 |
|
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: 113.34 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--PNERLGKLKQDQFAY-- 76
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgePIRDAREDYRRRLAYlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 ------EEFTVLDTVIMgHAELWEIKQERERIyslPEMSEEEGLR-VADLEVKFgemdgytvesragelllnvgipleqh 149
Cdd:COG4133 82 hadglkPELTVRENLRF-WAALYGLRADREAI---DEALEAVGLAgLADLPVRQ-------------------------- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 150 ngpMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNS--TMIII-SHDRHFL 215
Cdd:COG4133 132 ---LSA---GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArgGAVLLtTHQPLEL 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
324-528 |
8.73e-29 |
|
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: 120.04 E-value: 8.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 324 NIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDFEVD---- 399
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTvren 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 -----------MTVFDWMSLWM-KPEDDEQSVRSVLGRLlfsQDDIK------------------------KSVKVLSGG 443
Cdd:TIGR03719 89 veegvaeikdaLDRFNEISAKYaEPDADFDKLAAEQAEL---QEIIDaadawdldsqleiamdalrcppwdADVTKLSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 444 EKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDE 523
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 245
|
....*
gi 490363216 524 FLAKK 528
Cdd:TIGR03719 246 WLEQK 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-228 |
9.51e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.01 E-value: 9.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD----------PNERLGKLKQDQF 74
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 75 AYEEFTVLDTVIMgHAELWEI--KQERERIYSLpemseeegLRVADLEVKFGEmdgytvesRAGELLLnvgipleqhngp 152
Cdd:COG1131 84 LYPDLTVRENLRF-FARLYGLprKEARERIDEL--------LELFGLTDAADR--------KVGTLSG------------ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 153 msevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQ---TLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:COG1131 135 ------GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEllrELAAEGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-528 |
1.03e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 120.44 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 324 NIAKGYEA--NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDfeVDMT 401
Cdd:PRK11147 5 SIHGAWLSfsDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRN--VEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 402 VFDWMS---------------LWMKPEDD------------------------EQSVRSVLGRLLFSQDdikKSVKVLSG 442
Cdd:PRK11147 83 VYDFVAegieeqaeylkryhdISHLVETDpseknlnelaklqeqldhhnlwqlENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 443 GEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYD 522
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
....*.
gi 490363216 523 EFLAKK 528
Cdd:PRK11147 240 QYLLEK 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-509 |
2.29e-28 |
|
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: 110.95 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-----SENAT-----IGYYA 389
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdiKKEPEevkrrIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDhatdfevdMTVFDWMSlwmkpeddeqsVRSVLgrllfsqddikksvkVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNH 469
Cdd:cd03230 80 EE--------PSLYENLT-----------VRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490363216 470 LDMESIESL-NMALELYQ--GTLIFVSHDREFVSSLANRIIEI 509
Cdd:cd03230 126 LDPESRREFwELLRELKKegKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-509 |
7.02e-28 |
|
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: 110.63 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYE-ANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT-----------IGYY 388
Cdd:cd03225 1 ELKNLSFSYPdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQDHATDFeVDMTVFDWMSLWMK-----PEDDEQSVRSVLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIM 463
Cdd:cd03225 81 FQNPDDQF-FGPTVEEEVAFGLEnlglpEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 464 DEPTNHLDMESIESLnMAL--ELYQG--TLIFVSHDREFVSSLANRIIEI 509
Cdd:cd03225 159 DEPTAGLDPAGRREL-LELlkKLKAEgkTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-228 |
8.81e-28 |
|
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: 110.63 E-value: 8.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAYEEFTVL---DTVIMG 88
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELRRKVGLVFqnpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 89 HaelweikqereriyslpemseeeglRVADlEVKFG----EMDGYTVESRAGELLLNVGI-PLEQHngPMSEVAPGWKLR 163
Cdd:cd03225 91 P-------------------------TVEE-EVAFGlenlGLPEEEIEERVEEALELVGLeGLRDR--SPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQ---TLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-511 |
1.94e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.52 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQD-------- 391
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvayv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 392 HATDFEVDMTVFDWMSLWM---KPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTN 468
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFqlrERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490363216 469 HLDMESIESLNMALELY----QGTLIFVSHDREFVSSLANRIIEITP 511
Cdd:COG4619 160 ALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-528 |
3.43e-27 |
|
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: 109.34 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATD---- 395
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 396 FE------VDMTVFD-----WMSLWMKPEDDEQSVRSVLGRLlfsqdDI----KKSVKVLSGGEKGRM-LFGKLMMQkPN 459
Cdd:COG1122 81 FQnpddqlFAPTVEEdvafgPENLGLPREEIRERVEEALELV-----GLehlaDRPPHELSGGQKQRVaIAGVLAME-PE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 460 VLIMDEPTNHLDMESIESL-NMALELYQG--TLIFVSHDREFVSSLANRIIEITPEKVTnFQGTYDEFLAKK 528
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELlELLKRLNKEgkTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-507 |
8.66e-27 |
|
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: 107.73 E-value: 8.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEN--------ATIGYYAQDH 392
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 393 ATDFEVDmTVFDWMSLWMKP-EDDEQSVRSVLGRL-LFSQDDikKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHL 470
Cdd:cd03226 81 DYQLFTD-SVREELLLGLKElDAGNEQAETVLKDLdLYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 471 DMESIESL-NMALELY-QGTLIFV-SHDREFVSSLANRII 507
Cdd:cd03226 158 DYKNMERVgELIRELAaQGKAVIViTHDYEFLAKVCDRVL 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-507 |
1.29e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.84 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK------WSENAT----IGYYA 389
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHAtdFEVDMTVFDWMSLW-----MKPEDDEQSVRSVLGRL-LfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIM 463
Cdd:COG1131 80 QEPA--LYPDLTVRENLRFFarlygLPRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490363216 464 DEPTNHLDMESIESL-NMALELYQG--TLIFVSHDREFVSSLANRII 507
Cdd:COG1131 156 DEPTSGLDPEARRELwELLRELAAEgkTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-240 |
2.16e-26 |
|
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: 112.72 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGnvfldpnerlgklkqdqfayeEFTVLDT 84
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG---------------------TIEIGET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAElweikQERERIYSLPEMSEE--EGLRVADLevkfgemDGYTVESRAGELLLNVGIPLEQHNgpMSEVAPGWKL 162
Cdd:TIGR03719 385 VKLAYVD-----QSRDALDPNKTVWEEisGGLDIIKL-------GKREIPSRAYVGRFNFKGSDQQKK--VGQLSGGERN 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMadLDYGG---LTVHPGNYDE 239
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFEGdshVEWFEGNFSE 528
|
.
gi 490363216 240 Y 240
Cdd:TIGR03719 529 Y 529
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-228 |
2.43e-26 |
|
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: 107.03 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD----PNERLGKLKQ----------DQFAYE 77
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRkvglvfqnpdDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 78 efTVLDTVIMGhaelweikqereriyslPE---MSEEEglrvadlevkfgemdgytVESRAGELLLNVGI-PLEQHNgpm 153
Cdd:COG1122 92 --TVEEDVAFG-----------------PEnlgLPREE------------------IRERVEEALELVGLeHLADRP--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 154 sevaP-----GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQT---LNERNSTMIIISHDRHFLNMVCTHMADL 225
Cdd:COG1122 132 ----PhelsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
...
gi 490363216 226 DYG 228
Cdd:COG1122 208 DDG 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
327-528 |
2.45e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 112.52 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 327 KGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDfeVDMTV---- 402
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLD--PEKTVrenv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 403 -------------FDWMSLWM-KPEDDEQSVRSVLGRLlfsQDDIK------------------------KSVKVLSGGE 444
Cdd:PRK11819 92 eegvaevkaaldrFNEIYAAYaEPDADFDALAAEQGEL---QEIIDaadawdldsqleiamdalrcppwdAKVTKLSGGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGTYDEF 524
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW 248
|
....
gi 490363216 525 LAKK 528
Cdd:PRK11819 249 LEQK 252
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
269-530 |
4.71e-26 |
|
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: 112.62 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 269 VSRFSANASKSRQATSRAKQIEKIQLTEVKASSRQNPFIRFEqekklFRNALEVENIAKGY-EANTPLFKDVNMMLEVGE 347
Cdd:COG2274 428 VAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-----LKGDIELENVSFRYpGDSPPVLDNISLTIKPGE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 348 KVAILGTNGVGKSTMIKTLVGELTPDNGRVK-------------WSENatIGYYAQDhatDFEVDMTVFDWMSLWMKPED 414
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpasLRRQ--IGVVLQD---VFLFSGTIRENITLGDPDAT 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 415 DEQsVRSVLgRLLFSQDDIKK-----------SVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES----IESLN 479
Cdd:COG2274 578 DEE-IIEAA-RLAGLHDFIEAlpmgydtvvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLR 655
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 480 malELYQG-TLIFVSHDREFVsSLANRIIEITPEKVTNfQGTYDEFLAKKGI 530
Cdd:COG2274 656 ---RLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHEELLARKGL 702
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
336-468 |
5.32e-26 |
|
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: 103.50 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 336 FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-----------SENATIGYYAQDHAtdFEVDMTVFD 404
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 405 ------WMSLWMKPEDDEQ--SVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTN 468
Cdd:pfam00005 79 nlrlglLLKGLSKREKDARaeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-505 |
1.33e-25 |
|
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: 110.28 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLAPTSGNVF--LDPNERLGKLKQDQFAYEEFTV 81
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhVALCEKCGYVERPSKVGEPCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 L-DTVIMGHAELW-----EIKQERERIYSLPE----MSEEEglRVADLEVKFGEMDGYTVES---RAGELLLNVGIpleQ 148
Cdd:TIGR03269 85 CgGTLEPEEVDFWnlsdkLRRRIRKRIAIMLQrtfaLYGDD--TVLDNVLEALEEIGYEGKEavgRAVDLIEMVQL---S 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 149 HNgpMSEVAP----GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRW----LEQTLNERNSTMIIISHDRHFLNMVCT 220
Cdd:TIGR03269 160 HR--ITHIARdlsgGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 221 HMADLDYGGLtVHPGNYDEymlaatqarerlladnakkkaqiselqsFVSRFSANASKSRQATSrakqiekiqltevkas 300
Cdd:TIGR03269 238 KAIWLENGEI-KEEGTPDE----------------------------VVAVFMEGVSEVEKECE---------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 301 srqnpfirFEQEKKLFRnaleVENIAKGY-EANTPLFKDV-NMMLEV--GEKVAILGTNGVGKSTMIKTLVGELTPDNGR 376
Cdd:TIGR03269 273 --------VEVGEPIIK----VRNVSKRYiSVDRGVVKAVdNVSLEVkeGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 377 V------KWSENATIGYYAQDHATDF------EVDM----TVFDWMSLWMKPE-DDEQSVRSVLGRLLFSQDDIKKSVKV 439
Cdd:TIGR03269 341 VnvrvgdEWVDMTKPGPDGRGRAKRYigilhqEYDLyphrTVLDNLTEAIGLElPDELARMKAVITLKMVGFDEEKAEEI 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 440 L-------SGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD-------MESIesLNMALELYQgTLIFVSHDREFVSSLANR 505
Cdd:TIGR03269 421 LdkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSI--LKAREEMEQ-TFIIVSHDMDFVLDVCDR 497
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-529 |
2.07e-25 |
|
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: 104.94 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANtPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS--ENATIGYYAQDHATDFE 397
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgeDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 398 VDMTVFDWMSLW-----------MKPEDDEQSVRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEP 466
Cdd:COG4555 81 DERGLYDRLTVReniryfaelygLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 467 TNHLDMESIESL-NMALELYQ--GTLIFVSHDREFVSSLANRIIeITPEKVTNFQGTYDEFLAKKG 529
Cdd:COG4555 160 TNGLDVMARRLLrEILRALKKegKTVLFSSHIMQEVEALCDRVV-ILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-509 |
2.55e-25 |
|
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: 101.94 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEANtPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATigyyaqdhatdfevdm 400
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 401 tvfdwmslwmkPEDDEQSVRSVLGRLlfSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESL-N 479
Cdd:cd00267 64 -----------AKLPLEELRRRIGYV--PQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlE 121
|
170 180 190
....*....|....*....|....*....|..
gi 490363216 480 MALELYQG--TLIFVSHDREFVSSLANRIIEI 509
Cdd:cd00267 122 LLRELAEEgrTVIIVTHDPELAELAADRVIVL 153
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-230 |
3.24e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 103.36 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKlkqdqfAYEEFtvldtv 85
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-----GK------PLSAM------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 imgHAELWeikqeRERIYSLPEMSEEEGLRVAD-LEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGWKLRV 164
Cdd:COG4619 68 ---PPPEW-----RRQVAYVPQEPALWGGTVRDnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGL 230
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-524 |
3.41e-25 |
|
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: 104.19 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT--------------I 385
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQDHATdfeVD-MTVFD------------WMSLW-MKPEDDEQSVRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFG 451
Cdd:cd03256 81 GMIFQQFNL---IErLSVLEnvlsgrlgrrstWRSLFgLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 452 KLMMQKPNVLIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLANRIIEITPEKVTnFQGTYDEF 524
Cdd:cd03256 157 RALMQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGLKDGRIV-FDGPPAEL 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-230 |
3.94e-25 |
|
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: 103.07 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKLKQDQfaYEEFTVLDT 84
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD-----GKSYQKN--IEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAelweikqererIYslPEMSEEEGLRVADLEVKFGEmdgytveSRAGELLLNVGipLEQHNG-PMSEVAPGWKLR 163
Cdd:cd03268 77 LIEAPG-----------FY--PNLTARENLRLLARLLGIRK-------KRIDEVLDVVG--LKDSAKkKVKGFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQT---LNERNSTMIIISHDRHFLNMVCTHMADLDYGGL 230
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
9.03e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 103.24 E-value: 9.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLIS-NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNvfldpnerlgklkqdqfayeEF 79
Cdd:COG1119 2 PLLElRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN--------------------DV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 TVLDTViMGHAELWEIKQereRI-YSLPEMSEE--EGLRVAD-----------LEVKFGEMDgytvESRAGELLLNVGI- 144
Cdd:COG1119 62 RLFGER-RGGEDVWELRK---RIgLVSPALQLRfpRDETVLDvvlsgffdsigLYREPTDEQ----RERARELLELLGLa 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 145 PLEQHN-GPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISH 210
Cdd:COG1119 134 HLADRPfGTLSQ---GEQRRVLIARALVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-228 |
2.66e-24 |
|
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: 101.36 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFA---------- 75
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigrtfqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 ---YEEFTVLDTVIMGHAElweikQERERIYSLPEMSEEEGLRvadlevkfgemdgytveSRAGELLLNVGIPlEQHNGP 152
Cdd:cd03219 84 prlFPELTVLENVMVAAQA-----RTGSGLLLARARREEREAR-----------------ERAEELLERVGLA-DLADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 153 MSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQtLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPeeteELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-509 |
3.18e-24 |
|
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: 100.64 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEAN---TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSE------- 381
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 382 NATIGYYAQDHAtdFEVDMTVFDWMSLWM-----KPEDDEQSVRSVLGRL-LfsQDDIKKSVKVLSGGEKGRMLFGKLMM 455
Cdd:cd03255 81 RRHIGFVFQSFN--LLPDLTALENVELPLllagvPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 456 QKPNVLIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREFVsSLANRIIEI 509
Cdd:cd03255 157 NDPKIILADEPTGNLDsetgkevMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-507 |
5.24e-24 |
|
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: 98.83 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENA---TIGY 387
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQdhatdfevdmtvfdwmslwmkpeDDEqsvrsvlgrlLFS---QDDIkksvkvLSGGEKGRMLFGKLMMQKPNVLIMD 464
Cdd:cd03246 81 LPQ-----------------------DDE----------LFSgsiAENI------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 465 EPTNHLDMESIESLNMA---LELYQGTLIFVSHDREFVSSlANRII 507
Cdd:cd03246 122 EPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLAS-ADRIL 166
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-507 |
5.51e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 98.66 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENA---TIGYYA 389
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaSLSPKElarKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QdhATDfEVDMTVFdwmslwmkpeddeqsvrsvlgrllfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNH 469
Cdd:cd03214 80 Q--ALE-LLGLAHL-----------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490363216 470 LD-------MESIESLNmalELYQGTLIFVSHDREFVSSLANRII 507
Cdd:cd03214 128 LDiahqielLELLRRLA---RERGKTVVMVLHDLNLAARYADRVI 169
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
9.39e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 9.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 11 FGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQ-----DQFAyeeFTVLDTV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLP---LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 IMGhaeLWeikqeRERIYSLPemseeegLRVADlevkfgemdgytvESRAGELLLNVGIpLEQHNGPMSEVAPGWKLRVL 165
Cdd:NF040873 79 AMG---RW-----ARRGLWRR-------LTRDD-------------RAAVDDALERVGL-ADLAGRQLGELSGGQRQRAL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE---RNSTMIIISHDRH 213
Cdd:NF040873 130 LAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEehaRGATVVVVTHDLE 180
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-231 |
1.65e-23 |
|
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: 97.51 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAyEEFTVLDT 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKELA-RKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VImghaELWEIKQERERIYSlpEMSeeeglrvadlevkfgemdgytvesrAGELllnvgipleQhngpmsevapgwklRV 164
Cdd:cd03214 81 AL----ELLGLAHLADRPFN--ELS-------------------------GGER---------Q--------------RV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDrhfLNMV---CTHMADLDYGGLT 231
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNLAaryADRVILLKDGRIV 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-212 |
4.15e-23 |
|
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: 97.56 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGS----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNERLGKLKQDQ 73
Cdd:cd03255 4 KNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFRRRH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 74 FAY--------EEFTVLDTVimghaelweikqereriySLPEMseeeglrvadlevkFGEMDGYTVESRAGELLLNVGIP 145
Cdd:cd03255 84 IGFvfqsfnllPDLTALENV------------------ELPLL--------------LAGVPKKERRERAEELLERVGLG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 146 LEQHNGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHDR 212
Cdd:cd03255 132 DRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
8.27e-23 |
|
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: 92.25 E-value: 8.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 223 ADLDYGGLTVHPGNYDEYMLAATQARERLLADNAKKKAQISELQSFVSRFSANASKSRQATSRAKQIEKIQltEVKASSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKME--RIEKPER 78
|
....*..
gi 490363216 303 QNPFIRF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-259 |
8.35e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.73 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGnvfldpnerlgklkqdqfayeEFTVLDT 84
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG---------------------TIKIGET 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAElweikQERERIysLPEMS--EE--EGLRVadleVKFGemdGYTVESRAGELLLNVGIPLEQHngPMSEVAPGW 160
Cdd:PRK11819 387 VKLAYVD-----QSRDAL--DPNKTvwEEisGGLDI----IKVG---NREIPSRAYVGRFNFKGGDQQK--KVGVLSGGE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMadLDYGG---LTVHPGNY 237
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFEGdsqVEWFEGNF 528
|
250 260
....*....|....*....|..
gi 490363216 238 DEYmlaATQARERLLADNAKKK 259
Cdd:PRK11819 529 QEY---EEDKKRRLGADAARPH 547
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-507 |
1.91e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 101.04 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNVFLDPN-----ERL-GKLKQDQFA--------------YEEFT--VLD-TVIm 87
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlKRFrGTELQNYFKklyngeikvvhkpqYVDLIpkVFKgKVR- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 88 ghaELWEIKQERERiysLPEMSEEEGLRVAdLEVKFGEMDGytvesraGELllnvgipleQhngpmsevapgwklRVLLA 167
Cdd:PRK13409 182 ---ELLKKVDERGK---LDEVVERLGLENI-LDRDISELSG-------GEL---------Q--------------RVAIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 168 QALFADPDILLLDEPTNNLDI-------DTIRWLEQtlnerNSTMIIISHDrhflnmvcthMADLDYGGLTVH-----PG 235
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHD----------LAVLDYLADNVHiaygePG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 236 NYDeymlAATQARERLLADNAKKKAQISElqsfvsrfsanasksrqatsrakqiEKIQLtevkassRQNPfIRFE----Q 311
Cdd:PRK13409 290 AYG----VVSKPKGVRVGINEYLKGYLPE-------------------------ENMRI-------RPEP-IEFEerppR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 312 EKKLFRNALEVENIAKGYEAntplFKdvnmmLEV-------GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEnaT 384
Cdd:PRK13409 333 DESERETLVEYPDLTKKLGD----FS-----LEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--K 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQDHATDFevDMTVFDWM--------SLWMKPEDDEqsvRSVLGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:PRK13409 402 ISYKPQYIKPDY--DGTVEDLLrsitddlgSSYYKSEIIK---PLQLERLL------DKNVKDLSGGELQRVAIAACLSR 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 457 KPNVLIMDEPTNHLDMEsiESLNMA------LELYQGTLIFVSHDREFVSSLANRII 507
Cdd:PRK13409 471 DADLYLLDEPSAHLDVE--QRLAVAkairriAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-507 |
1.99e-22 |
|
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: 101.01 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNerlgklkqdqfaYEEftVLD----TvimghaelwEIKQERERIYslp 106
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPS------------WDE--VLKrfrgT---------ELQDYFKKLA--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 107 emseEEGLRVA------DLEVKFgemdgytVESRAGELL---------------LNVGIPLEQHNGPMSevapGWKL-RV 164
Cdd:COG1245 157 ----NGEIKVAhkpqyvDLIPKV-------FKGTVRELLekvdergkldelaekLGLENILDRDISELS----GGELqRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDI-------DTIRwleqTLNERNSTMIIISHDrhflnmvcthMADLDYGGLTVH---- 233
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDIyqrlnvaRLIR----ELAEEGKYVLVVEHD----------LAILDYLADYVHilyg 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 234 -PGNYDeymlAATQARerlladnaKKKAQISE-LQSFVS----RFsanasksrqatsRAKQIEkiqlTEVKASSRqnpfi 307
Cdd:COG1245 288 ePGVYG----VVSKPK--------SVRVGINQyLDGYLPeenvRI------------RDEPIE----FEVHAPRR----- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 308 rFEQEKKLfrnaLEVENIAKGYEAntplFKdvnmmLEV-------GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwS 380
Cdd:COG1245 335 -EKEEETL----VEYPDLTKSYGG----FS-----LEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--D 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 381 ENATIGYYAQDHATDFevDMTVFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 460
Cdd:COG1245 399 EDLKISYKPQYISPDY--DGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 461 LIMDEPTNHLDMEsiESLNMA------LELYQGTLIFVSHDREFVSSLANRII 507
Cdd:COG1245 477 YLLDEPSAHLDVE--QRLAVAkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
293-529 |
2.08e-22 |
|
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: 100.61 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 293 QLTEVKASSR-------QNPFIRFEQEKKLF--RNALEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTM 362
Cdd:COG4987 298 HLGRVRAAARrlnelldAPPAVTEPAEPAPApgGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 363 IKTLVGELTPDNGRVK--------WSENA---TIGYYAQDHATdFevDMTVFDwmSLWM-KPEDDEQSVRSV-----LGR 425
Cdd:COG4987 378 LALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIAVVPQRPHL-F--DTTLRE--NLRLaRPDATDEELWAAlervgLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 426 LLFSQDD----------IKksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLnMA--LELYQG-TLIFV 492
Cdd:COG4987 453 WLAALPDgldtwlgeggRR-----LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL-LAdlLEALAGrTVLLI 526
|
250 260 270
....*....|....*....|....*....|....*..
gi 490363216 493 SHDREFVsSLANRIIEITPEKVTnFQGTYDEFLAKKG 529
Cdd:COG4987 527 THRLAGL-ERMDRILVLEDGRIV-EQGTHEELLAQNG 561
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-526 |
2.35e-22 |
|
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: 95.65 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK-----WSENATIGYYA----- 389
Cdd:cd03261 1 IELRGLTKSFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSEAELYRlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 ----QDHATdFEvDMTVFDWMSLWMK-----PEDD-EQSVRSVLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPN 459
Cdd:cd03261 80 gmlfQSGAL-FD-SLTVFENVAFPLRehtrlSEEEiREIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 460 VLIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLANRIIEITPEKVTnFQGTYDEFLA 526
Cdd:cd03261 157 LLLYDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRA 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
332-512 |
2.63e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.92 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTP--DN-----GRVKWSEN-----ATIGYYAQDHATDFEVD 399
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtyGNdvrlfGERRGGEDvwelrKRIGLVSPALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 MTV--------FDWMSLWMKPED-DEQSVRSVLGRL-LfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNH 469
Cdd:COG1119 95 ETVldvvlsgfFDSIGLYREPTDeQRERARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490363216 470 LDMESIESLNMALELY--QG--TLIFVSHDREfvsslanriiEITPE 512
Cdd:COG1119 173 LDLGARELLLALLDKLaaEGapTLVLVTHHVE----------EIPPG 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-509 |
7.30e-22 |
|
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: 92.45 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEAN-TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsenatigyyaqdhatdfev 398
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 dmtvfDWMSLwmkPEDDEQSVRSVLGrlLFSQDDI--KKSVK--VLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES 474
Cdd:cd03228 62 -----DGVDL---RDLDLESLRKNIA--YVPQDPFlfSGTIRenILSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 490363216 475 IESLNMAL-ELYQG-TLIFVSHDREFVsSLANRIIEI 509
Cdd:cd03228 132 EALILEALrALAKGkTVIVIAHRLSTI-RDADRIIVL 167
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-239 |
9.08e-22 |
|
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: 94.11 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQD------------ 72
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAelyrlrrrmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 73 -QFA--YEEFTVLDTVimghaelweikqereriySLP-----EMSEEEglrvadlevkfgemdgytVESRAGELLLNVGI 144
Cdd:cd03261 83 fQSGalFDSLTVFENV------------------AFPlrehtRLSEEE------------------IREIVLEKLEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 145 PLEQHNGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQTLnerNSTMIIISHDRHFLNM 217
Cdd:cd03261 127 RGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL---GLTSIMVTHDLDTAFA 202
|
250 260
....*....|....*....|..
gi 490363216 218 VCTHMADLdYGGLTVHPGNYDE 239
Cdd:cd03261 203 IADRIAVL-YDGKIVAEGTPEE 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
9.99e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 94.72 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGS-KPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFA---- 75
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 ---------YEEFTVLDTVIMGHaelweikQERERIYSLPEMSEEEGLRVADLEvkfgemdgytVESRAGELLLNVGIpL 146
Cdd:COG0411 82 artfqnprlFPELTVLENVLVAA-------HARLGRGLLAALLRLPRARREERE----------ARERAEELLERVGL-A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 147 EQHNGPMSEVAPGWKLRVLLAQALFADPDILLLDEP--------TNNLdIDTIRWLEQtlnERNSTMIIISHDRHFLNMV 218
Cdd:COG0411 144 DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLRD---ERGITILLIEHDMDLVMGL 219
|
250
....*....|
gi 490363216 219 CTHMADLDYG 228
Cdd:COG0411 220 ADRIVVLDFG 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
1.12e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE---RLGKL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwsPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQD---QFAyeeFTVLDTVIMGHAELWEIKQERERIYslpemseEEGLRVADLEvKFGEMDgYTVESrAGElllnvgipl 146
Cdd:PRK13548 82 PQHsslSFP---FTVEEVVAMGRAPHGLSRAEDDALV-------AAALAQVDLA-HLAGRD-YPQLS-GGE--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 147 eqhngpmsevapgwKLRVLLAQAL------FADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDrhfLN 216
Cdd:PRK13548 140 --------------QQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---LN 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
319-529 |
1.13e-21 |
|
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: 98.29 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK-------------WSENatI 385
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdldpasWRRQ--I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQdHATDFEvdMTVFDWMSLWmKPEDDEQSVRSVLGR-----LLFSQDD-----IKKSVKVLSGGEKGRMLFGKLMM 455
Cdd:COG4988 414 AWVPQ-NPYLFA--GTIRENLRLG-RPDASDEELEAALEAagldeFVAALPDgldtpLGEGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 456 QKPNVLIMDEPTNHLDMESIESLNMAL-ELYQG-TLIFVSHDREFVsSLANRIIEITPEKVTNfQGTYDEFLAKKG 529
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALrRLAKGrTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKNG 563
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-507 |
1.30e-21 |
|
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: 92.25 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS-------------ENATIG 386
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQDHAtdfevdmtVFDWMSlwmkpeddeqsvrsVLGRLLFSqddikksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEP 466
Cdd:cd03229 80 MVFQDFA--------LFPHLT--------------VLENIALG----------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490363216 467 TNHLDMESIESLNMAL----ELYQGTLIFVSHDREFVSSLANRII 507
Cdd:cd03229 128 TSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVV 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-507 |
1.64e-21 |
|
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: 92.97 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENAT----------IGYYA 389
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDvtgvpperrnIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHAtdfevdmtVFDWMSLW-----------MKPEDDEQSVRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKP 458
Cdd:cd03259 79 QDYA--------LFPHLTVAeniafglklrgVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 459 NVLIMDEPTNHLDMESIESLNMALELYQG----TLIFVSHDREFVSSLANRII 507
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-501 |
2.46e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 328 GYEANtPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDFEVDMTVFDWMS 407
Cdd:NF040873 1 GYGGR-PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 408 L--------WMKPE-DDEQSVRSVLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESL 478
Cdd:NF040873 80 MgrwarrglWRRLTrDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*.
gi 490363216 479 N--MALELYQG-TLIFVSHDREFVSS 501
Cdd:NF040873 159 IalLAEEHARGaTVVVVTHDLELVRR 184
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-241 |
2.79e-21 |
|
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: 97.60 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE---RLGKLKQDQFAYEEfT 80
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDgidlrqidPASlrrQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDTVIMGHaelweikqereriyslPEMSEEEGLRVADL-----EVKfgEM-DGYtvESRAGELllnvGIPLeqhngpmS 154
Cdd:COG2274 565 IRENITLGD----------------PDATDEEIIEAARLaglhdFIE--ALpMGY--DTVVGEG----GSNL-------S 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 155 EvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFLNmvcthMAD----LDYG 228
Cdd:COG2274 614 G---GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIR-----LADriivLDKG 685
|
250
....*....|...
gi 490363216 229 GLtVHPGNYDEYM 241
Cdd:COG2274 686 RI-VEDGTHEELL 697
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
5.76e-21 |
|
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: 92.17 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD----PNERLGKLKQD 72
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 73 -QFAYEE--------FTVLDTVimghaelweikqereriyslpemseEEGLRVAdlevkfGEMDgytVESRAGELLLNVG 143
Cdd:COG1124 81 vQMVFQDpyaslhprHTVDRIL-------------------------AEPLRIH------GLPD---REERIAELLEQVG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 144 IPLEQHNGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHDRHflnmVC 219
Cdd:COG1124 127 LPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLA----VV 202
|
....*
gi 490363216 220 THMAD 224
Cdd:COG1124 203 AHLCD 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
1.49e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.11 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAY--- 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 ------EEF------TVLDTVimghaelweikqereriySLPemseeegLRVAdlevkfgEMDGYTVESRAGELLLNVGI 144
Cdd:COG2884 80 rigvvfQDFrllpdrTVYENV------------------ALP-------LRVT-------GKSRKEIRRRVREVLDLVGL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 145 pLEQHNGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQtLNERNSTMIIISHDRHFLN 216
Cdd:COG2884 128 -SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETsweiMELLEE-INRRGTTVLIATHDLELVD 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-231 |
1.51e-20 |
|
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: 89.94 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGnRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNE---RLGKLKQDQFA 75
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqPQKlrrRIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTV---LDTVimghAELWEIKQERERiyslpemseeeglrvadlevkfgemdgytveSRAGELLLNVGipLEQH-NG 151
Cdd:cd03264 84 YPNFTVrefLDYI----AWLKGIPSKEVK-------------------------------ARVDEVLELVN--LGDRaKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 152 PMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDID---TIRWLEQTLNErNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEeriRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
...
gi 490363216 229 GLT 231
Cdd:cd03264 206 KLV 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-467 |
3.27e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE--RLGklkqdqfa 75
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrfrsPRDaqAAG-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 yeeftvldtVIMGHAELweikqereriySL-PEMSEEEGLRVADLEVKFGEMDGYTVESRAGELL--LNVGIPLEQhngP 152
Cdd:COG1129 81 ---------IAIIHQEL-----------NLvPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLarLGLDIDPDT---P 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 153 MSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqTLNERNSTMIIIShdrHFLN--------- 216
Cdd:COG1129 138 VGDLSVAQQQLVEIARALSRDARVLILDEPTASLTereverlFRIIR----RLKAQGVAIIYIS---HRLDevfeiadrv 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 217 -------MVCTH-MADLDYGGLTvhpgnydEYMLaatqARErlLADNAKKKAQiselqsfvsrfsanasksrqatsrakq 288
Cdd:COG1129 211 tvlrdgrLVGTGpVAELTEDELV-------RLMV----GRE--LEDLFPKRAA--------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 289 iekiQLTEVkassrqnpfirfeqekklfrnALEVENIAKGyeantPLFKDVNmmLEV--GEKVAILGTNGVGKSTMIKTL 366
Cdd:COG1129 251 ----APGEV---------------------VLEVEGLSVG-----GVVRDVS--FSVraGEILGIAGLVGAGRTELARAL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 367 VGELTPDNGRVKWSENAT------------IGYYAQDHATD--FeVDMTVFDWMSL----------WMKPEDDEQSVRSV 422
Cdd:COG1129 299 FGADPADSGEIRLDGKPVrirsprdairagIAYVPEDRKGEglV-LDLSIRENITLasldrlsrggLLDRRRERALAEEY 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 490363216 423 LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:COG1129 378 IKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-506 |
3.50e-20 |
|
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: 88.85 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDH--ATDFE 397
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRdiAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 398 -----VDMTVFDWMSLWMK----PEDD-EQSVRSVlGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:cd03301 80 nyalyPHMTVYDNIAFGLKlrkvPKDEiDERVREV-AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 468 NHLD------MES-IESLNMALelyQGTLIFVSHDREFVSSLANRI 506
Cdd:cd03301 159 SNLDaklrvqMRAeLKRLQQRL---GTTTIYVTHDQVEAMTMADRI 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-509 |
4.03e-20 |
|
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: 89.86 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEA---NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-----------SENAT 384
Cdd:COG1124 1 MLEVRNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQDHATDFEVDMTVFDWMS--LW-MKPEDDEQSVRSVL------GRLLF---SQddikksvkvLSGGEKGRMLFGK 452
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILAepLRiHGLPDREERIAELLeqvglpPSFLDrypHQ---------LSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 453 LMMQKPNVLIMDEPTNHLDMeSI--ESLNMALEL---YQGTLIFVSHDREFVSSLANRIIEI 509
Cdd:COG1124 152 ALILEPELLLLDEPTSALDV-SVqaEILNLLKDLreeRGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-506 |
5.01e-20 |
|
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: 89.32 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS---------ENATIGYYAQ 390
Cdd:cd03299 1 LKVENLSKDW--KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHATdFEvDMTVFD------WMSLWMKPEDDEQsVRSVLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMD 464
Cdd:cd03299 79 NYAL-FP-HMTVYKniayglKKRKVDKKEIERK-VLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 465 EPTNHLDMES----IESLNMALELYQGTLIFVSHDREFVSSLANRI 506
Cdd:cd03299 155 EPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
7.61e-20 |
|
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: 87.96 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftv 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 lDTVIMGHAElweikqERERI------YSL-PEMSEEE----GLRVadlevkfGEMDGYTVESRAGELLLNVGIPLEQHN 150
Cdd:cd03259 61 -GRDVTGVPP------ERRNIgmvfqdYALfPHLTVAEniafGLKL-------RGVPKAEIRARVRELLELVGLEGLLNR 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 151 GPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDtIRW-----LEQTLNERNSTMIIISHDR 212
Cdd:cd03259 127 YP-HELSGGQQQRVALARALAREPSLLLLDEPLSALDAK-LREelreeLKELQRELGITTIYVTHDQ 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
7.95e-20 |
|
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: 88.03 E-value: 7.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE---RLGKLKQDQFAYEEfTVLDTVI 86
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPADlrrNIGYVPQDVTLFYG-TLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 87 MGHaelweikqereriyslPEMSEEEGLRVAdlevKFGEMDGYTVESRAGeLLLNVGiplEQHNGpmseVAPGWKLRVLL 166
Cdd:cd03245 100 LGA----------------PLADDERILRAA----ELAGVTDFVNKHPNG-LDLQIG---ERGRG----LSGGQRQAVAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 167 AQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFLNMV 218
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSLLDLV 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-519 |
1.04e-19 |
|
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: 87.63 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGeKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSE----------NATIGYYA 389
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHatDFEVDMTVFDWM--SLWMK---PEDDEQSVRSVLGRL-LFsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIM 463
Cdd:cd03264 79 QEF--GVYPNFTVREFLdyIAWLKgipSKEVKARVDEVLELVnLG--DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 464 DEPTNHLDMES-IESLNMALELYQGTLIFVS-HDREFVSSLANRIIEITPEKVTnFQG 519
Cdd:cd03264 155 DEPTAGLDPEErIRFRNLLSELGEDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-228 |
1.11e-19 |
|
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: 87.34 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAYeeftvldt 84
Cdd:cd03269 4 ENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-GKPLDIAARNRIGY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimghaelweikqereriysLPEmseEEGL----RVADLEVKFGEMDGYTVE---SRAGELLLNVGIPlEQHNGPMSEVA 157
Cdd:cd03269 75 --------------------LPE---ERGLypkmKVIDQLVYLAQLKGLKKEearRRIDEWLERLELS-EYANKRVEELS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 158 PGWKLRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-526 |
1.28e-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: 91.89 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANT-PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGeLTPDNGRV------------KWSEN--- 382
Cdd:COG1123 4 LLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgevlldgrdllELSEAlrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 383 ATIGYYAQDHATDFeVDMTVFDWMS-----LWMKPEDDEQSVRSVLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQK 457
Cdd:COG1123 83 RRIGMVFQDPMTQL-NPVTVGDQIAealenLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 458 PNVLIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLANRIIEITPEKVTnFQGTYDEFLA 526
Cdd:COG1123 161 PDLLIADEPTTALDvttqaeiLDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVMDDGRIV-EDGPPEEILA 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-507 |
1.31e-19 |
|
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: 87.34 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENA-------TIGYYAQDH 392
Cdd:cd03269 1 LEVENVTKRFGRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 393 AtdFEVDMTVFDWM----SLW-MKPEDDEQSVRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:cd03269 80 G--LYPKMKVIDQLvylaQLKgLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490363216 468 NHLDMESIESLNMALELYQG---TLIFVSHDREFVSSLANRII 507
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVL 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-223 |
1.34e-19 |
|
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: 88.11 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQD------------- 72
Cdd:COG1127 10 NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKelyelrrrigmlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 73 QFA--YEEFTVLDTVIMGhaeLweikqeRERiyslPEMSEEEglrvadlevkfgemdgytVESRAGELLLNVGipLEQHN 150
Cdd:COG1127 89 QGGalFDSLTVFENVAFP---L------REH----TDLSEAE------------------IRELVLEKLELVG--LPGAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 151 GPM-SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT-------IRwleqTLNER-NSTMIIISHDRHFLNMVCTH 221
Cdd:COG1127 136 DKMpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavidelIR----ELRDElGLTSVVVTHDLDSAFAIADR 211
|
..
gi 490363216 222 MA 223
Cdd:COG1127 212 VA 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
2.07e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQD---- 72
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERelar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 73 ----------QFAY--EEFTVLDTVIMghaelweikqereriyslpemseeeGLRVADLEVKfgemdgyTVESRAGELLL 140
Cdd:COG1136 83 lrrrhigfvfQFFNllPELTALENVAL-------------------------PLLLAGVSRK-------ERRERARELLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 141 NVGIPLEQHNGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHDRHFLN 216
Cdd:COG1136 131 RVGLGDRLDHRP-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAA 209
|
.
gi 490363216 217 M 217
Cdd:COG1136 210 R 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-495 |
3.75e-19 |
|
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: 90.50 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSEN---ATIGYY 388
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQDhATDFevDMTVFDWMSLwMKPEDDEQSVRSV-----LGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKP 458
Cdd:TIGR02868 415 AQD-AHLF--DTTVRENLRL-ARPDATDEELWAAlervgLADWLRALPDGLDTVlgeggARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490363216 459 NVLIMDEPTNHLDMES----IESLNMALELYqgTLIFVSHD 495
Cdd:TIGR02868 491 PILLLDEPTEHLDAETadelLEDLLAALSGR--TVVLITHH 529
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-228 |
3.90e-19 |
|
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: 84.93 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQdqfayeeftv 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLED---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 ldtvimghaelwEIKQERERIyslpemseeeGLRVADlevkFGEMDGYTVESragelllNVGIPLeqhNGpmsevapGWK 161
Cdd:cd03229 70 ------------ELPPLRRRI----------GMVFQD----FALFPHLTVLE-------NIALGL---SG-------GQQ 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQTLNER-NSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
319-507 |
4.56e-19 |
|
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: 86.10 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSE-----------NATIG 386
Cdd:cd03245 2 RIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQDhATDFEvdMTVFDWMSLWMKPEDDEQSVRSV--LGRLLFSQDD-------IKKSVKVLSGGEKGRMLFGKLMMQK 457
Cdd:cd03245 82 YVPQD-VTLFY--GTLRDNITLGAPLADDERILRAAelAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 458 PNVLIMDEPTNHLDMESIESLNMALELYQG--TLIFVSHdREFVSSLANRII 507
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRII 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-231 |
4.67e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 86.23 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVF---LDPNERlgklkqdqfaYEEFTVLDTVIMGH 89
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvagLVPWKR----------RKKFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 90 -AELWEIKQERE------RIYSLPEmsEEEGLRVADLevkfgemdgytVEsragelLLNVGIPLEQhngPMSEVAPGWKL 162
Cdd:cd03267 103 kTQLWWDLPVIDsfyllaAIYDLPP--ARFKKRLDEL-----------SE------LLDLEELLDT---PVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 163 RVLLAQALFADPDILLLDEPTNNLDI---DTIRWLEQTLN-ERNSTMIIISHDRHFLNMVCTHMADLDYGGLT 231
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
320-509 |
6.45e-19 |
|
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: 85.54 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT-------IGYYAQDH 392
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 393 ATDFE-----VDMTVFDWMSLWM-----KPEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:cd03292 81 GVVFQdfrllPDRNVYENVAFALevtgvPPREIRKRVPAAL-ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 463 MDEPTNHLD-------MESIESLNMAlelyqGTLIFVS-HDREFVSSLANRIIEI 509
Cdd:cd03292 160 ADEPTGNLDpdttweiMNLLKKINKA-----GTTVVVAtHAKELVDTTRHRVIAL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-230 |
8.76e-19 |
|
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: 85.25 E-value: 8.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGS--KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE----------RLGKL 69
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDtvimgHAELWEikqereRIYSLPEmsEEEGLRVADLEVKFGemdgytvesragelllnvgipLEQH 149
Cdd:cd03263 81 PQFDALFDELTVRE-----HLRFYA------RLKGLPK--SEIKEEVELLLRVLG---------------------LTDK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 150 -NGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:cd03263 127 aNKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTHSMDEAEALCDRIAIMS 206
|
....
gi 490363216 227 YGGL 230
Cdd:cd03263 207 DGKL 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
1.13e-18 |
|
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: 82.70 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftvldtvimGHAEL-WEI 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD--------------------------GQDLTdDER 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 96 KQERERIYSLPE----MSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGP---MSEVAPGWKLRVLLAQ 168
Cdd:pfam00005 55 KSLRKEIGYVFQdpqlFPRLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIAR 134
|
170
....*....|....*.
gi 490363216 169 ALFADPDILLLDEPTN 184
Cdd:pfam00005 135 ALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-507 |
1.21e-18 |
|
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: 83.25 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsenatigyyaqdhatdfevd 399
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 mtvfdwmslwmkpEDDEQSVRSV-----LGRLLFSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES 474
Cdd:cd03216 60 -------------DGKEVSFASPrdarrAGIAMVYQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 490363216 475 IESLnmaLELY-----QG-TLIFVSHDREFVSSLANRII 507
Cdd:cd03216 118 VERL---FKVIrrlraQGvAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-211 |
1.29e-18 |
|
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: 84.92 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DL---APTSGNVFLD----------PNE---RLG 67
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLipgAPDEGEVLLDgkdiydldvdVLElrrRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 68 KLKQDQFAYEeFTVLDTVIMG--HAELWEIKQERERIyslpemseEEGLRVADLevkFGEmdgytVESRAGELLLNVGip 145
Cdd:cd03260 85 MVFQKPNPFP-GSIYDNVAYGlrLHGIKLKEELDERV--------EEALRKAAL---WDE-----VKDRLHALGLSGG-- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 146 lEQhngpmsevapgwkLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHD 211
Cdd:cd03260 146 -QQ-------------QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAElkKEYTIVIVTHN 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-218 |
2.76e-18 |
|
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: 82.26 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftvldtvimgHAE 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD---------------------------GAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 L--WEIKQERERIYSLPEmseeeglrvadlevkfgemdgyTVESRAGELLLNVgipleqhngpmseVAPGWKLRVLLAQA 169
Cdd:cd03246 66 IsqWDPNELGDHVGYLPQ----------------------DDELFSGSIAENI-------------LSGGQRQRLGLARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 170 LFADPDILLLDEPTNNLDIDTIRWLEQT---LNERNSTMIIISHDRHFLNMV 218
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLASA 162
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
2.86e-18 |
|
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: 84.17 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE--RLGKLKQDQF 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 75 AYEeftvldtviMG----HAELWEIKQERERIySLPemseeegLRVADLEVKFgemdgytVESRAGELLLNVGIPLEQHN 150
Cdd:cd03258 81 RRR---------IGmifqHFNLLSSRTVFENV-ALP-------LEIAGVPKAE-------IEERVLELLELVGLEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 151 GPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQTLN-ERNSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:cd03258 137 YP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINrELGLTIVLITHEMEVVKRICDRVAVME 215
|
..
gi 490363216 227 YG 228
Cdd:cd03258 216 KG 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
318-528 |
3.11e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.90 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV---------------KWSEN 382
Cdd:PRK13636 4 YILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 383 ATIGYYAQDH----ATDFEvDMTvFDWMSLWMkPEDD-EQSVRSVLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQK 457
Cdd:PRK13636 84 VGMVFQDPDNqlfsASVYQ-DVS-FGAVNLKL-PEDEvRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 458 PNVLIMDEPTNHLDMESI-ESLNMALELYQG---TLIFVSHDREFVSSLANRIIEITPEKVTnFQGTYDEFLAKK 528
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVsEIMKLLVEMQKElglTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEK 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-224 |
1.37e-17 |
|
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: 81.78 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 17 FENISVKFGGGNRY-----------------GLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYEE- 78
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 79 --------FTVLD---TVimghaelweikqeRERIyslpemseEEGLRVAdlevkfgEMDGYTVESRAGELLLNVGIPLE 147
Cdd:cd03257 84 iqmvfqdpMSSLNprmTI-------------GEQI--------AEPLRIH-------GKLSKKEARKEAVLLLLVGVGLP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 148 qhngpmSEVA---P-----GWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHDrhfL 215
Cdd:cd03257 136 ------EEVLnryPhelsgGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHD---L 206
|
....*....
gi 490363216 216 NMVCtHMAD 224
Cdd:cd03257 207 GVVA-KIAD 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-251 |
1.85e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeEFTVLDtv 85
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD----------------GLKVND-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 imGHAELWEIKQER----ERIYSLPEMSEEEGLRVADLEVKfgEMDGYTVESRAGELLLNVGIPLEQHNGPmSEVAPGWK 161
Cdd:PRK09493 68 --PKVDERLIRQEAgmvfQQFYLFPHLTALENVMFGPLRVR--GASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLDID---TIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTvHPGNYD 238
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA-EDGDPQ 221
|
250
....*....|...
gi 490363216 239 EymLAATQARERL 251
Cdd:PRK09493 222 V--LIKNPPSQRL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-507 |
1.89e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.06 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGY---EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------SENATIGYYA 389
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHAtdfevdmtVFDWMSLW-----------MKPEDDEQSVRSVLGRL-LfsQDDIKKSVKVLSGGEK-----GRMLfgk 452
Cdd:COG1116 87 QEPA--------LLPWLTVLdnvalglelrgVPKAERRERARELLELVgL--AGFEDAYPHQLSGGMRqrvaiARAL--- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 453 lmMQKPNVLIMDEPTNHLDMESIESLN-MALELYQG---TLIFVSHD-REFVsSLANRII 507
Cdd:COG1116 154 --ANDPEVLLMDEPFGALDALTRERLQdELLRLWQEtgkTVLFVTHDvDEAV-FLADRVV 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-511 |
2.01e-17 |
|
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: 81.36 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFK---DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV------KWSENATIGYYAQ 390
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHAtdfevdmtVFDWMSLW-----------MKPEDDEQSVRSVLGRL-LfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 458
Cdd:cd03293 81 QDA--------LLPWLTVLdnvalglelqgVPKAEARERAEELLELVgL--SGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 459 NVLIMDEPTNHLDMESIESLNMAL-ELYQG---TLIFVSHDREFVSSLANRIIEITP 511
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELlDIWREtgkTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-506 |
2.22e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--PNERLGKLKQDQFAyeeftvld 83
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnPCARLTPAKAHQLG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 tvimghaelweikqererIYSLPemseEEGLRVADLEVK----FGEMDGYTVESRAGELL--LNVGIPLEQHNGPMsEVA 157
Cdd:PRK15439 88 ------------------IYLVP----QEPLLFPNLSVKenilFGLPKRQASMQKMKQLLaaLGCQLDLDSSAGSL-EVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 158 PGWKLRVLlaQALFADPDILLLDEPTNNLD-IDTIRWLEQ--TLNERNSTMIIISHDRHFLNMVCTH---MADldygGLT 231
Cdd:PRK15439 145 DRQIVEIL--RGLMRDSRILILDEPTASLTpAETERLFSRirELLAQGVGIVFISHKLPEIRQLADRisvMRD----GTI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 232 VHPGNYDEYMLAAT-QARERlladnAKKKAQISELQSFVSRFSANasksRQATSRAKQIekiqltevkassrqnpfirfe 310
Cdd:PRK15439 219 ALSGKTADLSTDDIiQAITP-----AAREKSLSASQKLWLELPGN----RRQQAAGAPV--------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 311 qekklfrnaLEVENIA-KGyeantplFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENATIG--- 386
Cdd:PRK15439 269 ---------LTVEDLTgEG-------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-MLNGKEINals 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 ----------YYAQDHATD---------FEVDMTVFDWMSLWMKPEDDEQSV---RSVLGrLLFSQDDikKSVKVLSGGE 444
Cdd:PRK15439 332 taqrlarglvYLPEDRQSSglyldaplaWNVCALTHNRRGFWIKPARENAVLeryRRALN-IKFNHAE--QAARTLSGGN 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLD----------MESIESLNMAlelyqgtLIFVSHDREFVSSLANRI 506
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDvsarndiyqlIRSIAAQNVA-------VLFISSDLEEIEQMADRV 473
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
320-523 |
2.65e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPL----FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwsenatigYYAQDHATD 395
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI---------IIDGVDITD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 396 FEVDMT--------VFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKV-------------------LSGGEKGRM 448
Cdd:PRK13637 74 KKVKLSdirkkvglVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRamnivgldyedykdkspfeLSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 449 LFGKLMMQKPNVLIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREFVSSLANRIIEITPEKVTnFQGTY 521
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE-LQGTP 229
|
..
gi 490363216 522 DE 523
Cdd:PRK13637 230 RE 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-507 |
3.94e-17 |
|
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: 80.56 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAK---GYEANtplfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENAT---- 384
Cdd:cd03219 1 LEVRGLTKrfgGLVAL----DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPPHEIarlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQdHATDFEvDMTVFD--------------WMSLWMKPEDD-EQSVRSVLGRL-LfsQDDIKKSVKVLSGGEKGRM 448
Cdd:cd03219 77 IGRTFQ-IPRLFP-ELTVLEnvmvaaqartgsglLLARARREEREaRERAEELLERVgL--ADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 449 LFGKLMMQKPNVLIMDEPT---NHLD----MESIESLNMalelyQG-TLIFVSHDREFVSSLANRII 507
Cdd:cd03219 153 EIARALATDPKLLLLDEPAaglNPEEteelAELIRELRE-----RGiTVLLVEHDMDVVMSLADRVT 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
321-529 |
3.96e-17 |
|
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: 80.73 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV-----------KWSENATIGYYA 389
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDhatDFEVDMTVFDWMSLwMKPEDDEQSVrSVLGRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMMQKP 458
Cdd:cd03254 84 QD---TFLFSGTIMENIRL-GRPNATDEEV-IEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 459 NVLIMDEPTNHLDMESIESLNMALE-LYQG-TLIFVSHdREFVSSLANRIIEITPEKVTNfQGTYDEFLAKKG 529
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEkLMKGrTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
3.99e-17 |
|
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: 78.96 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQD----QFAY--EEFTVLDTV 85
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-GVDLRDLDLEslrkNIAYvpQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 ImghaelweikqeRERIYSlpemseeeglrvadlevkfgemdgytvesrAGElllnvgipleqhngpmsevapgwKLRVL 165
Cdd:cd03228 92 I------------RENILS------------------------------GGQ-----------------------RQRIA 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRH 213
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAHRLS 156
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-248 |
4.48e-17 |
|
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: 84.05 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAyEEFTVL--------D 83
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDLR-RRIAVVpqrphlfdT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 TVimghaelweikqeRE--RIySLPEMSEEEGLRVADLeVKFGEM-----DGYtvESRAGELllnvGIPL---EQHngpm 153
Cdd:COG4987 424 TL-------------REnlRL-ARPDATDEELWAALER-VGLGDWlaalpDGL--DTWLGEG----GRRLsggERR---- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 154 sevapgwklRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFLNMVcTHMADLDYGGLt 231
Cdd:COG4987 479 ---------RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEalAGRTVLLITHRLAGLERM-DRILVLEDGRI- 547
|
250
....*....|....*..
gi 490363216 232 VHPGNYDEymLAATQAR 248
Cdd:COG4987 548 VEQGTHEE--LLAQNGR 562
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
346-510 |
4.58e-17 |
|
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: 80.03 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK-----W----------SENATIGYYAQDHATdFEvDMTVFDWMSLWM 410
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLfdsrkkinlpPQQRKIGLVFQQYAL-FP-HLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 411 K---PEDDEQSVRSVLGRLLFSQDdIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES----IESLNMALE 483
Cdd:cd03297 101 KrkrNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKK 179
|
170 180
....*....|....*....|....*..
gi 490363216 484 LYQGTLIFVSHDREFVSSLANRIIEIT 510
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-226 |
4.97e-17 |
|
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: 80.17 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayEEFTVLDtviMGHAELWE 94
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR---------------HDGGWVD---LAQASPRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 95 IKQERER--------IYSLPemseeeglRVADLEV------KFGEMDGyTVESRAGELLLNVGIPLEQHngpmsEVAP-- 158
Cdd:COG4778 87 ILALRRRtigyvsqfLRVIP--------RVSALDVvaepllERGVDRE-EARARARELLARLNLPERLW-----DLPPat 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 159 ---GWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqTLNERNSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:COG4778 153 fsgGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIE----EAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-507 |
6.48e-17 |
|
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: 79.86 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEAN---TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEN-------------- 382
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 383 ATIGYYAQDHATDFEVDMTVFD--WMSLW---MKPEDDEQSVRSVLGRLLFSQDD--IKKSVKVLSGGEKGRMLFGKLMM 455
Cdd:cd03257 82 KEIQMVFQDPMSSLNPRMTIGEqiAEPLRihgKLSKKEARKEAVLLLLVGVGLPEevLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 456 QKPNVLIMDEPTNHLDMES-IESLNMALEL---YQGTLIFVSHDREFVSSLANRII 507
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVqAQILDLLKKLqeeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-213 |
6.61e-17 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 79.60 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklkqdQFAYEEFTVLDt 84
Cdd:TIGR02673 6 NVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQV--------------RIAGEDVNRLR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimGHaelwEIKQERERI-------YSLPEMSEEEGLRVAdLEVKFgeMDGYTVESRAGELLLNVGIPLEQHNGPMsEVA 157
Cdd:TIGR02673 71 ---GR----QLPLLRRRIgvvfqdfRLLPDRTVYENVALP-LEVRG--KKEREIQRRVGAALRQVGLEHKADAFPE-QLS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQTLNERNSTMIIISHDRH 213
Cdd:TIGR02673 140 GGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLserILDLLKRLNKRGTTVIVATHDLS 198
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
334-507 |
7.78e-17 |
|
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: 80.24 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 334 PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK--------WSENATIGYYAQ-DHATDFEVDMTVFD 404
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARARRVALvEQDSDTAVPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 405 --------WMSLW-MKPEDDEQSVRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES- 474
Cdd:TIGR03873 95 vvalgripHRSLWaGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAq 173
|
170 180 190
....*....|....*....|....*....|....*
gi 490363216 475 IESLNMALELY--QGTLIFVSHDREFVSSLANRII 507
Cdd:TIGR03873 174 LETLALVRELAatGVTVVAALHDLNLAASYCDHVV 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-507 |
8.45e-17 |
|
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: 83.10 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK--------WSENA---TIGY 387
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladADADSwrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQdhaTDFEVDMTVFDWMSLWMKPEDDEQSVRSV-----------LGRLLFSQddIKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:TIGR02857 401 VPQ---HPFLFAGTIAENIRLARPDASDAEIREALeragldefvaaLPQGLDTP--IGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 457 KPNVLIMDEPTNHLDMESIESLNMAL-ELYQG-TLIFVSHDREfVSSLANRII 507
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALrALAQGrTVLLVTHRLA-LAALADRIV 527
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-214 |
1.08e-16 |
|
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: 78.73 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDqfayeeftvldt 84
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLTDDKKN------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimghaelweIKQERERI------YSL-PEMSEEEGLRVADLEVKfgEMDGYTVESRAGELLLNVGIPLEQHNGPmSEVA 157
Cdd:cd03262 71 ----------INELRQKVgmvfqqFNLfPHLTVLENITLAPIKVK--GMSKAEAEERALELLEKVGLADKADAYP-AQLS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQT---LNERNSTMIIISHDRHF 214
Cdd:cd03262 138 GGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVmkdLAEEGMTMVVVTHEMGF 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-245 |
1.18e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAyeeftvldt 84
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAFA--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimghaelweikqeRERIYSLPEMSEEEGLRVADLEV-----------KFGEMDGYTVEsragELLLNVGI-PLEQHngP 152
Cdd:PRK10575 85 --------------RKVAYLPQQLPAAEGMTVRELVAigrypwhgalgRFGAADREKVE----EAISLVGLkPLAHR--L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 153 MSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDrhfLNMV---CTHMADL 225
Cdd:PRK10575 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD---INMAaryCDYLVAL 221
|
250 260
....*....|....*....|
gi 490363216 226 dYGGLTVHPGNYDEYMLAAT 245
Cdd:PRK10575 222 -RGGEMIAQGTPAELMRGET 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-532 |
1.36e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATDFE 397
Cdd:PRK09544 3 SLVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 398 VDMTVFDWMSLwmKPEDDEQSVRSVLGRLLfSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIES 477
Cdd:PRK09544 82 LPLTVNRFLRL--RPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 478 L-----NMALELYQGTLIfVSHDREFVSSLANRIIEI--------TPEKVTnfqgTYDEFLAKKGIDG 532
Cdd:PRK09544 159 LydlidQLRRELDCAVLM-VSHDLHLVMAKTDEVLCLnhhiccsgTPEVVS----LHPEFISMFGPRG 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
336-507 |
1.37e-16 |
|
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: 78.73 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 336 FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEN--ATIGYyaqdhATDFEVDMTV-----FDWMSL 408
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGL-----GGGFNPELTGreniyLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 409 WMKPEDDEQSVRSVLGrllFSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD-------MESIESLN 479
Cdd:cd03220 113 GLSRKEIDEKIDEIIE---FSElgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafqekcQRRLRELL 189
|
170 180
....*....|....*....|....*...
gi 490363216 480 MAlelyQGTLIFVSHDREFVSSLANRII 507
Cdd:cd03220 190 KQ----GKTVILVSHDPSSIKRLCDRAL 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-523 |
1.49e-16 |
|
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: 79.31 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS-ENAT--------IGYYA 389
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgEDATdvpvqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHATdFEvDMTVFDWMS--LWMKP---EDDEQSVRSVLGRLL-FSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKPNVL 461
Cdd:cd03296 81 QHYAL-FR-HMTVFDNVAfgLRVKPrseRPPEAEIRAKVHELLkLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 462 IMDEPTNHLDMESIESLNMAL-ELYQG---TLIFVSHDREFVSSLANRIIEITPEKVTNFqGTYDE 523
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLrRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQV-GTPDE 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-531 |
1.65e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK-----------WSENAT 384
Cdd:PRK13635 3 EEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQDHATDFeVDMTVFDWMSLWMK----PEDDEQS-VRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 459
Cdd:PRK13635 83 VGMVFQNPDNQF-VGATVQDDVAFGLEnigvPREEMVErVDQAL-RQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 460 VLIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSlANRII---------EITPEKVtnFQgtYDE 523
Cdd:PRK13635 161 IIILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHDLDEAAQ-ADRVIvmnkgeileEGTPEEI--FK--SGH 232
|
....*...
gi 490363216 524 FLAKKGID 531
Cdd:PRK13635 233 MLQEIGLD 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-467 |
1.68e-16 |
|
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: 78.63 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFkDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-SENAT-----------IGY 387
Cdd:cd03224 1 LEVENLNAGYGKSQILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHATdFEvDMTVFD--WMSLWMKPEDD-EQSVRSVLGrlLFS--QDDIKKSVKVLSGGEKgRML-FGKLMMQKPNVL 461
Cdd:cd03224 80 VPEGRRI-FP-ELTVEEnlLLGAYARRRAKrKARLERVYE--LFPrlKERRKQLAGTLSGGEQ-QMLaIARALMSRPKLL 154
|
....*.
gi 490363216 462 IMDEPT 467
Cdd:cd03224 155 LLDEPS 160
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
310-530 |
1.98e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.13 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 310 EQEKKLFRNALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW---------- 379
Cdd:COG1132 330 AVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltl 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 380 -SENATIGYYAQDHatdFEVDMTVFDWMSLWmKPEDDEQSVRSVLgRLLFSQDDIKK------------SVKvLSGGEKG 446
Cdd:COG1132 410 eSLRRQIGVVPQDT---FLFSGTIRENIRYG-RPDATDEEVEEAA-KAAQAHEFIEAlpdgydtvvgerGVN-LSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 447 RMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMAL-ELYQG-TLIFVSHdRefVSSLAN----------RIIEitpekv 514
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALeRLMKGrTTIVIAH-R--LSTIRNadrilvlddgRIVE------ 554
|
250
....*....|....*.
gi 490363216 515 tnfQGTYDEFLAKKGI 530
Cdd:COG1132 555 ---QGTHEELLARGGL 567
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
334-509 |
2.52e-16 |
|
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: 78.53 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 334 PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK------WSEN----ATIGY-YAQdhATDFEVDMTV 402
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRkkflRRIGVvFGQ--KTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 403 FDWMSL----WMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESL 478
Cdd:cd03267 113 IDSFYLlaaiYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190
....*....|....*....|....*....|....*
gi 490363216 479 NMAL----ELYQGTLIFVSHDREFVSSLANRIIEI 509
Cdd:cd03267 193 RNFLkeynRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-211 |
3.08e-16 |
|
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: 78.15 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFL--------DPNER-LGKLKQDQFAY 76
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvPVQERnVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 EEFTVLDTVIMGhaelWEIKQERERiyslpeMSEEEglrvadlevkfgemdgytVESRAGELLLNVGIPLEQHNGPmSEV 156
Cdd:cd03296 87 RHMTVFDNVAFG----LRVKPRSER------PPEAE------------------IRAKVHELLKLVQLDWLADRYP-AQL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHD 211
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-507 |
3.70e-16 |
|
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: 77.41 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLF---KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGrvkwseNATIGYYAQDHATdF 396
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEP-A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 397 EV---------DMTVFDWMSLW-----------MKPEDDEQSVRSVLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:cd03266 75 EArrrlgfvsdSTGLYDRLTARenleyfaglygLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 457 KPNVLIMDEPTNHLDMESIESLNMALELY---QGTLIFVSHDREFVSSLANRII 507
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVV 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-494 |
3.91e-16 |
|
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: 76.20 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQdhatdFEV 398
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 DMTVFDwmslwMKPEDDEQSVRSVLGRLlfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES-IES 477
Cdd:cd03247 76 LISVLN-----QRPYLFDTTLRNNLGRR-------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQL 137
|
170
....*....|....*...
gi 490363216 478 LNMALELYQG-TLIFVSH 494
Cdd:cd03247 138 LSLIFEVLKDkTLIWITH 155
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
302-507 |
4.01e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 302 RQNPFIRFEQEKKLFRNALEV--------ENIAKGYEANT-PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGEL-- 370
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLDLservaivlEAFGVELRVVErYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 371 TPDNGRVKWSENatigyyaqdhatDFEVDMTVFDwmSLWMKpEDDEQSVRsVLGRL-LFSQDDIKKSVKVLSGGEKGRML 449
Cdd:COG2401 83 TPVAGCVDVPDN------------QFGREASLID--AIGRK-GDFKDAVE-LLNAVgLSDAVLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 450 FGKLMMQKPNVLIMDEPTNHLDMES--IESLNMALELYQG--TLIFVSHDREFVSSLA-NRII 507
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTakRVARNLQKLARRAgiTLVVATHHYDVIDDLQpDLLI 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-495 |
4.45e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYA---------- 389
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlarrlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 -QDHATdfEVDMTVFD--------WMSLWMK-PEDDEQSVRSVLGRLLFSQDdIKKSVKVLSGGEKGRMLFGKLMMQKPN 459
Cdd:PRK11231 82 pQHHLT--PEGITVRElvaygrspWLSLWGRlSAEDNARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 490363216 460 VLIMDEPTNHLDM-ESIESLNMALELYQG--TLIFVSHD 495
Cdd:PRK11231 159 VVLLDEPTTYLDInHQVELMRLMRELNTQgkTVVTVLHD 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-211 |
6.04e-16 |
|
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: 77.22 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE--------------RLGKLKQDQFAYE 77
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 78 EFTVLDTVIMGhaelweikqereriySLPEMSEEEGLrvadlevkFGemdGYTVES--RAGELLLNVGIpLEQHNGPMSE 155
Cdd:cd03256 92 RLSVLENVLSG---------------RLGRRSTWRSL--------FG---LFPKEEkqRALAALERVGL-LDKAYQRADQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHD 211
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-512 |
6.34e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 75.27 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLvGELTP-DNGRVKWSENATIGYYAQdhatdfev 398
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQ-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 dmtvfdwmslwmKPEDDEQSVRSVLgrllfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESL 478
Cdd:cd03223 72 ------------RPYLPLGTLREQL---------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180 190
....*....|....*....|....*....|....
gi 490363216 479 NMALELYQGTLIFVSHdREFVSSLANRIIEITPE 512
Cdd:cd03223 131 YQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-211 |
7.03e-16 |
|
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: 76.74 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD------PNERLGKLKQDQFA 75
Cdd:cd03293 5 NVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQQDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTVLDTVIMGhaelweikqereriyslPEMSeeeglRVADLEVKfgemdgytveSRAGELLLNVGIPLEQHNGPmSE 155
Cdd:cd03293 85 LPWLTVLDNVALG-----------------LELQ-----GVPKAEAR----------ERAEELLELVGLSGFENAYP-HQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHD 211
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-262 |
7.27e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE---RLGKL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpismlsSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDTVIMG---HAELWEikqereriyslpEMSEEEGLRVADlevkfgEMDGYTVESRAgelllnvgipl 146
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLWG------------RLSAEDNARVNQ------AMEQTRINHLA----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 147 eqhNGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDID---TIRWLEQTLNERNSTMIIISHDrhfLNMV---CT 220
Cdd:PRK11231 133 ---DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD---LNQAsryCD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490363216 221 HMADLDYGGLtVHPGNYDEYMlaatqaRERLLADNAKKKAQI 262
Cdd:PRK11231 207 HLVVLANGHV-MAQGTPEEVM------TPGLLRTVFDVEAEI 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
320-506 |
7.75e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENaTIGYyaqDHATDFEVD 399
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKY---DKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 MTV---------------------FDWMSLWMKPEDDEQSVRSVLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKP 458
Cdd:PRK13639 78 KTVgivfqnpddqlfaptveedvaFGPLNLGLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 459 NVLIMDEPTNHLD-MESIESLNMALEL-YQG-TLIFVSHDREFVSSLANRI 506
Cdd:PRK13639 157 EIIVLDEPTSGLDpMGASQIMKLLYDLnKEGiTIIISTHDVDLVPVYADKV 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-226 |
9.53e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LIS-NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDqfAYEEFT 80
Cdd:PRK09544 4 LVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK--LYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDTVimghaelweikqerERIyslpeMSEEEGLRVADLEVKFGEMdgytvesRAGELLlnvgipleqhNGPMSEVAPGW 160
Cdd:PRK09544 82 LPLTV--------------NRF-----LRLRPGTKKEDILPALKRV-------QAGHLI----------DAPMQKLSGGE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 161 KLRVLLAQALFADPDILLLDEPTNNLDI-------DTIrwlEQTLNERNSTMIIISHDRHFLnmvcthMADLD 226
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLI---DQLRRELDCAVLMVSHDLHLV------MAKTD 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
1.16e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD---------------PNERLGKLKQDQFAYEEFTVLD 83
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 TVIMghaelweikqereriyslpemseeeglrvadlEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPmSEVAPGWKLR 163
Cdd:PRK11629 107 NVAM--------------------------------PLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDI---DTIRWLEQTLNERNST-MIIISHD 211
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-212 |
1.18e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.26 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLIS-NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLgklkqdqfayeeF 79
Cdd:COG1118 1 MSIEvRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN-GRDL------------F 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 TVLDTvimghaelweikQEReRI------YSL-PEMSEEE----GLRVADL---EVKfgemdgytveSRAGELLLNVGIP 145
Cdd:COG1118 68 TNLPP------------RER-RVgfvfqhYALfPHMTVAEniafGLRVRPPskaEIR----------ARVEELLELVQLE 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 146 -LEQHngpmsevAP-----GWKLRVLLAQALFADPDILLLDEPTNNLDI---DTIR-WLEQTLNERNSTMIIISHDR 212
Cdd:COG1118 125 gLADR-------YPsqlsgGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-506 |
1.24e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.87 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGR--------VKWSEN--ATIGYYA 389
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHATDFEvdMTVFDWMsLWM------KPEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIM 463
Cdd:cd03265 80 QDLSVDDE--LTGWENL-YIHarlygvPGAERRERIDELL-DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 464 DEPTNHLDMES-------IESLNMAlelyQGTLIFV-SHDREFVSSLANRI 506
Cdd:cd03265 156 DEPTIGLDPQTrahvweyIEKLKEE----FGMTILLtTHYMEEAEQLCDRV 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
320-523 |
1.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK------WSEN-----ATIGYY 388
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepiTKENirevrKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQD-----HATDFEVDMTvFDWMSLWMKPEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIM 463
Cdd:PRK13652 84 FQNpddqiFSPTVEQDIA-FGPINLGLDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 464 DEPTNHLDMESIESL----NMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNfQGTYDE 523
Cdd:PRK13652 162 DEPTAGLDPQGVKELidflNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA-YGTVEE 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-510 |
1.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.08 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV------------KWSENaTI 385
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKWVRS-KV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQDhATDFEVDMTVFDWMS-----LWMKPEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 460
Cdd:PRK13647 82 GLVFQD-PDDQVFSSTVWDDVAfgpvnMGLDKDEVERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 461 LIMDEPTNHLDMESIESLNMALELY--QG-TLIFVSHDREFVSSLANRIIEIT 510
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLAAEWADQVIVLK 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
320-522 |
2.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPL----FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW----SENATIGYYAQD 391
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 392 HATDFEVDMT-----------------------------------VFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKS 436
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrvgvvfqfaeyqlfeqtiekdiIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 437 VKVLSGGEKGRM-LFGKLMMQkPNVLIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLANRIIEITPE 512
Cdd:PRK13651 163 PFELSGGQKRRVaLAGILAME-PDFLVFDEPTAGLDPQgVKEILEIFDNLNKQgkTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|
gi 490363216 513 KVTNFQGTYD 522
Cdd:PRK13651 242 KIIKDGDTYD 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-231 |
3.06e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-----------PNERLGKL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDTVIMGHAelweikqereriyslPEMSeeeglrvadlevKFGEMDgyTVESRAGELLLNVGIPLEQH 149
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRT---------------PHRS------------RFDTWT--ETDRAAVERAMERTGVAQFA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 150 NGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDID-TIRWLE--QTLNERNSTMIIISHDrhfLNMV---CTHMA 223
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHD---LDLAaryCDELV 210
|
....*...
gi 490363216 224 DLDYGGLT 231
Cdd:PRK09536 211 LLADGRVR 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-497 |
3.26e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.13 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 27 GNRYGLIGANGSGKSTFMKILGGDLAPTSG---NVFLDPNeRLGKLKQDQFAYEEFTVLDTVIMGHAELWEIKQERERIy 103
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGerqSQFSHIT-RLSFEQLQKLVSDEWQRNNTDMLSPGEDDTGRTTAEII- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 104 sLPEMSEEEglRVADLEVKFGEMDgytvesragelLLNvgipleqhnGPMSEVAPGWKLRVLLAQALFADPDILLLDEPT 183
Cdd:PRK10938 107 -QDEVKDPA--RCEQLAQQFGITA-----------LLD---------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 184 NNLDIDTIRWLEQ---TLNERNSTMIIISHDRHFLNMVCTHMADLdyggltvhpgnyDEYMLAATQARERLLADnakkkA 260
Cdd:PRK10938 164 DGLDVASRQQLAEllaSLHQSGITLVLVLNRFDEIPDFVQFAGVL------------ADCTLAETGEREEILQQ-----A 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 261 QISELqsfvsrfsanasksrqatSRAKQIEKIQLTEvKASSRQNPFIRFEQEKKLFRNALEVENiakgyeaNTPLFKDVN 340
Cdd:PRK10938 227 LVAQL------------------AHSEQLEGVQLPE-PDEPSARHALPANEPRIVLNNGVVSYN-------DRPILHNLS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 341 MMLEVGEKVAILGTNGVGKSTMIKTLVG--------ELT-----PDNGRVKWSENATIGYYAQDHATDFEVDMTV----- 402
Cdd:PRK10938 281 WQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysnDLTlfgrrRGSGETIWDIKKHIGYVSSSLHLDYRVSTSVrnvil 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 403 ---FDWMSLWMKPEDDEQS-VRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDmesieSL 478
Cdd:PRK10938 361 sgfFDSIGIYQAVSDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD-----PL 435
|
490 500
....*....|....*....|....*...
gi 490363216 479 NMALELY---------QGTLIFVSHDRE 497
Cdd:PRK10938 436 NRQLVRRfvdvlisegETQLLFVSHHAE 463
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
320-530 |
3.30e-15 |
|
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: 74.96 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-----------SENATIGYY 388
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQdhatdfevDMTVFDwmslwmkpEDDEQSVRsvLGRLLFSQDDIKKSVKV------------------------LSGGE 444
Cdd:cd03253 81 PQ--------DTVLFN--------DTIGYNIR--YGRPDATDEEVIEAAKAaqihdkimrfpdgydtivgerglkLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLD----MESIESLNmalELYQG-TLIFVSHDREFVSSlANRIIEITPEKVTNfQG 519
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDthteREIQAALR---DVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RG 217
|
250
....*....|.
gi 490363216 520 TYDEFLAKKGI 530
Cdd:cd03253 218 THEELLAKGGL 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
31-213 |
3.62e-15 |
|
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: 74.78 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQ----------FAYEEF------TVLDTVimghaelwe 94
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDArarlrarhvgFVFQSFqllptlTALENV--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 95 ikqereriySLPemSEEEGLRVAdlevkfgemdgytvESRAGELLLNVGI-PLEQHngpmsevAP-----GWKLRVLLAQ 168
Cdd:COG4181 112 ---------MLP--LELAGRRDA--------------RARARALLERVGLgHRLDH-------YPaqlsgGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 169 ALFADPDILLLDEPTNNLDIDT----IRWLEQtLN-ERNSTMIIISHDRH 213
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATgeqiIDLLFE-LNrERGTTLVLVTHDPA 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-507 |
4.24e-15 |
|
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: 75.14 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsENATIGYYAQDHATDFEvdMTVFDWMSlwmkpeddeqSVRSVLGR 425
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYE--GTVRDLLS----------SITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 426 LLFSQDDIKKSVKV----------LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDME----SIESLNMALELYQGTLIF 491
Cdd:cd03237 92 HPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFV 171
|
170
....*....|....*.
gi 490363216 492 VSHDREFVSSLANRII 507
Cdd:cd03237 172 VEHDIIMIDYLADRLI 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
4.88e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.89 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNV-FLDPNErlgKLKQDQFAYEEf 79
Cdd:PRK13651 7 NIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDE---KNKKKTKEKEK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 tVLDTVIMGHA---ELWEIKQERERI--------YSLPEMSEEEglrvadlEVKFGE----MDGYTVESRAGELLLNVGI 144
Cdd:PRK13651 83 -VLEKLVIQKTrfkKIKKIKEIRRRVgvvfqfaeYQLFEQTIEK-------DIIFGPvsmgVSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 145 PLEQHNGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-IDTIRWLE--QTLNERNSTMIIISHD 211
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-507 |
5.52e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 76.34 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNmmLEV--GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT----------IGY 387
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVS--LEIasGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpprerrVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHATdFEvDMTVFDwmslwmkpeddeqSVRSVLGRLLFSQDDIKKSVK-----V------------LSGGEKGRMLF 450
Cdd:COG1118 80 VFQHYAL-FP-HMTVAE-------------NIAFGLRVRPPSKAEIRARVEellelVqlegladrypsqLSGGQRQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 451 GKLMMQKPNVLIMDEPTNHLD------MESieSLNMALELYQGTLIFVSHDREFVSSLANRII 507
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-512 |
5.80e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 294 LTEVKASSRQNPFIRFEQEkklfrNALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGeLTPD 373
Cdd:COG4178 342 LEAADALPEAASRIETSED-----GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 374 -NGRVKWSENATIGYYAQ----------------DHATDFevdmtvfdwmslwmkpeDDEQsVRSV-----LGRLLFSQD 431
Cdd:COG4178 416 gSGRIARPAGARVLFLPQrpylplgtlreallypATAEAF-----------------SDAE-LREAleavgLGHLAERLD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 432 DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLnMAL---ELYQGTLIFVSHdREFVSSLANRIIE 508
Cdd:COG4178 478 EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL-YQLlreELPGTTVISVGH-RSTLAAFHDRVLE 555
|
....
gi 490363216 509 ITPE 512
Cdd:COG4178 556 LTGD 559
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
320-529 |
6.40e-15 |
|
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: 74.44 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPL-FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV-----------KWSENATIGY 387
Cdd:cd03252 1 ITFEHVRFRYKPDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHATdfeVDMTVFDWMSLwmkpEDDEQSVRSVL--GRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLM 454
Cdd:cd03252 81 VLQENVL---FNRSIRDNIAL----ADPGMSMERVIeaAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 455 MQKPNVLIMDEPTNHLDMESIESL--NMALELYQGTLIFVSHDREFVSSlANRIIEITPEKVTNfQGTYDEFLAKKG 529
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAImrNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELLAENG 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-228 |
6.46e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 10 QFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE-RLGKLKQDQ---FAYEEFTVLDT- 84
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTiNLVRDKDGQlkvADKNQLRLLRTr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 --VIMGHAELWEIKQERERIYSLPemSEEEGLRVADlevkfgemdgytVESRAGELLLNVGIPLEQHNGPMSEVAPGWKL 162
Cdd:PRK10619 94 ltMVFQHFNLWSHMTVLENVMEAP--IQVLGLSKQE------------ARERAVKYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 163 RVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
336-528 |
1.00e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 336 FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT--IGYyaqdhATDFEVDMTVfdwmslwmkpe 413
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalLEL-----GAGFHPELTG----------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 414 ddEQSVRSVlGRLL-FSQDDIKK-----------------SVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDME-- 473
Cdd:COG1134 106 --RENIYLN-GRLLgLSRKEIDEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfq 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 474 --SIESLNmalELYQ--GTLIFVSHDREFVSSLANRIIEI---------TPEKVTNFqgtYDEFLAKK 528
Cdd:COG1134 183 kkCLARIR---ELREsgRTVIFVSHSMGAVRRLCDRAIWLekgrlvmdgDPEEVIAA---YEALLAGR 244
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-227 |
1.06e-14 |
|
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: 76.56 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGnvfldpnerlgklkqdqfayeeft 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG------------------------ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vldTVIMGHAELWEIKQE--RERIYSLP------EMSEEEGLRVADLEVKFGEMDGytVESRAGELLLNVGIPlEQHNGP 152
Cdd:TIGR02857 378 ---SIAVNGVPLADADADswRDQIAWVPqhpflfAGTIAENIRLARPDASDAEIRE--ALERAGLDEFVAALP-QGLDTP 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 153 MSE----VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTirwlEQTLNE------RNSTMIIISHDRHflnmvctHM 222
Cdd:TIGR02857 452 IGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEalralaQGRTVLLVTHRLA-------LA 520
|
....*
gi 490363216 223 ADLDY 227
Cdd:TIGR02857 521 ALADR 525
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-228 |
1.07e-14 |
|
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: 73.17 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSG-------NVFLDPNE---RLGKLKQDQFA 75
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPREvrrRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTVLDTVIMgHAelweikqereRIYSLPemseeeglrvadlevkfgemdGYTVESRAGELLLNVGIpLEQHNGPMSE 155
Cdd:cd03265 85 DDELTGWENLYI-HA----------RLYGVP---------------------GAERRERIDELLDFVGL-LEAADRLVKT 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-209 |
1.14e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAYeeft 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLDPEDRRRIGY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vldtvimghaelweikqereriysLPemsEEEGL----RVADLEVKFGEMDGYT---VESRAGELLLNVGIPlEQHNGPM 153
Cdd:COG4152 76 ------------------------LP---EERGLypkmKVGEQLVYLARLKGLSkaeAKRRADEWLERLGLG-DRANKKV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIIS 209
Cdd:COG4152 128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRElaAKGTTVIFS 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
1.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftvlDTVIMGHAELWEIKQE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD---------------------DITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 99 RERI---YSLPEMSEEEGlrVADLEVKFG----EMDGYTVESRAGELLLNVGIP---LEQHNGPMSevapGWKLR-VLLA 167
Cdd:PRK13646 84 RKRIgmvFQFPESQLFED--TVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrdvMSQSPFQMS----GGQMRkIAIV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490363216 168 QALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-507 |
1.26e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 324 NIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKST---MIKTL----VGELTPDNGRVKWSENA--TIGYYAQDHAt 394
Cdd:PRK11000 8 NVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLeditSGDLFIGEKRMNDVPPAerGVGMVFQSYA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 dFEVDMTVFDWMSLWMK-----PEDDEQSVRSV-----LGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMD 464
Cdd:PRK11000 86 -LYPHLSVAENMSFGLKlagakKEEINQRVNQVaevlqLAHLL------DRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 465 EPTNHLD------MES-IESLNMALelyQGTLIFVSHDREFVSSLANRII 507
Cdd:PRK11000 159 EPLSNLDaalrvqMRIeISRLHKRL---GRTMIYVTHDQVEAMTLADKIV 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-507 |
1.62e-14 |
|
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: 72.98 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTL-----VGELTPDNGRV--------KWSEN---- 382
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVlldgkdiyDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 383 -ATIGYYAQdHATDFevDMTVFDWMSL-----WMKPEDD-EQSVRSVLGR-LLFSQDDIKKSVKVLSGGEKGRMLFGKLM 454
Cdd:cd03260 80 rRRVGMVFQ-KPNPF--PGSIYDNVAYglrlhGIKLKEElDERVEEALRKaALWDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 455 MQKPNVLIMDEPTNHLDMES---IESLNMALElYQGTLIFVSHDREFVSSLANRII 507
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPIStakIEELIAELK-KEYTIVIVTHNMQQAARVADRTA 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-218 |
1.65e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 75.94 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNERLGK----LKQDqfayeeft 80
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwDREELGRhigyLPQD-------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vldtvimghAELWE--IkqeRERIYSLPEMSEE---EGLRVADLEvkfgEM-----DGYtvESRAGELllnvGIPLeqhn 150
Cdd:COG4618 415 ---------VELFDgtI---AENIARFGDADPEkvvAAAKLAGVH----EMilrlpDGY--DTRIGEG----GARL---- 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 151 gpmsevAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISHDRHFLNMV 218
Cdd:COG4618 469 ------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRalkARGATVVVITHRPSLLAAV 533
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
329-509 |
1.75e-14 |
|
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: 72.53 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 329 YEANTPLFKDVNmmLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwsenaTIGyyAQDHAT----DFEVDM---- 400
Cdd:cd03298 9 SYGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV------LIN--GVDVTAappaDRPVSMlfqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 401 -------TVFDWMSLWMKP-----EDDEQSVRSVLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTN 468
Cdd:cd03298 79 nnlfahlTVEQNVGLGLSPglkltAEDRQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490363216 469 HLD-MESIESLNMALELY---QGTLIFVSHDREFVSSLANRIIEI 509
Cdd:cd03298 158 ALDpALRAEMLDLVLDLHaetKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-210 |
1.90e-14 |
|
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: 73.03 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAyEEFTVL- 82
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLR-RAIGVVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 83 -DTVIMGHAELWEIKqereriYSLPEMSEEE---GLRVADLEVKFGEM-DGYtvESRAGELllnvGIPLeqhngpmsevA 157
Cdd:cd03253 82 qDTVLFNDTIGYNIR------YGRPDATDEEvieAAKAAQIHDKIMRFpDGY--DTIVGER----GLKL----------S 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-186 |
1.96e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQF-GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERlgklkqdQFAyeeftvlD 83
Cdd:PRK11288 8 DGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-------RFA-------S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 TVIMGHAELWEIKQErerIYSLPEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQhNGPMSEVAPGWKLR 163
Cdd:PRK11288 73 TTAALAAGVAIIYQE---LHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDP-DTPLKYLSIGQRQM 148
|
170 180
....*....|....*....|...
gi 490363216 164 VLLAQALFADPDILLLDEPTNNL 186
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSL 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-210 |
2.07e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNE--RLG-------- 67
Cdd:COG3845 10 GITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsPRDaiALGigmvhqhf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 68 KLkqdqfaYEEFTVLDTVIMGHAELWE----IKQERERIyslPEMSEEEGLRVaDLEVKfgemdgytVESragellLNVG 143
Cdd:COG3845 90 ML------VPNLTVAENIVLGLEPTKGgrldRKAARARI---RELSERYGLDV-DPDAK--------VED------LSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 144 iplEQHngpmsevapgwklRVLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqTLNERNSTMIIISH 210
Cdd:COG3845 146 ---EQQ-------------RVEILKALYRGARILILDEPTAVLTpqeadelFEILR----RLAAEGKSIIFITH 199
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
2.12e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.35 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVF---LDPNERlgklkQDQFAYEEftvldTVIMGH-AELW 93
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPFKR-----RKEFARRI-----GVVFGQrSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 ---------EIKQErerIYSLPEmseeeglrvADLEVKFGEMdgytVEsragelLLNVGIPLEQhngPMSEVAPGWKLRV 164
Cdd:COG4586 109 wdlpaidsfRLLKA---IYRIPD---------AEYKKRLDEL----VE------LLDLGELLDT---PVRQLSLGQRMRC 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDI---DTIRWLEQTLN-ERNSTMIIISHD 211
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNrERGTTILLTSHD 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-232 |
3.23e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.79 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnERLGKLkqdqfAY---------EEFTVLDTVIM 87
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRV-----SSllglgggfnPELTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 88 GHAELW----EIKQERERIYSLpemseeeglrvADLEvKFGEMdgytvesragelllnvgipleqhngPMSEVAPGWKLR 163
Cdd:cd03220 108 NGRLLGlsrkEIDEKIDEIIEF-----------SELG-DFIDL-------------------------PVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTV 232
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDaafqekcQRRLR----ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-507 |
3.47e-14 |
|
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: 71.79 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENATIGYYAQD-HATDFEV 398
Cdd:cd03262 1 IEIKNLHKSFGDFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-IIDGLKLTDDKKNiNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 DMtVFDWMSLW------------------MKPEDDEQSVRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 460
Cdd:cd03262 79 GM-VFQQFNLFphltvlenitlapikvkgMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 461 LIMDEPTNHLDMESI-ESLNMALELYQG--TLIFVSHDREFVSSLANRII 507
Cdd:cd03262 157 MLFDEPTSALDPELVgEVLDVMKDLAEEgmTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-211 |
3.57e-14 |
|
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: 72.33 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPnerlgklkqdqfayEEFTVLDT 84
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG--------------EDIREQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 V----IMGHAelweIKQererIYSLPEMSEEE--GLrVADLEvKFGEMdgyTVESRAGELLLNVGIPLEQHNG--PmSEV 156
Cdd:cd03295 71 VelrrKIGYV----IQQ----IGLFPHMTVEEniAL-VPKLL-KWPKE---KIRERADELLALVGLDPAEFADryP-HEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQ---TLNER-NSTMIIISHD 211
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQElGKTIVFVTHD 195
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
320-530 |
4.29e-14 |
|
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: 71.88 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYE-ANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-----------SENATIGY 387
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDhatDFEVDMTVFDWMSlWMKPEDDEQSVRSVLgRLLFSQDDIKKS------------VKvLSGGEKGRMLFGKLMM 455
Cdd:cd03251 81 VSQD---VFLFNDTVAENIA-YGRPGATREEVEEAA-RAANAHEFIMELpegydtvigergVK-LSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 456 QKPNVLIMDEPTNHLDMESIESLNMALE-LYQG-TLIFVSHDREFVSSlANRIIEITPEKVTNfQGTYDEFLAKKGI 530
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALErLMKNrTTFVIAHRLSTIEN-ADRIVVLEDGKIVE-RGTHEELLAQGGV 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
4.49e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQD----QFAY--EEFTVL-DT 84
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-GVDIRDLTLEslrrQIGVvpQDTFLFsGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VimghaelweikqeRERI-YSLPEMSEEE---GLRVADLEVKFGEM-DGYtvESRAGElllnvgipleqhNGpmSEVAPG 159
Cdd:COG1132 430 I-------------RENIrYGRPDATDEEveeAAKAAQAHEFIEALpDGY--DTVVGE------------RG--VNLSGG 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 160 WKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
338-528 |
4.70e-14 |
|
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: 73.61 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 338 DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK-----WSENAT----------IGYYAQDhATDFEvDMTV 402
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtLFDSRKgiflppekrrIGYVFQE-ARLFP-HLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 403 FDWMSLWMK---PEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES----- 474
Cdd:TIGR02142 93 RGNLRYGMKrarPSERRISFERVI-ELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeil 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 475 --IESLNMALELyqgTLIFVSHDREFVSSLANRIIEITPEKVTNFqGTYDEFLAKK 528
Cdd:TIGR02142 172 pyLERLHAEFGI---PILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWASP 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
329-531 |
5.27e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.75 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 329 YEANTPL----FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATD--------- 395
Cdd:PRK13634 12 YQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPlrkkvgivf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 396 -------FEvdMTV-----FDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRM-LFGKLMMQkPNVLI 462
Cdd:PRK13634 92 qfpehqlFE--ETVekdicFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVaIAGVLAME-PEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 463 MDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLANRIIEI---------TPEKVtnFQGTydEFLA 526
Cdd:PRK13634 169 LDEPTAGLDpkgrkemMEMFYKLHKEKGL---TTVLVTHSMEDAARYADQIVVMhkgtvflqgTPREI--FADP--DELE 241
|
....*
gi 490363216 527 KKGID 531
Cdd:PRK13634 242 AIGLD 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-524 |
7.07e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.20 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFkDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwsenaTIGyyaqDHATDF-- 396
Cdd:PRK11124 2 SIQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL------NIA----GNHFDFsk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 397 ------------EVDMtVFDWMSLW--MKPEDD--EQSVRsVLGrlLFSQDDIKKSVKV----------------LSGGE 444
Cdd:PRK11124 71 tpsdkairelrrNVGM-VFQQYNLWphLTVQQNliEAPCR-VLG--LSKDQALARAEKLlerlrlkpyadrfplhLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLANRIIEITPEKVTNfQGTY 521
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETgiTQVIVTHEVEVARKTASRVVYMENGHIVE-QGDA 225
|
...
gi 490363216 522 DEF 524
Cdd:PRK11124 226 SCF 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-216 |
8.53e-14 |
|
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: 70.51 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNErLGKLKQDQFAYeeftvldt 84
Cdd:cd03292 5 NVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGRAIPY-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 vimghaelweIKQERERIYS----LPEMSEEEGLRVAdLEVKfgEMDGYTVESRAGELLLNVGIPLEQHNGPMsEVAPGW 160
Cdd:cd03292 76 ----------LRRKIGVVFQdfrlLPDRNVYENVAFA-LEVT--GVPPREIRKRVPAALELVGLSHKHRALPA-ELSGGE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 161 KLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQTLNERNSTMIIISHDRHFLN 216
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVD 200
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
8.66e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNERLGK----L 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDTVIMG---HAELWEIKQERERIyslpemseEEGLRVADLEvkfgemdgytvesragelllnvgiPL 146
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpYSKGRLTAEDREII--------DEAIAYLDLE------------------------DL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 147 EQHNgpMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHD 211
Cdd:COG4604 129 ADRY--LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
320-467 |
8.82e-14 |
|
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: 70.78 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFkDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-SENAT-----------IGY 387
Cdd:COG0410 4 LEVENLHAGYGGIHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHatdfEV--DMTVFDWMSLWMKPEDDEQSVRSVLGRL--LFS--QDDIKKSVKVLSGGEKgRML-FGKLMMQKPNV 460
Cdd:COG0410 83 VPEGR----RIfpSLTVEENLLLGAYARRDRAEVRADLERVyeLFPrlKERRRQRAGTLSGGEQ-QMLaIGRALMSRPKL 157
|
....*..
gi 490363216 461 LIMDEPT 467
Cdd:COG0410 158 LLLDEPS 164
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-476 |
1.05e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAkGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS-ENATIGYYAQD-----HA 393
Cdd:PRK13539 3 LEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 394 TDFEVDMTVFDWMSLWMK-----PEDDEQSVRSV-LGRLLfsqdDIKksVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAflggeELDIAAALEAVgLAPLA----HLP--FGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
....*....
gi 490363216 468 NHLDMESIE 476
Cdd:PRK13539 156 AALDAAAVA 164
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-484 |
1.09e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------SENAT-----IGYY 388
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddveALSARaasrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQDHATDFE------VDM------TVFDWMSlwmkpEDDEQSVRSVLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:PRK09536 83 PQDTSLSFEfdvrqvVEMgrtphrSRFDTWT-----ETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQ 156
|
170 180
....*....|....*....|....*....
gi 490363216 457 KPNVLIMDEPTNHLDM-ESIESLNMALEL 484
Cdd:PRK09536 157 ATPVLLLDEPTASLDInHQVRTLELVRRL 185
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-526 |
1.35e-13 |
|
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: 70.41 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK--------WSENA---TIGYY 388
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgedireQDPVElrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQD-----HatdfevdMTVFDWMSL------WMKPEDDEQsVRSVLGRL-LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:cd03295 81 IQQiglfpH-------MTVEENIALvpkllkWPKEKIRER-ADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 457 KPNVLIMDEPTNHLDMESIESL-----NMALELYQgTLIFVSHDREFVSSLANRIIEITPEKVTNFqGTYDEFLA 526
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLqeefkRLQQELGK-TIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEILR 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-210 |
1.36e-13 |
|
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: 70.34 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDP-----------NERLGKLKQ 71
Cdd:cd03251 4 KNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 DQFAYEeftvlDTVimghaelweikqeRERI-YSLPEMSEEEGLRVADL----EVKFGEMDGYtvESRAGElllnvgipl 146
Cdd:cd03251 84 DVFLFN-----DTV-------------AENIaYGRPGATREEVEEAARAanahEFIMELPEGY--DTVIGE--------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 147 eqhNGpmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:cd03251 135 ---RG--VKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAH 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-529 |
1.50e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.94 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 303 QNPFIRF--EQEKKLFRNALEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK- 378
Cdd:PRK11160 320 QKPEVTFptTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 379 -------WSENA---TIGYYAQdhatdfEVDM---TVFDWMSLWMKPEDDEQ---SVRSV-LGRLLfsQDD------IKK 435
Cdd:PRK11160 400 ngqpiadYSEAAlrqAISVVSQ------RVHLfsaTLRDNLLLAAPNASDEAlieVLQQVgLEKLL--EDDkglnawLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 436 SVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESiESLNMAL--ELYQG-TLIFVSH--------DREFVssLAN 504
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET-ERQILELlaEHAQNkTVLMITHrltgleqfDRICV--MDN 548
|
250 260
....*....|....*....|....*.
gi 490363216 505 -RIIEitpekvtnfQGTYDEFLAKKG 529
Cdd:PRK11160 549 gQIIE---------QGTHQELLAQQG 565
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-511 |
1.52e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIakGYEAN-TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENA-----------T 384
Cdd:PRK10247 5 SPLLQLQNV--GYLAGdAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlkpeiyrqQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQDHAT--DFEVDMTVFDWMSLWMKPedDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:PRK10247 83 VSYCAQTPTLfgDTVYDNLIFPWQIRNQQP--DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 463 MDEPTNHLDMESIESLNMALELY----QGTLIFVSHDREFVSSlANRIIEITP 511
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKDEINH-ADKVITLQP 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
319-507 |
1.63e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFkDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwsenaTIGyyaqDHATDF-- 396
Cdd:COG4161 2 SIQLKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL------NIA----GHQFDFsq 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 397 ------------EVDMtVFDWMSLW--MKPEDD--EQSVRsVLGrlLFSQDDIKKSVKVL----------------SGGE 444
Cdd:COG4161 71 kpsekairllrqKVGM-VFQQYNLWphLTVMENliEAPCK-VLG--LSKEQAREKAMKLLarlrltdkadrfplhlSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLANRII 507
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTgiTQVIVTHEVEFARKVASQVV 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-187 |
1.64e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSkplF---ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFL-----DPNE-----RLGKLKQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDiatrrRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 73 QFA-YEEFTV---LDTvimgHAelweikqereRIYSLPEmsEEEGLRVADLEVKFGEMDgyTVESRAGELllnvgiPLeq 148
Cdd:NF033858 347 AFSlYGELTVrqnLEL----HA----------RLFHLPA--AEIAARVAEMLERFDLAD--VADALPDSL------PL-- 400
|
170 180 190
....*....|....*....|....*....|....*....
gi 490363216 149 hngpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLD 187
Cdd:NF033858 401 ----------GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-228 |
1.72e-13 |
|
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: 70.60 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQF-AYEEftvldtvimgha 90
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRrAFRR------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 91 ELWEIKQERERIYSlPEMSEEEGLR--VADLEvkfgEMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGWKLRVLLAQ 168
Cdd:TIGR02769 89 DVQLVFQDSPSAVN-PRMTVRQIIGepLRHLT----SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 169 ALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-228 |
1.76e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE-----------RLGKLK 70
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 71 QDQFAYEEFTVLDTVIMGhaelweiKQERERIYSLPEMSEEEGLRVADLEVKFGEMDGYTVESRAGelllnvgipleqhn 150
Cdd:PRK10253 88 QNATTPGDITVQELVARG-------RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSG-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 151 gpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHDrhfLNMVC---THMA 223
Cdd:PRK10253 147 --------GQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQACryaSHLI 215
|
....*
gi 490363216 224 DLDYG 228
Cdd:PRK10253 216 ALREG 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-506 |
1.85e-13 |
|
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: 69.96 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEN--ATIGYYAQDHATDFE 397
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdiTNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 398 V-----DMTVFDWMS--LWMK--PEDD-EQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:cd03300 80 NyalfpHLTVFENIAfgLRLKklPKAEiKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490363216 468 NHLDMESIESLNMALELYQG----TLIFVSHDREFVSSLANRI 506
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-514 |
2.37e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAPT---SGNVFLDPNERLGKLKQDqfaye 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 78 efTVLDTVIMGHAELWEIkqereriyslPEMSEEEGLRVA-DLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPMSEV 156
Cdd:TIGR02633 75 --TERAGIVIIHQELTLV----------PELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQtlneRNSTMIIISHDRHFLNMVCTHMADLDYGG 229
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTeketeilLDIIRDLKA----HGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 230 ltvHPGNYDeymlAATQARERLLADNAKKkaqisELQSFVSRfsanasksrqatsrakqiEKIQLTEVkassrqnpfirf 309
Cdd:TIGR02633 219 ---HVATKD----MSTMSEDDIITMMVGR-----EITSLYPH------------------EPHEIGDV------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 310 eqekklfrnALEVENIAKGYEANTPLFK--DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPD-------NGRVKWS 380
Cdd:TIGR02633 257 ---------ILEARNLTCWDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfegnvfiNGKPVDI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 381 EN------ATIGYYAQDHATD---------FEVDMTVFDWMSLWMKPED--DEQSVRSVLGRLLFSQDDIKKSVKVLSGG 443
Cdd:TIGR02633 328 RNpaqairAGIAMVPEDRKRHgivpilgvgKNITLSVLKSFCFKMRIDAaaELQIIGSAIQRLKVKTASPFLPIGRLSGG 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 444 EKGRMLFGKLMMQKPNVLIMDEPTNHLDMES---IESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKV 514
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-210 |
2.70e-13 |
|
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: 67.84 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKlkqdqfayeEFTVLDTV 85
Cdd:cd03216 5 GITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GK---------EVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 imgHAelweikqERERIYSLPEMSeeeglrvadlevkFGEmdgytvesragelllnvgipleqhngpmsevapgwKLRVL 165
Cdd:cd03216 71 ---DA-------RRAGIAMVYQLS-------------VGE-----------------------------------RQMVE 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490363216 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISH 210
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRrlrAQGVAVIFISH 140
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-210 |
3.21e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 11 FGSKPLFeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklkqdqfayeefTVLDTVIMGHA 90
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---------------------RVDDTLITSTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 91 ELWEIKQERER---IYSLPE--MSEEEGLRvadlEVKFGEMD-GYT---VESRAGELLLNVGIPLEQHNGPMSEVAPGWK 161
Cdd:PRK13649 76 KNKDIKQIRKKvglVFQFPEsqLFEETVLK----DVAFGPQNfGVSqeeAEALAREKLALVGISESLFEKNPFELSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLE---QTLNERNSTMIIISH 210
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMtlfKKLHQSGMTIVLVTH 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-511 |
3.41e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.00 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGY------EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkW--SENA-------- 383
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LvrHDGGwvdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 384 ----------TIGYYAQ-----------DHATDFEVDMTVfdwmslwmKPEDDEQSVRSVLGRLlfsqdDIKKSVKVL-- 440
Cdd:COG4778 84 preilalrrrTIGYVSQflrviprvsalDVVAEPLLERGV--------DREEARARARELLARL-----NLPERLWDLpp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 441 ---SGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES----IESLNMALElyQGT-LIFVSHDREFVSSLANRIIEITP 511
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA--RGTaIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
4.05e-13 |
|
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: 68.55 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPL----FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNE---RL 66
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkePAEarrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 67 GKLKQDQFAYEEFTVldtvimghaelWEIKQERERIYSLpEMSEEEGlRVADLEVKFgEMDGYtvesragelllnvgipL 146
Cdd:cd03266 81 GFVSDSTGLYDRLTA-----------RENLEYFAGLYGL-KGDELTA-RLEELADRL-GMEEL----------------L 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 147 EQHNGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDI---DTIRWLEQTLNERNSTMIIISHDRHFLNMVC 219
Cdd:cd03266 131 DRRVGGFST---GMRQKVAIARALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLC 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-187 |
4.20e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklkqdqfayeefTVLDTV 85
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---------------------TVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 IMGHAELweikqERERIYSLP-------EMSEEEGLRVadlevkFGE---MDGYTVESRAGELLLNVGIPlEQHNGPMSE 155
Cdd:PRK13536 105 VPARARL-----ARARIGVVPqfdnldlEFTVRENLLV------FGRyfgMSTREIEAVIPSLLEFARLE-SKADARVSD 172
|
170 180 190
....*....|....*....|....*....|..
gi 490363216 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLD 187
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
320-514 |
5.33e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENATIGYY----------- 388
Cdd:PRK10253 8 LRGEQLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYaskevarrigl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 -AQDHATdfEVDMTVFDWMSLWMKP---------EDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 458
Cdd:PRK10253 86 lAQNATT--PGDITVQELVARGRYPhqplftrwrKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 459 NVLIMDEPTNHLDM-ESIESLNMALEL--YQG-TLIFVSHDREFVSSLANRIIEITPEKV 514
Cdd:PRK10253 163 AIMLLDEPTTWLDIsHQIDLLELLSELnrEKGyTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
6.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.38 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 11 FGSKPLFEnISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpneRLGklkqdqfayeeftvlDTVIMGHA 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVG---------------DIVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 91 ELWEIKQERER---IYSLPE--MSEEEGLRvadlEVKFGE----MDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGWK 161
Cdd:PRK13643 75 KQKEIKPVRKKvgvVFQFPEsqLFEETVLK----DVAFGPqnfgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEqTLNERNSTMIIISH 210
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFE-SIHQSGQTVVLVTH 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-506 |
6.24e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.25 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 313 KKLFRNALEVENIAKGYEANtPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS--ENATIGYYAQ 390
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHATDFEV-----DMTVFDWMSLWMK----PEDD-EQSVRSVLGrLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 460
Cdd:PRK11607 92 PINMMFQSyalfpHMTVEQNIAFGLKqdklPKAEiASRVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 461 LIMDEPTNHLDMESIESLNMA----LELYQGTLIFVSHDREFVSSLANRI 506
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
320-514 |
6.43e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT------------IGY 387
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHATDF-----EVDMTvFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:PRK13644 82 VFQNPETQFvgrtvEEDLA-FGPENLCLPPIEIRKRVDRALAEIGLEKYR-HRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 463 MDEPTNHLDMESIES-LNMALELYQ--GTLIFVSHDREFVSSlANRII---------EITPEKV 514
Cdd:PRK13644 160 FDEVTSMLDPDSGIAvLERIKKLHEkgKTIVYITHNLEELHD-ADRIIvmdrgkivlEGEPENV 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-211 |
6.44e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.27 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklKQDQFAYEEFTVldtvimghael 92
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----------TVGGMVLSEETV----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 93 WEIKQERERIYSLPEmSEEEGLRVADlEVKFG---------EMdgytVEsRAGELLLNVGIPLEQHNGPmSEVAPGWKLR 163
Cdd:PRK13635 77 WDVRRQVGMVFQNPD-NQFVGATVQD-DVAFGlenigvpreEM----VE-RVDQALRQVGMEDFLNREP-HRLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQtlnERNSTMIIISHD 211
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-490 |
7.58e-13 |
|
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: 67.52 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIA--KGYEAntpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENA---TIGYYAQD--- 391
Cdd:cd03231 1 LEADELTceRDGRA---LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfQRDSIARGlly 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 392 --HATDFEVDMTVFDWMSLWMKPEDDEQsVRSVLGRL-LFSQDDIkkSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTN 468
Cdd:cd03231 78 lgHAPGIKTTLSVLENLRFWHADHSDEQ-VEEALARVgLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....
gi 490363216 469 HLDMESIESL--NMALELYQGTLI 490
Cdd:cd03231 155 ALDKAGVARFaeAMAGHCARGGMV 178
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-210 |
8.20e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAPT---SGNVFLDpnerlGKLKQDQfayeefTV 81
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFE-----GEELQAS------NI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 LDT-----VIMgHAELWEIkqereriyslPEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNgPMSEV 156
Cdd:PRK13549 77 RDTeragiAII-HQELALV----------KELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT-PVGNL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNL---DIDTIRWLEQTLNERNSTMIIISH 210
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-212 |
8.31e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 69.74 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQDqfa 75
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglpPEKRnVGMVFQD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 yeeftvldtvimghaelweikqereriYSL-PEMSeeeglrVADlEVKFG-EMDGY---TVESRAGELLLNVGIpleqhn 150
Cdd:COG3842 86 ---------------------------YALfPHLT------VAE-NVAFGlRMRGVpkaEIRARVAELLELVGL------ 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 151 GPMSEVAP-----GWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHDR 212
Cdd:COG3842 126 EGLADRYPhqlsgGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-495 |
8.87e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.26 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK--------WS--ENATI-GY 387
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWSpaELARRrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQdHAT---DFEVD----MTVFDWMSLwmkPEDDEQSVRSVL---------GRlLFSQddikksvkvLSGGEKGRMLFG 451
Cdd:PRK13548 81 LPQ-HSSlsfPFTVEevvaMGRAPHGLS---RAEDDALVAAALaqvdlahlaGR-DYPQ---------LSGGEQQRVQLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 452 KLMMQ------KPNVLIMDEPTNHLDM-ESIESLNMALEL---YQGTLIFVSHD 495
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLaHQHHVLRLARQLaheRGLAVIVVLHD 200
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-211 |
9.57e-13 |
|
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: 68.44 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 4 SNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNERLGKLKQDQFA- 75
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamSRKELRELRRKKISm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 -YEEF------TVLDTVIMGhAELWEI-KQERERiyslpemseeeglrvadlevkfgemdgytvesRAGELLLNVGIPLE 147
Cdd:cd03294 107 vFQSFallphrTVLENVAFG-LEVQGVpRAEREE--------------------------------RAAEALELVGLEGW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 148 QHNGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDiDTIRWLEQTL-----NERNSTMIIISHD 211
Cdd:cd03294 154 EHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRREMQDEllrlqAELQKTIVFITHD 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
1.22e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.47 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdltalpPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 DQ--FAYeeFTVLDTVIMG-HAELWEIKQERERIYslpEMSEEEGLrvADLEVKF-GEMDGytvesragelllnvgiple 147
Cdd:COG3840 79 ENnlFPH--LTVAQNIGLGlRPGLKLTAEQRAQVE---QALERVGL--AGLLDRLpGQLSG------------------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 148 qhngpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHD 211
Cdd:COG3840 133 -----------GQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-211 |
1.62e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 67.84 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGklkqdqfayeeftvLDTVIMGHae 91
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----G--------------LDTLDEEN-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIkqeRERI---YSLPE------MSEEEglrVA----DLEVKFGEMdgytvESRAGELLLNVGipleqhngpMSE--- 155
Cdd:TIGR04520 72 LWEI---RKKVgmvFQNPDnqfvgaTVEDD---VAfgleNLGVPREEM-----RKRVDEALKLVG---------MEDfrd 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 156 VAP-----GWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQtlnERNSTMIIISHD 211
Cdd:TIGR04520 132 REPhllsgGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNK---EEGITVISITHD 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
319-507 |
1.68e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.59 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS-ENAT--------IGYYA 389
Cdd:COG3842 5 ALELENVSKRYGDVTAL-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgRDVTglppekrnVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QD-----HatdfevdMTVFD-----WMSLWMKPEDDEQSVRSVLGRLlfsqdDI----KKSVKVLSGGEKgrmlfgklmm 455
Cdd:COG3842 84 QDyalfpH-------LTVAEnvafgLRMRGVPKAEIRARVAELLELV-----GLeglaDRYPHQLSGGQQ---------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 456 Q----------KPNVLIMDEPTNHLDMESIESlnMALELYQ------GTLIFVSHDREFVSSLANRII 507
Cdd:COG3842 142 QrvalaralapEPRVLLLDEPLSALDAKLREE--MREELRRlqrelgITFIYVTHDQEEALALADRIA 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
1.73e-12 |
|
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: 69.70 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAY------EEFTVLDTV 85
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRrvsvcaQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 IMGHAELweikqereriySLPEMSEEEGLRVadLE-VKFGEMdgytVESRAGELLLNVGipleqhnGPMSEVAPGWKLRV 164
Cdd:TIGR02868 425 VRENLRL-----------ARPDATDEELWAA--LErVGLADW----LRALPDGLDTVLG-------EGGARLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN--ERNSTMIIISHD 211
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLaaLSGRTVVLITHH 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-510 |
2.03e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 323 ENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNG----------RVKWSE----NATIGYY 388
Cdd:PRK10908 5 EHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghditRLKNREvpflRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQDHatDFEVDMTVFDWMSLWM-----KPEDDEQSVRSVLGR--LLfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 461
Cdd:PRK10908 85 FQDH--HLLMDRTVYDNVAIPLiiagaSGDDIRRRVSAALDKvgLL---DKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 462 IMDEPTNHLDMESIESLNMALELYQG---TLIFVSHDREFVSSLANRIIEIT 510
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
2.42e-12 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 69.30 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNERLGK----LKQDqfayeeft 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDgadlkqwDRETFGKhigyLPQD-------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vldtvimghAELWE--IKQERERIYSLPEmSEE--EGLRVADL-EVKFGEMDGYTVESRAGelllnvGIPLeqhngpmse 155
Cdd:TIGR01842 401 ---------VELFPgtVAENIARFGENAD-PEKiiEAAKLAGVhELILRLPDGYDTVIGPG------GATL--------- 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 156 vAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE---RNSTMIIISHDRHFLNMV 218
Cdd:TIGR01842 456 -SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlkaRGITVVVITHRPSLLGCV 520
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
2.58e-12 |
|
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: 66.59 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQDQFAYEEFTVLDTVIMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 89 HAELWEIKQERERiySLPEMSEeeglrvadlevkfgemdgytvesragelLLNVGIPLEQHNGPMSEvapGWKLRVLLAQ 168
Cdd:cd03299 96 LKKRKVDKKEIER--KVLEIAE----------------------------MLGIDHLLNRKPETLSG---GEQQRVAIAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490363216 169 ALFADPDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHD 211
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-506 |
2.70e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK----------WSENATIGYY 388
Cdd:PRK13536 41 AIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQDHATDFEvdMTVFDWMSLW-----MKPEDDEQSVRSVLGrllFSQDDIKKSVKV--LSGGEKGRMLFGKLMMQKPNVL 461
Cdd:PRK13536 120 PQFDNLDLE--FTVRENLLVFgryfgMSTREIEAVIPSLLE---FARLESKADARVsdLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 462 IMDEPTN-------HLDMESIESLnmaleLYQG-TLIFVSHDREFVSSLANRI 506
Cdd:PRK13536 195 ILDEPTTgldpharHLIWERLRSL-----LARGkTILLTTHFMEEAERLCDRL 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
3.02e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.19 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD---------PNERLGKLKQDQFA 75
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhaRDRKVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTVLDTVIMGHAELweikQERERiyslPemseeeglrvadlevkfgemDGYTVESRAGELLLNVGIPLEQHNGPmSE 155
Cdd:PRK10851 86 FRHMTVFDNIAFGLTVL----PRRER----P--------------------NAAAIKAKVTQLLEMVQLAHLADRYP-AQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDR 212
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-228 |
3.26e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFL--DP--------NERLGKLKQDQFA 75
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvpsrarhaRQRVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTVLDTV-IMGHAELWEIKQERERIYSLPEMSEeeglrvadlevkfgemdgytVESRAgelllnvgipleqhNGPMS 154
Cdd:PRK13537 92 DPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAK--------------------LENKA--------------DAKVG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT--IRWLE-QTLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:PRK13537 138 ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWERlRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
318-514 |
3.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.03 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEAN-----TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV------------KWS 380
Cdd:PRK13633 3 EMIKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 381 ENATIGYYAQDH-----ATDFEVDMTvFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMM 455
Cdd:PRK13633 83 IRNKAGMVFQNPdnqivATIVEEDVA-FGPENLGIPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 456 QKPNVLIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSH--------DREFVSSLANRIIEITPEKV 514
Cdd:PRK13633 161 MRPECIIFDEPTAMLDpsgrrevVNTIKELN---KKYGITIILITHymeeaveaDRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-254 |
4.01e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSG-----NVFLDPNERLGKLK----- 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 71 ---QDQFAYEEF------TVLDTVImghaelweikqereriyslpemseeEGLRVADLEVKfgemdgYTVESRAGELLLN 141
Cdd:PRK11264 83 lrqHVGFVFQNFnlfphrTVLENII-------------------------EGPVIVKGEPK------EEATARARELLAK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 142 VGIPLEQHNGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqTLNERNSTMIIISHDRHF 214
Cdd:PRK11264 132 VGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEMSF 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490363216 215 LNMVCTHMADLDyGGLTVHPGNYDEYMLAATQARERLLAD 254
Cdd:PRK11264 207 ARDVADRAIFMD-QGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-210 |
4.46e-12 |
|
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: 64.64 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--PNERLGKLKQDQFAyeeft 80
Cdd:cd03247 4 NNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDgvPVSDLEKALSSLIS----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDtvimghaelweikqerERIYSLpemseeeglrvadlevkfgemdgytvesrAGELLLNVGIPLeqhngpmsevAPGW 160
Cdd:cd03247 79 VLN----------------QRPYLF-----------------------------DTTLRNNLGRRF----------SGGE 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:cd03247 104 RQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvlKDKTLIWITH 155
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
320-509 |
4.54e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEA---NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS---------------E 381
Cdd:PRK11629 6 LQCDNLCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 382 NATIGYYAQDH--ATDFEVDMTVFdwMSLW---MKPEDDEQSVRSVLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQ 456
Cdd:PRK11629 86 NQKLGFIYQFHhlLPDFTALENVA--MPLLigkKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 457 KPNVLIMDEPTNHLDM---ESIESLNMALELYQGT-LIFVSHDREFVSSLaNRIIEI 509
Cdd:PRK11629 163 NPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEM 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
320-474 |
4.61e-12 |
|
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: 65.13 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTP-LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS--ENATIGYYA-QDHATD 395
Cdd:cd03369 7 IEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgiDISTIPLEDlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 396 FEVDMTVFDwmslwmkpeddeQSVRSVLGRL-LFSQDDIKKSVKV------LSGGEKGRMLFGKLMMQKPNVLIMDEPTN 468
Cdd:cd03369 87 IPQDPTLFS------------GTIRSNLDPFdEYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
....*.
gi 490363216 469 HLDMES 474
Cdd:cd03369 155 SIDYAT 160
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-210 |
4.71e-12 |
|
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: 66.02 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLK----QDQFAY--EEFTVLDTVImg 88
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLNlrwlRSQIGLvsQEPVLFDGTI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 89 haelweikqeRERI-YSLPEMSEEEGLRVA------DLEVKFgeMDGYtvESRAGElllnvgipleqhNGpmSEVAPGWK 161
Cdd:cd03249 94 ----------AENIrYGKPDATDEEVEEAAkkanihDFIMSL--PDGY--DTLVGE------------RG--SQLSGGQK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRamKGRTTIVIAH 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
5.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE-----------RLGKLKQ 71
Cdd:PRK13632 11 ENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlkeirkKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 D---QFAyeEFTVLDTVIMGhaeLWEIKQERERIYSLpemseeeglrVADLEVKFGeMDGYtvesragelllnvgIPLEQ 148
Cdd:PRK13632 91 NpdnQFI--GATVEDDIAFG---LENKKVPPKKMKDI----------IDDLAKKVG-MEDY--------------LDKEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 149 HNgpmseVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13632 141 QN-----LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
5.62e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAYEEFTV-------LDT 84
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRKAFRRDIqmvfqdsISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAELWEIkqeRERIYSLPEMSEEEGLRvadlevkfgemdgytvesRAGELLLNVGIPLEQHNGPMSEVAPGWKLRV 164
Cdd:PRK10419 102 VNPRKTVREII---REPLRHLLSLDKAERLA------------------RASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 165 LLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGL 230
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-506 |
5.74e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGY---EANtplfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT----------- 384
Cdd:COG3845 5 ALELRGITKRFggvVAN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprdaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 -IGYYAQdHATDFEVdMTVFDWMSLWMKPED----DEQSVRSVLGRLlfSQD-----DIKKSVKVLSGGEKGR--MLfgK 452
Cdd:COG3845 81 gIGMVHQ-HFMLVPN-LTVAENIVLGLEPTKggrlDRKAARARIREL--SERygldvDPDAKVEDLSVGEQQRveIL--K 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 453 LMMQKPNVLIMDEPTNHLDMESIESL-----NMALElyQGTLIFVSHD-REfVSSLANRI 506
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELfeilrRLAAE--GKSIIFITHKlRE-VMAIADRV 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-507 |
6.10e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKgYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRvkwsenatIGYYAQD----HAT 394
Cdd:PRK10851 2 SIEIANIKK-SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH--------IRFHGTDvsrlHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 DFEV-----------DMTVFDWMSLWMkpeddeqsvrSVLGRL-LFSQDDIKKSVKVL-----------------SGGEK 445
Cdd:PRK10851 73 DRKVgfvfqhyalfrHMTVFDNIAFGL----------TVLPRReRPNAAAIKAKVTQLlemvqlahladrypaqlSGGQK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 446 GRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMAL----ELYQGTLIFVSHDREFVSSLANRII 507
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVV 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-211 |
6.33e-12 |
|
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: 65.34 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQDqfay 76
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpPHKRpVNTVFQN---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 eeftvldtvimghaelweikqereriYSL-PEMSEEE----GLRVAdlevkfgEMDGYTVESRAGELLLNVGipLEQHNG 151
Cdd:cd03300 81 --------------------------YALfPHLTVFEniafGLRLK-------KLPKAEIKERVAEALDLVQ--LEGYAN 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 152 PM-SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTL----NERNSTMIIISHD 211
Cdd:cd03300 126 RKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrlqKELGITFVFVTHD 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-466 |
7.01e-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: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEN------------ATIGY 387
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDhATDFEvDMTVFDWMSLWMK-PEDDEQSVRSVLGRLL--FSQDDIKKSVKV-LSGGEKGRMLFGKLMMQKPNVLIM 463
Cdd:cd03218 80 LPQE-ASIFR-KLTVEENILAVLEiRGLSKKEREEKLEELLeeFHITHLRKSKASsLSGGERRRVEIARALATNPKFLLL 157
|
...
gi 490363216 464 DEP 466
Cdd:cd03218 158 DEP 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
8.36e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD------PNERLGKLKQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 75 AYEEFTVLDTVIMGhaelweikqereriYSLPEMSEEEGlrvadlevkfgemdgytvESRAGELLLNVGIPlEQHNGPMS 154
Cdd:PRK11248 81 LLPWRNVQDNVAFG--------------LQLAGVEKMQR------------------LEIAHQMLKKVGLE-GAEKRYIW 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTiRWLEQTL-----NERNSTMIIISHD 211
Cdd:PRK11248 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT-REQMQTLllklwQETGKQVLLITHD 188
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-211 |
1.07e-11 |
|
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: 64.24 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 27 GNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftvlDTVIMGHAELWEIKQERERI---- 102
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN---------------------GTVLFDSRKKINLPPQQRKIglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 103 --YSL-PEMSEEE----GLRV-ADLEVKFgemdgytvesRAGELLLNVGI-PLEQHngPMSEVAPGWKLRVLLAQALFAD 173
Cdd:cd03297 82 qqYALfPHLNVREnlafGLKRkRNREDRI----------SVDELLDLLGLdHLLNR--YPAQLSGGEKQRVALARALAAQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490363216 174 PDILLLDEPTNNLDIDT----IRWLEQTLNERNSTMIIISHD 211
Cdd:cd03297 150 PELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-210 |
1.32e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 64.21 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 8 TMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG---DLAPTSGNVFLDPNERLGKLKQDQFAY-------- 76
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQKCVAYvrqddill 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 EEFTVLDTV-IMGHAELWEIKQERERiyslPEMSEEEGLR-VADLEVkfgemdgytvesrAGELLLNVGIpleqhngpms 154
Cdd:cd03234 94 PGLTVRETLtYTAILRLPRKSSDAIR----KKRVEDVLLRdLALTRI-------------GGNLVKGISG---------- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 155 evapGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQtLNERNSTMIIISH 210
Cdd:cd03234 147 ----GERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQ-LARRNRIVILTIH 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
1.48e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.06 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSG-------NVFLDPNERLGKLKQDQFAYeeftvldtvimgha 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLRREHFGF-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 91 elweIKQereRIYSLPEMSEEEGLRV----ADLEVKfgemdgyTVESRAGELLLNVGIPLEQHNGPmSEVAPGWKLRVLL 166
Cdd:PRK10535 91 ----IFQ---RYHLLSHLTAAQNVEVpavyAGLERK-------QRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490363216 167 AQALFADPDILLLDEPTNNLD----IDTIRWLEQtLNERNSTMIIISHD 211
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
320-507 |
1.52e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.12 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSenatigyyAQDHA------ 393
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD--------GQDIThvpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 394 ----TDFEV-----DMTVFDWMS--LWMK--PEDD-EQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 459
Cdd:PRK09452 86 rhvnTVFQSyalfpHMTVFENVAfgLRMQktPAAEiTPRVMEAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 460 VLIMDEPTNHLDMESieSLNMALELYQ-----G-TLIFVSHDREFVSSLANRII 507
Cdd:PRK09452 165 VLLLDESLSALDYKL--RKQMQNELKAlqrklGiTFVFVTHDQEEALTMSDRIV 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-210 |
1.62e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAYeeft 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vldtviMGHAElwEIKqereriyslPEMSEEEGLRV-ADLevkFGemdgyTVESRAGELLLNVGIPLEQHNgPMSEVAPG 159
Cdd:PRK13539 78 ------LGHRN--AMK---------PALTVAENLEFwAAF---LG-----GEELDIAAALEAVGLAPLAHL-PFGYLSAG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 160 WKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLE---QTLNERNSTMIIISH 210
Cdd:PRK13539 132 QKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAeliRAHLAQGGIVIAATH 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-528 |
1.65e-11 |
|
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: 67.24 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 333 TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS------------------ENATIG-------Y 387
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSgrisfspqtswimpgtikDNIIFGlsydeyrY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDHATDFEVDMTVFdwmslwmkPEDDeqsvRSVLGrllfsqddikKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:TIGR01271 519 TSVIKACQLEEDIALF--------PEKD----KTVLG----------EGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 468 NHLDM----ESIESLNMALeLYQGTLIFVSHDREFVSSlANRIIeITPEKVTNFQGTYDEFLAKK 528
Cdd:TIGR01271 577 THLDVvtekEIFESCLCKL-MSNKTRILVTSKLEHLKK-ADKIL-LLHEGVCYFYGTFSELQAKR 638
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-210 |
1.69e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFA-------YEE 78
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKLAAqlgigiiYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 79 FTVLDtvimghaelweikqereriyslpEMSEEEGLRVADLEVK--FGE--MDGYTVESRAGELLLNVGIPLEQhNGPMS 154
Cdd:PRK09700 89 LSVID-----------------------ELTVLENLYIGRHLTKkvCGVniIDWREMRVRAAMMLLRVGLKVDL-DEKVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNL---DIDTIRWLEQTLNERNSTMIIISH 210
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
320-526 |
1.86e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.01 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEaNTPLfkDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsENATIGYYA---------- 389
Cdd:COG3840 2 LRLDDLTYRYG-DFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTALPpaerpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 QDHaTDFEvDMTVFDWMSLWMKP-----EDDEQSVRSVLGRL-LFSQDDIKKSVkvLSGGEKGR-MLFGKLMMQKPnVLI 462
Cdd:COG3840 78 QEN-NLFP-HLTVAQNIGLGLRPglkltAEQRAQVEQALERVgLAGLLDRLPGQ--LSGGQRQRvALARCLVRKRP-ILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 463 MDEPTNHLD------MesiesLNMALEL---YQGTLIFVSHDREFVSSLANRIIEITPEKVTnFQGTYDEFLA 526
Cdd:COG3840 153 LDEPFSALDpalrqeM-----LDLVDELcreRGLTVLMVTHDPEDAARIADRVLLVADGRIA-ADGPTAALLD 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
318-507 |
1.94e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSE---NATIGYYAQD--- 391
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVL-HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitiDTARSLSQQKgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 392 HATDFEVDMtVFDWMSLW---------------MKPEDDEQSV---RSVLGRL-LFSQDDikKSVKVLSGGEKGRMLFGK 452
Cdd:PRK11264 81 RQLRQHVGF-VFQNFNLFphrtvleniiegpviVKGEPKEEATaraRELLAKVgLAGKET--SYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 453 LMMQKPNVLIMDEPTNHLDMESI-ESLNMALELYQG--TLIFVSHDREFVSSLANRII 507
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVgEVLNTIRQLAQEkrTMVIVTHEMSFARDVADRAI 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
318-507 |
2.52e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEANT--PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV-----------KWSENAT 384
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQDHATDFeVDMTVFDWMSLWMK----PEDDEQS-VRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 459
Cdd:PRK13650 83 IGMVFQNPDNQF-VGATVEDDVAFGLEnkgiPHEEMKErVNEAL-ELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 460 VLIMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVsSLANRII 507
Cdd:PRK13650 161 IIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-210 |
2.59e-11 |
|
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: 63.40 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPN-----------ERLGKLKQDQFAYEEfTVL 82
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 83 DTVIMGHAelwEIKQERERiyslpEMSEEEGlrvADLEVKFGEMDGYTVESRAGELLlnvgipleqhngpmSEvapGWKL 162
Cdd:cd03254 95 ENIRLGRP---NATDEEVI-----EAAKEAG---AHDFIMKLPNGYDTVLGENGGNL--------------SQ---GERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 163 RVLLAQALFADPDILLLDEPTNNLDIDTirwlEQTLNE------RNSTMIIISH 210
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTET----EKLIQEaleklmKGRTSIIIAH 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-230 |
3.19e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklkqdqfayeeftvldtvimghaelwEIkqe 98
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----------------------------------EV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 99 RERIYSL--------PEMSEEE---------GLRVADLEVKFGEmdgytVESRAGelllnvgipLEQH-NGPM----Sev 156
Cdd:COG1134 86 NGRVSALlelgagfhPELTGREniylngrllGLSRKEIDEKFDE-----IVEFAE---------LGDFiDQPVktysS-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 157 apGWKLRVLLAQALFADPDILLLDEptnNL---DID----TIRWLEQtLNERNSTMIIISHDRHFLNMVCTHMADLDYGG 229
Cdd:COG1134 150 --GMRARLAFAVATAVDPDILLVDE---VLavgDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
.
gi 490363216 230 L 230
Cdd:COG1134 224 L 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-218 |
3.68e-11 |
|
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: 62.54 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLAPTSGNVFLD--------PNERlgklkqdqf 74
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKgeditdlpPEER--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 75 ayeeftvldtVIMGHAELWeikQERERIyslpemseeEGLRVADLeVKFgemdgytvesragellLNVGIpleqhngpms 154
Cdd:cd03217 75 ----------ARLGIFLAF---QYPPEI---------PGVKNADF-LRY----------------VNEGF---------- 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 155 evAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISHDRHFLNMV 218
Cdd:cd03217 106 --SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINklrEEGKSVLIITHYQRLLDYI 170
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-210 |
5.02e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 9 MQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKlkqdqfayeeftvldtvimg 88
Cdd:PRK13637 16 TPFEKKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 89 HAELWEIKQERERIYSLPEMSEEEGLRVADLE---VKFGEMDGyTVESRAGELLLNVGIPLEQH--NGPMsEVAPGWKLR 163
Cdd:PRK13637 75 KVKLSDIRKKVGLVFQYPEYQLFEETIEKDIAfgpINLGLSEE-EIENRVKRAMNIVGLDYEDYkdKSPF-ELSGGQKRR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDI---DTIRWLEQTLNER-NSTMIIISH 210
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKEyNMTIILVSH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-211 |
5.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSgnvflDPNERLgklkqdqfayeeftVLDTVIMGHAELW 93
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKI--------------TVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 EIKQERERIYSLPEmSEEEGLRVADlEVKFGemdgytVESRA----------GELLLNVGIpLEQHNGPMSEVAPGWKLR 163
Cdd:PRK13640 81 DIREKVGIVFQNPD-NQFVGATVGD-DVAFG------LENRAvprpemikivRDVLADVGM-LDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEqtlNERNSTMIIISHD 211
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDpagkeqiLKLIRKLK---KKNNLTVISITHD 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-212 |
5.35e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNErlgklkqdqfayeeftVLDTV 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED----------------VTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 ImghaelweikQERE-----RIYSL-PEMSEEE----GLR---VADLEVKfgemdgytveSRAGELLLNVGIP------L 146
Cdd:PRK11432 75 I----------QQRDicmvfQSYALfPHMSLGEnvgyGLKmlgVPKEERK----------QRVKEALELVDLAgfedryV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 147 EQHNGpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDI-------DTIRWLEQTLnerNSTMIIISHDR 212
Cdd:PRK11432 135 DQISG-------GQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQF---NITSLYVTHDQ 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
5.71e-11 |
|
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: 65.15 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDP-----------NERLGKL 69
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEfTVLDTVIMGhaelweikqereriySLPEMSEEEGLRVADL-EVKfgemdgytveSRAGELLLNVGIPLEQ 148
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLG---------------AKENVSQDEIWAACEIaEIK----------DDIENMPLGYQTELSE 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 149 HNGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDT-IRWLEQTLNERNSTMIIISH 210
Cdd:TIGR01193 608 EGSSISG---GQKQRIALARALLTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH 667
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
319-507 |
6.23e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------SENAT-----IG 386
Cdd:PRK13632 7 MIKVENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitisKENLKeirkkIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQDHATDFeVDMTVFDWMSLW----------MKPEDDEQSVRSVLGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:PRK13632 87 IIFQNPDNQF-IGATVEDDIAFGlenkkvppkkMKDIIDDLAKKVGMEDYL------DKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 457 KPNVLIMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVsSLANRII 507
Cdd:PRK13632 160 NPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-211 |
6.33e-11 |
|
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: 61.89 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVF--------LDPNER-LGKLKQDQFAY 76
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 EEFTVLDTVIMGHaelweikqeRERIYSLPEMSEeeglRVadlevkfgemdgytveSRAGELLlnvGIPLEQHNGPmSEV 156
Cdd:cd03301 85 PHMTVYDNIAFGL---------KLRKVPKDEIDE----RV----------------REVAELL---QIEHLLDRKP-KQL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-507 |
7.80e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFK--------DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsENATIGYYAQD 391
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKhqhqtvlnNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 392 HATDF--EVDMTVFDWMSLWmkpeDDEQSVRSVLG---RLLFSQDDIKKSVKV--------------------LSGGEKG 446
Cdd:PRK10419 83 QRKAFrrDIQMVFQDSISAV----NPRKTVREIIReplRHLLSLDKAERLARAsemlravdlddsvldkrppqLSGGQLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 447 RMLFGKLMMQKPNVLIMDEPTNHLDM---ESIESLNMALELYQGT-LIFVSHDREFVSSLANRII 507
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVM 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-239 |
7.88e-11 |
|
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: 62.12 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNErLGKL------KQDQFAYEEFTVLDTVIMGHAE 91
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD-LALAdpawlrRQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIKQERERIyslpemseEEGLRVADLEVKFGEM-DGYtvESRAGElllnvgipleqhNGpmSEVAPGWKLRVLLAQAL 170
Cdd:cd03252 98 LADPGMSMERV--------IEAAKLAGAHDFISELpEGY--DTIVGE------------QG--AGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 171 FADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDrhfLNMV-CTHMADLDYGGLTVHPGNYDE 239
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDicAGRTVIIIAHR---LSTVkNADRIIVMEKGRIVEQGSHDE 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-210 |
8.11e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.12 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpneRLGklkqdqfayeeftvlDTVIMGHAELWEIKQE 98
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV------TIG---------------ERVITAGKKNKKLKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 99 RER---IYSLPE--MSEEEGLRvadlEVKFGEMD-GYTVE---SRAGELLLNVGIPLE-QHNGPMsEVAPGWKLRVLLAQ 168
Cdd:PRK13634 84 RKKvgiVFQFPEhqLFEETVEK----DICFGPMNfGVSEEdakQKAREMIELVGLPEElLARSPF-ELSGGQMRRVAIAG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 169 ALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISH 210
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-210 |
8.34e-11 |
|
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: 62.18 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER----LGKL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpMHKRarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDTvIMGHAELWEiKQERERIYSLPEMSEEEGLrvadlevkfgemdgytvesraGELLLNVGIPLeqh 149
Cdd:cd03218 81 PQEASIFRKLTVEEN-ILAVLEIRG-LSKKEREEKLEELLEEFHI---------------------THLRKSKASSL--- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 150 ngpmsevAPGWKLRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQTLNERNSTMIIISH 210
Cdd:cd03218 135 -------SGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDH 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-509 |
1.23e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 337 KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKwsenaTIGYYAQDHATDFEVDMT-VFDWMS-LW--MKP 412
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPFKRRKEFARRIGvVFGQRSqLWwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 413 ED-----------DEQSVRSVLGRL--LFSQDDI-KKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES---- 474
Cdd:COG4586 114 IDsfrllkaiyriPDAEYKKRLDELveLLDLGELlDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeai 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 490363216 475 ---IESLNmalELYQGTLIFVSHDREFVSSLANRIIEI 509
Cdd:COG4586 194 refLKEYN---RERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
319-504 |
1.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTP-----LFkDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK--------WSENATI 385
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegraLF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitsTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQDHATDFE------VDMTV-----FDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLM 454
Cdd:PRK13649 81 KQIRKKVGLVFQfpesqlFEETVlkdvaFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 455 MQKPNVLIMDEPTNHLDMESIESLnMAL--ELYQG--TLIFVSHDREFVSSLAN 504
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKEL-MTLfkKLHQSgmTIVLVTHLMDDVANYAD 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
332-530 |
1.63e-10 |
|
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: 61.40 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTL-------VGELTPDNGRVK------WSENatIGYYAQDHATdFev 398
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVDIRdlnlrwLRSQ--IGLVSQEPVL-F-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 DMTVFDWMSLWMKPEDDEQSVRSVlgRLLFSQDDIKK-----------SVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:cd03249 90 DGTIAENIRYGKPDATDEEVEEAA--KKANIHDFIMSlpdgydtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 468 NHLDMESIESLNMALE-LYQG-TLIFVSHdRefVSSL--ANRIIEITPEKVTNfQGTYDEFLAKKGI 530
Cdd:cd03249 168 SALDAESEKLVQEALDrAMKGrTTIVIAH-R--LSTIrnADLIAVLQNGQVVE-QGTHDELMAQKGV 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
329-507 |
1.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 329 YEANTPL----FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSE---------------NATIGYYA 389
Cdd:PRK13646 12 YQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 Q-DHATDFEVDM---TVFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDE 465
Cdd:PRK13646 92 QfPESQLFEDTVereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 466 PTNHLDMES---IESLNMALELYQG-TLIFVSHDREFVSSLANRII 507
Cdd:PRK13646 172 PTAGLDPQSkrqVMRLLKSLQTDENkTIILVSHDMNEVARYADEVI 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
320-466 |
1.80e-10 |
|
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: 61.14 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS-ENAT-----------IGY 387
Cdd:TIGR04406 2 LVAENLIKSYKKRK-VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDhATDFEvDMTVFDWMS--LWMKPEDDEQSVRSVLGRLL--FSQDDIKKSVKV-LSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:TIGR04406 81 LPQE-ASIFR-KLTVEENIMavLEIRKDLDRAEREERLEALLeeFQISHLRDNKAMsLSGGERRRVEIARALATNPKFIL 158
|
....
gi 490363216 463 MDEP 466
Cdd:TIGR04406 159 LDEP 162
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-239 |
2.05e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKLKQdqFAYEEFTVlDTVIMGHaelw 93
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD-----GKVLY--FGKDIFQI-DAIKLRK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 EIKQERERIYSLPEMSEEEGlrVADLEVKFGEMDGYTVESRAGELLLNVGIPLEQH---NGPMSEVAPGWKLRVLLAQAL 170
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDN--IAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 171 FADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFLNMVCTHMADLdYGGLTVHPGNYDE 239
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITElkNEIAIVIVSHNPQQVARVADYVAFL-YNGELVEWGSSNE 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-211 |
2.70e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 61.29 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKlkqdqfayeeftvlDTVimghaelW 93
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-GDLLTE--------------ENV-------W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 EIKQERERIYSLPEmSEEEGLRVADlEVKFG----EMDGYTVESRAGELLLNVGIPLEQHNGPmSEVAPGWKLRVLLAQA 169
Cdd:PRK13650 78 DIRHKIGMVFQNPD-NQFVGATVED-DVAFGlenkGIPHEEMKERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 170 LFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-210 |
2.98e-10 |
|
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: 60.20 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNV--------FLDPNER-LGKLKQDQFA 75
Cdd:cd03298 4 DKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtAAPPADRpVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTVLDTVIMGhaelweikqereriyslpemseeeglRVADLevKFGEMDGYTVESRAGElllnVGIPLEQHNGPmSE 155
Cdd:cd03298 82 FAHLTVEQNVGLG--------------------------LSPGL--KLTAEDRQAIEVALAR----VGLAGLEKRLP-GE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN----ERNSTMIIISH 210
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLdlhaETKMTVLMVTH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-474 |
3.76e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFKdVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDN---------GRVKWSEN-------- 382
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHA-VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 383 --ATIGYYAQDHatDFEVDMTVFD------------WMSL--WMKPEDDEQSVRSV--LGRLLFSQddikKSVKVLSGGE 444
Cdd:PRK09984 84 srANTGYIFQQF--NLVNRLSVLEnvligalgstpfWRTCfsWFTREQKQRALQALtrVGMVHFAH----QRVSTLSGGQ 157
|
170 180 190
....*....|....*....|....*....|
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDMES 474
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-509 |
4.00e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.97 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSEN----------ATIGYY 388
Cdd:PRK13537 7 PIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQ--DHATDFEV--DMTVFD-WMSLwmkpedDEQSVRSVLGRLL-FSQDDIKKSVKV--LSGGEKGRMLFGKLMMQKPNV 460
Cdd:PRK13537 86 PQfdNLDPDFTVreNLLVFGrYFGL------SAAAARALVPPLLeFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 461 LIMDEPTN-------HLDMESIESLnmaleLYQG-TLIFVSHDREFVSSLANRIIEI 509
Cdd:PRK13537 160 LVLDEPTTgldpqarHLMWERLRSL-----LARGkTILLTTHFMEEAERLCDRLCVI 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
320-509 |
4.11e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGY---EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNG--RVKWSENATIG-------- 386
Cdd:PRK10535 5 LELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVATLDadalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 ----------YYAQDHAT---DFEVDmtvfdwmSLWMKPEDDEQSVRSV--LGRLLFSqDDIKKSVKVLSGGEKGRMLFG 451
Cdd:PRK10535 85 rehfgfifqrYHLLSHLTaaqNVEVP-------AVYAGLERKQRLLRAQelLQRLGLE-DRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 452 KLMMQKPNVLIMDEPTNHLDMESIESLnMALeLYQ-----GTLIFVSHDREfVSSLANRIIEI 509
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEV-MAI-LHQlrdrgHTVIIVTHDPQ-VAAQAERVIEI 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-228 |
4.84e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 17 FENISVKFGGGNR-----------------YGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQdqfayeef 79
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD-GVDLTALSE-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 tvldtvimghAELWeikQERERI------YSLpeMSEeeglR-VAD-----LEVkfgemDGYT---VESRAGELLLNVGI 144
Cdd:COG1135 75 ----------RELR---AARRKIgmifqhFNL--LSS----RtVAEnvalpLEI-----AGVPkaeIRKRVAELLELVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 145 PLEQHNGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IrwLE--QTLNER-NSTMIIISHDRHFLNMV 218
Cdd:COG1135 131 SDKADAYP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsI--LDllKDINRElGLTIVLITHEMDVVRRI 207
|
250
....*....|
gi 490363216 219 CTHMADLDYG 228
Cdd:COG1135 208 CDRVAVLENG 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
330-507 |
5.37e-10 |
|
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: 59.02 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 330 EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWseNATIGYYAQdhaTDFEVDMTVFDWMsLW 409
Cdd:cd03250 15 QETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQ---EPWIQNGTIRENI-LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 410 MKPEdDEQSVRSVLGRLLFSQDdikksVKVLSG------GEKGRMLFGKlmmQK------------PNVLIMDEPTNHLD 471
Cdd:cd03250 89 GKPF-DEERYEKVIKACALEPD-----LEILPDgdlteiGEKGINLSGG---QKqrislaravysdADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 472 MES----IESLNMALELYQGTLIFVSHDREFVSSlANRII 507
Cdd:cd03250 160 AHVgrhiFENCILGLLLNNKTRILVTHQLQLLPH-ADQIV 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
316-471 |
5.67e-10 |
|
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: 58.72 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 316 FRNaLEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTP--DNGRV--------KWSENATI 385
Cdd:cd03213 6 FRN-LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQD---HATdfevdMTVFDwmslwmkpeddeqsvrsvlgRLLFSqddikKSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:cd03213 85 GYVPQDdilHPT-----LTVRE--------------------TLMFA-----AKLRGLSGGERKRVSIALELVSNPSLLF 134
|
....*....
gi 490363216 463 MDEPTNHLD 471
Cdd:cd03213 135 LDEPTSGLD 143
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-511 |
6.21e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAqDHATDFEV 398
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 D-----MTVFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDI----KKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNH 469
Cdd:PRK11248 79 EgllpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLegaeKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490363216 470 LDMESIESLN-MALELYQGT---LIFVSHDREFVSSLANRIIEITP 511
Cdd:PRK11248 159 LDAFTREQMQtLLLKLWQETgkqVLLITHDIEEAVFMATELVLLSP 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
6.29e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 32 LIGANGSGKSTFMKILGGDLAPTSGNVFLdPNERLGKLKQDQ----------FAYEEFTVLDTVimghaelweikQERER 101
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSL-VGQPLHQMDEEAraklrakhvgFVFQSFMLIPTL-----------NALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 102 IySLPEMseeegLRvadlevkfGEMDGYTvESRAGELLLNVGIPLEQHNGPmSEVAPGWKLRVLLAQALFADPDILLLDE 181
Cdd:PRK10584 109 V-ELPAL-----LR--------GESSRQS-RNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....
gi 490363216 182 PTNNLDIDT---IRWLEQTLN-ERNSTMIIISHD 211
Cdd:PRK10584 173 PTGNLDRQTgdkIADLLFSLNrEHGTTLILVTHD 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
342-495 |
6.47e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 342 MLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGR----VKWSEnaTIGYYA----QDHATDF-EVDMTVFdwmslwMKP 412
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeePSWDE--VLKRFRgtelQNYFKKLyNGEIKVV------HKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 413 EDDEQSVRSVLGR---LLFSQDD----------------IKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDME 473
Cdd:PRK13409 167 QYVDLIPKVFKGKvreLLKKVDErgkldevverlgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180
....*....|....*....|....*.
gi 490363216 474 siESLNMAL---ELYQG-TLIFVSHD 495
Cdd:PRK13409 247 --QRLNVARlirELAEGkYVLVVEHD 270
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
337-494 |
7.19e-10 |
|
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: 58.69 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 337 KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVG--ELTPDNGRVKwsenatigYYAQDhATDFEVD----MTVFdwMSLWM 410
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL--------FKGED-ITDLPPEerarLGIF--LAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 411 KPEDDEQSVRSVLgrllfsqddikKSVKV-LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQG-- 487
Cdd:cd03217 86 PPEIPGVKNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeg 154
|
....*...
gi 490363216 488 -TLIFVSH 494
Cdd:cd03217 155 kSVLIITH 162
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-211 |
7.24e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.90 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 26 GGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQFAY----EE----FTVL--DTVIM---GHAEL 92
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpqsEEvdwsFPVLveDVVMMgryGHMGW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 93 WEIKQERERiyslpEMSEEEGLRVADLEVKFGEMdgytvesraGELllnvgipleqhngpmsevAPGWKLRVLLAQALFA 172
Cdd:PRK15056 112 LRRAKKRDR-----QIVTAALARVDMVEFRHRQI---------GEL------------------SGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490363216 173 DPDILLLDEPTNNLDIDT---IRWLEQTLNERNSTMIIISHD 211
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-211 |
7.76e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPN--------------ERLGKLKQDQFAYE 77
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvrKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 78 EFTVLDTV---IMGHAELWEikqerERIYSLPEMS-EEEGLRvadlevkfgemdgytvesRAGELLlnvgiPleqhngpm 153
Cdd:PRK11831 98 DMNVFDNVaypLREHTQLPA-----PLLHSTVMMKlEAVGLR------------------GAAKLM-----P-------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNS----TMIIISHD 211
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-504 |
8.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.67 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTL--VGELTPD---NGRVKW----------SENA 383
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFfnqniyerrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 384 TIGYYAQDHATDFEVDMTVFDWMSL------WMKPEDDEQSVRSVLGRLLFsQDDIK----KSVKVLSGGEKGRMLFGKL 453
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYgvkivgWRPKLEIDDIVESALKDADL-WDEIKhkihKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 454 MMQKPNVLIMDEPTNHLD------MES-IESLNMALELyqgTLIFVSHDREFVSSLAN 504
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDpiasmkVESlIQSLRLRSEL---TMVIVSHNLHQVSRLSD 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-210 |
8.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPnerlgklkqdqfayeeftvLDTVIMGHaeL 92
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-------------------LDTSDEEN--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 93 WEIKQERERIYSLPE------MSEE------EGLRVADLEVKfgemdgytveSRAGELLLNVGipleqhngpMSEV---A 157
Cdd:PRK13633 81 WDIRNKAGMVFQNPDnqivatIVEEdvafgpENLGIPPEEIR----------ERVDESLKKVG---------MYEYrrhA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 158 P-----GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNS----TMIIISH 210
Cdd:PRK13633 142 PhllsgGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-506 |
8.58e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------------SENATIG 386
Cdd:COG1129 4 LLEMRGISKSFGGVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrsprdAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQdhatdfEV----DMTV---------------FDWMSLwmkpeddEQSVRSVLGRLLFsqdDIKKSVKV--LSGGEK 445
Cdd:COG1129 83 IIHQ------ELnlvpNLSVaeniflgreprrgglIDWRAM-------RRRARELLARLGL---DIDPDTPVgdLSVAQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 446 GRMLFGKLMMQKPNVLIMDEPTNHLDMESIESL-NMALEL-YQG-TLIFVSHDREFVSSLANRI 506
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLfRIIRRLkAQGvAIIYISHRLDEVFEIADRV 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-229 |
9.19e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKqDQFAYeeft 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRRQR-DEYHQ---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vlDTVIMGHAElwEIKqereriyslPEMSEEEGLRVadlevkFGEMDGYTVESRAGELLLNVGIpLEQHNGPMSEVAPGW 160
Cdd:PRK13538 75 --DLLYLGHQP--GIK---------TELTALENLRF------YQRLHGPGDDEALWEALAQVGL-AGFEDVPVRQLSAGQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIII-SHdrHFLNMVCTHMADLDYGG 229
Cdd:PRK13538 135 QRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhaEQGGMVILtTH--QDLPVASDKVRKLRLGQ 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
316-531 |
9.22e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 316 FRNALEVENIAKGYEANTPL-FKDV-NMMLEVGEK--VAILGTNGVGKSTMIKTLVGELTPDNGRvkwsenATIGYYA-- 389
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTPFeFKALnNTSLTFKKNkvTCVIGTTGSGKSTMIQLTNGLIISETGQ------TIVGDYAip 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 -------------------------QDHATDFEVDMTvFDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGE 444
Cdd:PRK13645 77 anlkkikevkrlrkeiglvfqfpeyQLFQETIEKDIA-FGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDMESIES-LNMALEL---YQGTLIFVSHDREFVSSLANRIIEITPEKVTNFQGT 520
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDfINLFERLnkeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
250
....*....|....*.
gi 490363216 521 YD-----EFLAKKGID 531
Cdd:PRK13645 236 FEifsnqELLTKIEID 251
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-523 |
9.99e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.49 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 333 TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSenATIGYYAQdhatdfevdmtvFDWMSLWMKP 412
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS--GRISFSSQ------------FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 413 ED-------DEQSVRSVLGRLLFSQDDIKKSVK----------VLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDM--- 472
Cdd:cd03291 116 ENiifgvsyDEYRYKSVVKACQLEEDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVfte 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 473 -ESIESLNMALeLYQGTLIFVSHDREFVSSlANRIIeITPEKVTNFQGTYDE 523
Cdd:cd03291 196 kEIFESCVCKL-MANKTRILVTSKMEHLKK-ADKIL-ILHEGSSYFYGTFSE 244
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
346-507 |
1.13e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwsenatigyyaqdhatdFEVDMTVFDWMSlwmkpeddeqsvrsvlgR 425
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------IYIDGEDILEEV-----------------L 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 426 LLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQG---------TLIFVSHDR 496
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlTVILTTNDE 126
|
170
....*....|.
gi 490363216 497 EFVSSLANRII 507
Cdd:smart00382 127 KDLGPALLRRR 137
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
320-506 |
1.13e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFK----DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDHATD 395
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 396 FEVDMTV-------------------FDWMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQ 456
Cdd:PRK13643 82 VRKKVGVvfqfpesqlfeetvlkdvaFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490363216 457 KPNVLIMDEPTNHLDMES-IESLNMALELYQG--TLIFVSHDREFVSSLANRI 506
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKArIEMMQLFESIHQSgqTVVLVTHLMDDVADYADYV 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-218 |
1.29e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.93 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLA--PTSGNVFLD--------PNER------LGk 68
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDgedilelsPDERaragifLA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 69 lkqdqFAYEEftvldtvimghaelwEIkqereriyslPEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIP--- 145
Cdd:COG0396 83 -----FQYPV---------------EI----------PGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDedf 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 146 LEQH-NGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE---RNSTMIIISHDRHFLNMV 218
Cdd:COG0396 133 LDRYvNEGFSG---GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlrsPDRGILIITHYQRILDYI 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
1.49e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNErlgkLKQDQfayeeftvldtvimghAELWEIKQE 98
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP----IKYDK----------------KSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 99 RERIYSLPEmSEEEGLRVADlEVKFGEMD-GYT---VESRAGELLLNVGIpLEQHNGPMSEVAPGWKLRVLLAQALFADP 174
Cdd:PRK13639 80 VGIVFQNPD-DQLFAPTVEE-DVAFGPLNlGLSkeeVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 175 DILLLDEPTNNLD---IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13639 157 EIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
320-484 |
1.81e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLF--------KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENA-TIGYYA- 389
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlHFGDYSy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 ---------QDHATDFEVDMTVFDWMSLWMK------PEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLM 454
Cdd:PRK15112 85 rsqrirmifQDPSTSLNPRQRISQILDFPLRlntdlePEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190
....*....|....*....|....*....|..
gi 490363216 455 MQKPNVLIMDEPTNHLDMeSIES--LNMALEL 484
Cdd:PRK15112 165 ILRPKVIIADEALASLDM-SMRSqlINLMLEL 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
350-513 |
2.36e-09 |
|
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: 57.23 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 350 AILGTNGVGKSTMIK----TLVGELTPDN-GRVKWSENATIGyyaqdhATDFEVDMTvfdwmsLWMKPEDDEQSVRS--V 422
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPNSkGGAHDPKLIREG------EVRAQVKLA------FENANGKKYTITRSlaI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 423 LGRLLF-SQDDIKK----SVKVLSGGEKgrMLFG--------KLMMQKPNVLIMDEPTNHLDMESIE-SLNMALELYQGT 488
Cdd:cd03240 94 LENVIFcHQGESNWplldMRGRCSGGEK--VLASliirlalaETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQ 171
|
170 180
....*....|....*....|....*....
gi 490363216 489 LIF----VSHDREFVsSLANRIIEITPEK 513
Cdd:cd03240 172 KNFqlivITHDEELV-DAADHIYRVEKDG 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-233 |
2.65e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.30 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklkqdQFAYEEFTvLDTvimGHAELWEIKQ 97
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI--------------TIAGYHIT-PET---GNKNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 98 ERERIYSLPEMSEEEGLRVADleVKFGEMD-GYT---VESRAGELLLNVGIPLEQHNGPMSEVAPGWKLRVLLAQALFAD 173
Cdd:PRK13641 86 KVSLVFQFPEAQLFENTVLKD--VEFGPKNfGFSedeAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 174 PDILLLDEPTNNLDIDTIRWLEQTLNERNS---TMIIISHDRHFLNMVCTHMADLDYGGLTVH 233
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-212 |
2.78e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQDQFAY 76
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvpPYQRpINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 EEFTVLDTVIMGhaelweIKQEReriysLPEmseeeglrvadlevkfGEmdgytVESRAGELLLNVGIPLEQHNGPmSEV 156
Cdd:PRK11607 104 PHMTVEQNIAFG------LKQDK-----LPK----------------AE-----IASRVNEMLGLVHMQEFAKRKP-HQL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLD--------IDTIRWLEQTlnerNSTMIIISHDR 212
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQ 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
3.26e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.82 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFldpnerlgklkqdqfayeeftvldtvIMGHae 91
Cdd:PRK13647 17 GTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVK--------------------------VMGR-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 lwEIKQERERiyslpEMSEEEGLRVADLE-----------VKFG----EMDGYTVESRAGELLLNVGIPLEQHNGPMsEV 156
Cdd:PRK13647 68 --EVNAENEK-----WVRSKVGLVFQDPDdqvfsstvwddVAFGpvnmGLDKDEVERRVEEALKAVRMWDFRDKPPY-HL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 157 APGWKLRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13647 140 SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-509 |
3.68e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTL-------VGELTPDNGRVKwsenatiGYYAQDH 392
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-------DPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 393 ATDFEVDMtVFDWMSLW------------------MKPEDDEQSVRSVLGRL-LFSQDDIKKSVkvLSGGEKGRMLFGKL 453
Cdd:PRK09493 74 LIRQEAGM-VFQQFYLFphltalenvmfgplrvrgASKEEAEKQARELLAKVgLAERAHHYPSE--LSGGQQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 454 MMQKPNVLIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLANRIIEI 509
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEgmTMVIVTHEIGFAEKVASRLIFI 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
320-506 |
3.71e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEAnTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKwsenatIGYYAQDHATDFEVD 399
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE------IGGNPCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 MtvfdwMSLWMKPED----DEQSVR-SVLGRLLFSQDDIKK---SVKVLSGGEKGRMLFGKL-------------MMQKP 458
Cdd:PRK15439 85 Q-----LGIYLVPQEpllfPNLSVKeNILFGLPKRQASMQKmkqLLAALGCQLDLDSSAGSLevadrqiveilrgLMRDS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 459 NVLIMDEPTNHLDMESIESL----NMALELYQGtLIFVSHDREFVSSLANRI 506
Cdd:PRK15439 160 RILILDEPTASLTPAETERLfsriRELLAQGVG-IVFISHKLPEIRQLADRI 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-516 |
3.73e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTpLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT------------IGY 387
Cdd:PRK10895 4 LTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhararrgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 388 YAQDhATDFEvDMTVFDWMSLWMKPEDD----EQSVRSVLGRLLFSQDDIKKSV-KVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:PRK10895 83 LPQE-ASIFR-RLSVYDNLMAVLQIRDDlsaeQREDRANELMEEFHIEHLRDSMgQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 463 MDEPTNHLDMESIESLNMALELYQ----GTLIFVSHDRE--------FVSSLANRIIEITPEKVTN 516
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRdsglGVLITDHNVREtlavceraYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
4.38e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.23 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLAP---TSGNVFLDpnerlgklKQDQFAy 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLD--------GQDIFK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 eeftvLDTVimghaelwEIKQERERIYSLPemSEEEGLRVADlEVKFGEMDGYTVESRAgELLLNVGIPLEQH------- 149
Cdd:PRK14247 75 -----MDVI--------ELRRRVQMVFQIP--NPIPNLSIFE-NVALGLKLNRLVKSKK-ELQERVRWALEKAqlwdevk 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 150 ---NGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:PRK14247 138 drlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLElkKDMTIVLVTH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
318-495 |
4.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGY-EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPD--------------NGRVKWSEN 382
Cdd:PRK13640 4 NIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 383 ATIGYYAQDHATDFeVDMTVFDWMSLWMK----PEDDEQS-VRSVLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQK 457
Cdd:PRK13640 84 EKVGIVFQNPDNQF-VGATVGDDVAFGLEnravPRPEMIKiVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490363216 458 PNVLIMDEPTNHLDMESIES-LNMALELY---QGTLIFVSHD 495
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQiLKLIRKLKkknNLTVISITHD 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-506 |
5.39e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGELTPDNGRV----KWSEnaTIGYYAQDHATDFEVDMtVFDWMSLWMKPEDDEQSVRS 421
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDE--ILDEFRGSELQNYFTKL-LEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 422 VLGR---LLFSQDD----------------IKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMEsiESLNMAL 482
Cdd:cd03236 103 VKGKvgeLLKKKDErgkldelvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRLNAAR 180
|
170 180
....*....|....*....|....*....
gi 490363216 483 ---ELYQGT--LIFVSHDREFVSSLANRI 506
Cdd:cd03236 181 lirELAEDDnyVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-228 |
5.52e-09 |
|
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: 56.35 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPnerlGKLKQDQFAYEEftv 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 lDTVIMGHAElwEIKQereriyslpEMSEEEGLRvadlevkFGEMDGYTveSRAGELLLNVGIPLEQHNgPMSEVAPGWK 161
Cdd:cd03231 74 -GLLYLGHAP--GIKT---------TLSVLENLR-------FWHADHSD--EQVEEALARVGLNGFEDR-PVAQLSAGQQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISHdrHFLNMVCTHMADLDYG 228
Cdd:cd03231 132 RRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAghcARGGMVVLTTH--QDLGLSEAGARELDLG 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-188 |
5.92e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNerlgKLKQDQFAYeeftvldtvimghaelweiKQ 97
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH----PLHFGDYSY-------------------RS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 98 ERER-IYSLPEMSEEEGLRVA---DLEVKFG-EMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGWKLRVLLAQALFA 172
Cdd:PRK15112 87 QRIRmIFQDPSTSLNPRQRISqilDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALIL 166
|
170
....*....|....*.
gi 490363216 173 DPDILLLDEPTNNLDI 188
Cdd:PRK15112 167 RPKVIIADEALASLDM 182
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
317-507 |
6.21e-09 |
|
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: 55.52 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIAKGyeantPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsENATIGYYAQDHATDF 396
Cdd:cd03215 2 EPVLEVRGLSVK-----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-DGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 397 EVDMTvfdwmslwmkPED-------DEQSVRS--VLGRLLfsqddikksvkvlSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:cd03215 76 GIAYV----------PEDrkreglvLDLSVAEniALSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490363216 468 NHLDMESIEslnmalELYQ---------GTLIFVSHDREFVSSLANRII 507
Cdd:cd03215 133 RGVDVGAKA------EIYRlireladagKAVLLISSELDELLGLCDRIL 175
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-509 |
6.30e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENATIGYYAQDHATDFEvD 399
Cdd:PRK11247 13 LLLNAVSKRYGERTVL-NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQ-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 M------TVFDWMSLWMK---PEDDEQSVRSV-LgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNH 469
Cdd:PRK11247 90 ArllpwkKVIDNVGLGLKgqwRDAALQALAAVgL------ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490363216 470 LD-MESIESLNMALELYQG---TLIFVSHDREFVSSLANRIIEI 509
Cdd:PRK11247 164 LDaLTRIEMQDLIESLWQQhgfTVLLVTHDVSEAVAMADRVLLI 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-527 |
6.36e-09 |
|
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: 58.28 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVG--ELTPDNGRVKW--SENATIGY-----YAQ 390
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL-KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvALCEKCGYverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHATDFEVDMTVFDwMSLWMKPEDDEQSVR-----------------SVLGRLLFSQDDI----KKSVKV---------- 439
Cdd:TIGR03269 80 EPCPVCGGTLEPEE-VDFWNLSDKLRRRIRkriaimlqrtfalygddTVLDNVLEALEEIgyegKEAVGRavdliemvql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 440 ----------LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALEL----YQGTLIFVSHDREFVSSLANR 505
Cdd:TIGR03269 159 shrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLTSHWPEVIEDLSDK 238
|
250 260
....*....|....*....|..
gi 490363216 506 IIEITPEKVTNfQGTYDEFLAK 527
Cdd:TIGR03269 239 AIWLENGEIKE-EGTPDEVVAV 259
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-507 |
6.37e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLDI-------DTIRWLEQtlnERNSTMIIISHDrhfLNMVcthmadldygglt 231
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilQLLRELQQ---ELNMGLLFITHN---LSIV------------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 232 vhpgnydeymlaatqareRLLADNAK--KKAQISELQSFVSRFSANA-SKSRQATSRAKQIEKIQLTEVKAssrqnPFIR 308
Cdd:PRK15134 221 ------------------RKLADRVAvmQNGRCVEQNRAATLFSAPThPYTQKLLNSEPSGDPVPLPEPAS-----PLLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 309 FEQ-------EKKLFRNALEvENIAkgyeantplFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLV------GELTPDNG 375
Cdd:PRK15134 278 VEQlqvafpiRKGILKRTVD-HNVV---------VKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIWFDGQ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 376 RV-KWSENATIGYYA------QDHATDFEVDMTVFDWMS-------LWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLS 441
Cdd:PRK15134 348 PLhNLNRRQLLPVRHriqvvfQDPNSSLNPRLNVLQIIEeglrvhqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFS 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 442 GGEKGRMLFGKLMMQKPNVLIMDEPTNHLD---MESIESLNMAL-ELYQGTLIFVSHDREFVSSLANRII 507
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVI 497
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-239 |
7.18e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLdpnerLGKlkqdqfayeeftvlDTVIMGHAELWEIKQER 99
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW-----LGK--------------DLLGMKDDEWRAVRSDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 100 ERIYSLPEMSEEEGLRVAD-----LEVKFGEMDGYTVESRAGELLLNVGIPLEQHNGPMSEVAPGWKLRVLLAQALFADP 174
Cdd:PRK15079 101 QMIFQDPLASLNPRMTIGEiiaepLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 175 DILLLDEPTNNLDID----TIRWLEQTLNERNSTMIIISHDrhfLNMVcTHMAD---LDYGGLTVHPGNYDE 239
Cdd:PRK15079 181 KLIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHD---LAVV-KHISDrvlVMYLGHAVELGTYDE 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-513 |
7.59e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPnerlgklkqdqfay 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 eeftvldtvimghaeLWEIKQERERIySLPEMSEEE--GLRVADLEVKFGE-MDG----YTV-ESRAGELLLNVGIP--- 145
Cdd:PRK10261 78 ---------------MLLRRRSRQVI-ELSEQSAAQmrHVRGADMAMIFQEpMTSlnpvFTVgEQIAESIRLHQGASree 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 146 --------LEQHNGPMSE---------VAPGWKLRVLLAQALFADPDILLLDEPTNNLDI-------DTIRWLEQtlnER 201
Cdd:PRK10261 142 amveakrmLDQVRIPEAQtilsryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaqilQLIKVLQK---EM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 202 NSTMIIISHDRHflnmVCTHMAD---LDYGGLTVHPGNYDEYMLAATQARER-LLAdnAKKKAQISELQSFVSRFSANAS 277
Cdd:PRK10261 219 SMGVIFITHDMG----VVAEIADrvlVMYQGEAVETGSVEQIFHAPQHPYTRaLLA--AVPQLGAMKGLDYPRRFPLISL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 278 KsrQATSRAKQIEKIQLTEVKASSR-QNPFIRFEQEKKLF-RNALEVENIAKgyeantplfkdVNMMLEVGEKVAILGTN 355
Cdd:PRK10261 293 E--HPAKQEPPIEQDTVVDGEPILQvRNLVTRFPLRSGLLnRVTREVHAVEK-----------VSFDLWPGETLSLVGES 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 356 GVGKST-------MIKTLVGELTPDNGRVK-------WSENATIGYYAQDHATDFEVDMTVFDWMslwMKP--------- 412
Cdd:PRK10261 360 GSGKSTtgrallrLVESQGGEIIFNGQRIDtlspgklQALRRDIQFIFQDPYASLDPRQTVGDSI---MEPlrvhgllpg 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 413 EDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMeSIES--LNMALELYQG--- 487
Cdd:PRK10261 437 KAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiINLLLDLQRDfgi 515
|
570 580 590
....*....|....*....|....*....|....
gi 490363216 488 TLIFVSHDREFVSSLANR--------IIEITPEK 513
Cdd:PRK10261 516 AYLFISHDMAVVERISHRvavmylgqIVEIGPRR 549
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
316-529 |
8.24e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.05 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 316 FRNALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-----------SENAT 384
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtraSLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 385 IGYYAQDhATDFevDMTVFDWMSLWmKPEDDEQSVRSVLGR-----LLFSQDDIKKSV-----KVLSGGEKGRMLFGKLM 454
Cdd:PRK13657 411 IAVVFQD-AGLF--NRSIEDNIRVG-RPDATDEEMRAAAERaqahdFIERKPDGYDTVvgergRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 455 MQKPNVLIMDEPTNHLDMESIESLNMAL-ELYQGTLIFV-SH--------DREFVssLAN-RIIEitpekvtnfQGTYDE 523
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALdELMKGRTTFIiAHrlstvrnaDRILV--FDNgRVVE---------SGSFDE 555
|
....*.
gi 490363216 524 FLAKKG 529
Cdd:PRK13657 556 LVARGG 561
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-254 |
8.58e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdlaPTSGNVfldpnerlgKLKQDQFAYEEFTV 81
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNW---------RVTADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 LDTV------IMGHaELWEIKQEREriySLPEMSEEEGLRVADlevkfgEMDGYTVES-----------RAGELLLNVGI 144
Cdd:PRK15093 76 LRLSprerrkLVGH-NVSMIFQEPQ---SCLDPSERVGRQLMQ------NIPGWTYKGrwwqrfgwrkrRAIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 145 plEQHNGPMS----EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQTLNERNSTMI-IISHDRHFLN 216
Cdd:PRK15093 146 --KDHKDAMRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqIFRLLTRLNQNNNTTIlLISHDLQMLS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490363216 217 MVCTHMaDLDYGGLTVHPGNYDEYMLAA----TQARERLLAD 254
Cdd:PRK15093 224 QWADKI-NVLYCGQTVETAPSKELVTTPhhpyTQALIRAIPD 264
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
9.17e-09 |
|
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: 55.55 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLdpnerlgklkQDQFAY---EEF----TVLDTV 85
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV----------PGSIAYvsqEPWiqngTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 IMGHaelwEIKQEReriYslpemseEEGLRVADLEVKFGEMDGytvesragelllnvgipleqhnGPMSEVAP------- 158
Cdd:cd03250 87 LFGK----PFDEER---Y-------EKVIKACALEPDLEILPD----------------------GDLTEIGEkginlsg 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWL-EQTLNE---RNSTMIIISHDRHFL 215
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGlllNNKTRILVTHQLQLL 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-210 |
9.79e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.20 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGK-LKQDQFAYEEFTVldtVIMGHAE 91
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-----GVpLVQYDHHYLHRQV---ALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIKQERERI-YSLPEMSEEEGLRVADLEVK---FGEM-DGY-TVESRAGELLlnvgipleqhngpmsevAPGWKLRVL 165
Cdd:TIGR00958 565 VLFSGSVRENIaYGLTDTPDEEIMAAAKAANAhdfIMEFpNGYdTEVGEKGSQL-----------------SGGQKQRIA 627
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490363216 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISH 210
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
335-471 |
1.00e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.75 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 335 LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPD---------NGRV--KWSENATIGYYAQDHAtdFEVDMTVF 403
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgsgsvllNGMPidAKEMRAISAYVQQDDL--FIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 404 D---WMSLWMKPEDDEQSVR-----SVLGRL-LFSQDD----IKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHL 470
Cdd:TIGR00955 118 EhlmFQAHLRMPRRVTKKEKrervdEVLQALgLRKCANtrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
.
gi 490363216 471 D 471
Cdd:TIGR00955 198 D 198
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
337-510 |
1.06e-08 |
|
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: 55.93 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 337 KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsENATIGYYAQDHATDFEvDMTVFDWMSLW------- 409
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMVVFQ-NYSLLPWLTVRenialav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 410 ------MKPEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMAL- 482
Cdd:TIGR01184 80 drvlpdLSKSERRAIVEEHI-ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELm 158
|
170 180 190
....*....|....*....|....*....|.
gi 490363216 483 ---ELYQGTLIFVSHDREFVSSLANRIIEIT 510
Cdd:TIGR01184 159 qiwEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
320-531 |
1.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPL--FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK-----------WSENATIG 386
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQDHATDFeVDMTVFDWMSLWMKPED--DEQSVRSVLGRLL-FSQDDIK-KSVKVLSGGEKGRMLFGKLMMQKPNVLI 462
Cdd:PRK13642 85 MVFQNPDNQF-VGATVEDDVAFGMENQGipREEMIKRVDEALLaVNMLDFKtREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 463 MDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVSS----LANRIIEITPEKVTNFQGTYDEFLAKKGID 531
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDLDEAASsdriLVMKAGEIIKEAAPSELFATSEDMVEIGLD 240
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
319-530 |
1.39e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 57.52 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSE----------------- 381
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraaigi 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 382 --------NATIGY---YAQDHATDFEVdmtvfdwmslwmkpeddEQSVRsvLGRLlfsqDDIKKS-------------V 437
Cdd:COG5265 437 vpqdtvlfNDTIAYniaYGRPDASEEEV-----------------EAAAR--AAQI----HDFIESlpdgydtrvgergL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 438 KvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMAL-ELYQG--TLIfVSH--------DREFVssLAN-R 505
Cdd:COG5265 494 K-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALrEVARGrtTLV-IAHrlstivdaDEILV--LEAgR 569
|
250 260
....*....|....*....|....*
gi 490363216 506 IIEitpekvtnfQGTYDEFLAKKGI 530
Cdd:COG5265 570 IVE---------RGTHAELLAQGGL 585
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
342-481 |
1.41e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 342 MLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGR----VKWSEnaTIGYYA----QDHatdFE---------------V 398
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeePSWDE--VLKRFRgtelQDY---FKklangeikvahkpqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 DM-------TVFDwmsLWMKpEDDEQSVRSVLGRLlfsqdDIK----KSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPT 467
Cdd:COG1245 170 DLipkvfkgTVRE---LLEK-VDERGKLDELAEKL-----GLEnildRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170
....*....|....
gi 490363216 468 NHLDMEsiESLNMA 481
Cdd:COG1245 241 SYLDIY--QRLNVA 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
350-517 |
1.54e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 350 AILGTNGVGKSTMIKTLVGELTPDNGRVKW-------SENAT--------IGYYAQD-----HatdfevdMTVFDWMSLW 409
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdAEKGIclppekrrIGYVFQDarlfpH-------YKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 410 MKPEDDEQ--SVRSVLGrllfsqddIKKSVK----VLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDM----ESIESLN 479
Cdd:PRK11144 101 MAKSMVAQfdKIVALLG--------IEPLLDrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 490363216 480 MALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNF 517
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-224 |
1.80e-08 |
|
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: 57.00 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLF--ENISVKFGGGNRY-----------------GLIGANGSGKS-TFMKILG---GDLAPTSGNVFLD-------P 62
Cdd:COG4172 3 SMPLLsvEDLSVAFGQGGGTveavkgvsfdiaagetlALVGESGSGKSvTALSILRllpDPAAHPSGSILFDgqdllglS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 63 NERLGKLKQDQFAyeeftvldtviMghaelweIKQERerIYSL-PEMSEEEGLRVAdLEVKFGeMDGYTVESRAGELLLN 141
Cdd:COG4172 83 ERELRRIRGNRIA-----------M-------IFQEP--MTSLnPLHTIGKQIAEV-LRLHRG-LSGAAARARALELLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 142 VGIP-----LEQ--HngpmsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIdTIRwlEQTLN-------ERNSTMII 207
Cdd:COG4172 141 VGIPdperrLDAypH-----QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQ--AQILDllkdlqrELGMALLL 212
|
250
....*....|....*..
gi 490363216 208 ISHDrhfLNMVcTHMAD 224
Cdd:COG4172 213 ITHD---LGVV-RRFAD 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-228 |
2.06e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.62 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKfgGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKlkqdqfayeeftVLDTVIMGhaeLWEIKQE 98
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-----GK------------PIDYSRKG---LMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 99 RERIYSLPEMSeeegLRVADL--EVKFGEMD----GYTVESRAGELLLNVGI-PLEqhNGPMSEVAPGWKLRVLLAQALF 171
Cdd:PRK13636 84 VGMVFQDPDNQ----LFSASVyqDVSFGAVNlklpEDEVRKRVDNALKRTGIeHLK--DKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 172 ADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-223 |
2.08e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERL---GKLKQDQFAYEEFTVLDTVIMGH 89
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtniSDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 90 AELWEIKqereRIYSLPemsEEEGLRVADLEVKFGEMDGYTvESRAGelllnvgipleQHNGpmsevapGWKLRVLLAQA 169
Cdd:TIGR01257 2031 EHLYLYA----RLRGVP---AEEIEKVANWSIQSLGLSLYA-DRLAG-----------TYSG-------GNKRKLSTAIA 2084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 170 LFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISHDRHFLNMVCTHMA 223
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVsiiREGRAVVLTSHSMEECEALCTRLA 2141
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-217 |
2.39e-08 |
|
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: 54.15 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 32 LIGANGSGKSTFMK----ILGGDLAPTSGNVFLDP-----NERLGKLK--------QDQFAYEEFTVLDTVIMGHAE--L 92
Cdd:cd03240 27 IVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPklireGEVRAQVKlafenangKKYTITRSLAILENVIFCHQGesN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 93 WEIKQERERiyslpeMSeeeglrvadlevkfgemdgytvesrAGElllnvgipleqhngpmsEVAPGWKLRVLLAQALFA 172
Cdd:cd03240 107 WPLLDMRGR------CS-------------------------GGE-----------------KVLASLIIRLALAETFGS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 173 DPDILLLDEPTNNLDIDTIRW-----LEQTLNERNSTMIIISHDRHFLNM 217
Cdd:cd03240 139 NCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
241-494 |
2.69e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.68 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 241 MLAATQARERLladnAKKKAQISELQSFVSR-------FSANAS---KSRQATSRAKQIEKIQLTEVKASS----RQNPF 306
Cdd:TIGR00954 376 LLKAADALGRL----MLAGRDMTRLAGFTARvdtllqvLDDVKSgnfKRPRVEEIESGREGGRNSNLVPGRgiveYQDNG 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 307 IRFEqekklfrnaleveNIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLvGELTPD-NGRVKWSENATI 385
Cdd:TIGR00954 452 IKFE-------------NIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKL 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQ----------DHATdfeVDMTVFDWMSLWMKPEDDEQSVRSV-LGRLL---FSQDDIKKSVKVLSGGEKGRMLFG 451
Cdd:TIGR00954 518 FYVPQrpymtlgtlrDQII---YPDSSEDMKRRGLSDKDLEQILDNVqLTHILereGGWSAVQDWMDVLSGGEKQRIAMA 594
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490363216 452 KLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQGTLIFVSH 494
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-216 |
3.07e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 54.57 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLA--PTSGNVFLDpNERLGKLKQDQFAyeef 79
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFK-GQDLLELEPDERA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 tvldtvimgHAELWEIKQERERIyslPEMSEEEGLRVADLEVKF----GEMDGYTVESRAGELLLNVGIPLEQHNGPMSE 155
Cdd:TIGR01978 76 ---------RAGLFLAFQYPEEI---PGVSNLEFLRSALNARRSargeEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNE 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 156 -VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISHDRHFLN 216
Cdd:TIGR01978 144 gFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINrlrEPDRSFLIITHYQRLLN 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
320-466 |
3.09e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.69 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVG--ELTPDNGRVKWsENATIgyyaqdhaTDFE 397
Cdd:COG0396 1 LEIKNLHVSVE-GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILL-DGEDI--------LELS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 398 VD-------------------MTVFDWMSL--------WMKPEDDEQSVRSVLGRLLFSQDDIKKSVKV-LSGGEKGRML 449
Cdd:COG0396 71 PDeraragiflafqypveipgVSVSNFLRTalnarrgeELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNE 150
|
170
....*....|....*..
gi 490363216 450 FGKLMMQKPNVLIMDEP 466
Cdd:COG0396 151 ILQMLLLEPKLAILDET 167
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
346-531 |
3.30e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.34 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWsENATIGYyaqdhatdfevdmtvfdwmslwmKPeddeQSVRsvlgr 425
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY-----------------------KP----QYID----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 426 llfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMEsiESLNMA------LELYQGTLIFVSHDREFV 499
Cdd:cd03222 72 --------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE--QRLNAArairrlSEEGKKTALVVEHDLAVL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 500 SSLANRII--EITPEKVTNF---QGT---YDEFLAKKGID 531
Cdd:cd03222 136 DYLSDRIHvfEGEPGVYGIAsqpKGTregINRFLRGYLIT 175
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
346-471 |
3.66e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGeLTPDNGRV--------KWS--ENATI-GYYAQDHATDFEVDmtVFDWMSLWM---K 411
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagqpleAWSaaELARHrAYLSQQQTPPFAMP--VFQYLTLHQpdkT 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 412 PEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQ-----KPN--VLIMDEPTNHLD 471
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLD 165
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
4.17e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVF-----LDPNER-LGKLKQdQF 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpLDYSKRgLLALRQ-QV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 75 AyeefTVLdtvimghaelweikQERERIYSLPEMSEEEGLRVADLEVKFGEmdgytVESRAGELLLNVGIPLEQHNgPMS 154
Cdd:PRK13638 80 A----TVF--------------QDPEQQIFYTDIDSDIAFSLRNLGVPEAE-----ITRRVDEALTLVDAQHFRHQ-PIQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQTLNErnstMIIISHD 211
Cdd:PRK13638 136 CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHD 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-228 |
4.18e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFA---------YEEF------TVLD 83
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQDLTALSEKELRkarrqigmiFQHFnllssrTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 TVimghaelweikqereriySLPemSEEEGLRVADlevkfgemdgytVESRAGELLLNVGIPlEQHNGPMSEVAPGWKLR 163
Cdd:PRK11153 102 NV------------------ALP--LELAGTPKAE------------IKARVTELLELVGLS-DKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNS----TMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
4.64e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKLKQDQfay 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 eeftvldtvimghaELWEIKQERERIYSLPEMSEEEGLRVADLE---VKFGEmDGYTVESRAGELLLNVGIPLEQHNGPM 153
Cdd:PRK13645 84 --------------EVKRLRKEIGLVFQFPEYQLFQETIEKDIAfgpVNLGE-NKQEAYKKVPELLKLVQLPEDYVKRSP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13645 149 FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHN 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-211 |
5.19e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 55.08 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKLkqdqfayeeftVLDT 84
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG-----GRD-----------VTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VImghaelweikQEReRI------YSL-PEMSEEE----GLRVADlevkfgeMDGYTVESRAGELLLNVGI-PLEQHNgP 152
Cdd:COG3839 71 PP----------KDR-NIamvfqsYALyPHMTVYEniafPLKLRK-------VPKAEIDRRVREAAELLGLeDLLDRK-P 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 153 mSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:COG3839 132 -KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
130-269 |
5.50e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 130 TVESRAGELLLNVGIP-----LE----QHNGPMSEvapgwklRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQ 196
Cdd:PRK11022 126 TRRQRAIDLLNQVGIPdpasrLDvyphQLSGGMSQ-------RVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLE 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 197 TLNERNSTMIIISHDrhfLNMVC--THMADLDYGGLTVHPGNYDEYMLAA----TQARERLLADNAKKKAQISELQSFV 269
Cdd:PRK11022 199 LQQKENMALVLITHD---LALVAeaAHKIIVMYAGQVVETGKAHDIFRAPrhpyTQALLRALPEFAQDKARLASLPGVV 274
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
332-529 |
5.66e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.50 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLV-------GELTPDNGRVKWSEN-------ATIGYYAQDHATDFE 397
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGVPLVQYDHhylhrqvALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 398 VDMTvfdwMSLWMKPEDDEQSVRSVLGRLLFSQD-------DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHL 470
Cdd:TIGR00958 573 ENIA----YGLTDTPDEEIMAAAKAANAHDFIMEfpngydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 471 DMESIESLNMALELYQGTLIFVSHDREFVSSlANRIIEITPEKVTNfQGTYDEFLAKKG 529
Cdd:TIGR00958 649 DAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVE-MGTHKQLMEDQG 705
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-506 |
5.86e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAtigYYAQDHATDFEV- 398
Cdd:PRK09700 6 ISMAGIGKSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN---YNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 ------DMTVFDWMSL--------------WMKPEDDEQSVRSVLGRLLFSQD---DIKKSVKVLSGGEKGRMLFGKLMM 455
Cdd:PRK09700 82 igiiyqELSVIDELTVlenlyigrhltkkvCGVNIIDWREMRVRAAMMLLRVGlkvDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 456 QKPNVLIMDEPTNHLDMESIESLNMALELYQG---TLIFVSHDREFVSSLANRI 506
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRY 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
318-505 |
6.00e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGY---EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENATIG 386
Cdd:PRK10584 5 NIVEVHHLKKSVgqgEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQDHATDFEVDMTVFDWMSL-------WMKPEDDEQSVRSvlGRLLFSQDDIKKSVK----VLSGGEKGRMLFGKLMM 455
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALenvelpaLLRGESSRQSRNG--AKALLEQLGLGKRLDhlpaQLSGGEQQRVALARAFN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 456 QKPNVLIMDEPTNHLDMESIE-------SLNMAlelYQGTLIFVSHDrefvSSLANR 505
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDkiadllfSLNRE---HGTTLILVTHD----LQLAAR 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-227 |
6.32e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.04 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKlkqdqfayeeftvldtvimghAE 91
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-GEPITK---------------------EN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 LWEIKQERERIYSLPEmsEEEGLRVADLEVKFGE----MDGYTVESRAGELLLNVGIPLEQHNGPmSEVAPGWKLRVLLA 167
Cdd:PRK13652 73 IREVRKFVGLVFQNPD--DQIFSPTVEQDIAFGPinlgLDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 168 QALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIIShdRHFLNMVcTHMADLDY 227
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNdlpETYGMTVIFS--THQLDLV-PEMADYIY 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
6.33e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfLDPNERLGKLKQD-QFAYEEF- 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDtRLMFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 -----TVLDTVIMGHAELWeikqereriyslpemseeeglRVADLEVkfgeMDGYTVESRAGELllnvgipleqhngPmS 154
Cdd:PRK11247 92 llpwkKVIDNVGLGLKGQW---------------------RDAALQA----LAAVGLADRANEW-------------P-A 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTiRWLEQTLNER-----NSTMIIISHD 211
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT-RIEMQDLIESlwqqhGFTVLLVTHD 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-229 |
6.39e-08 |
|
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: 52.16 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAP-TSGNVfldpnerlgklkqdqfayeeftvldtvimghae 91
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRI--------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 lweIKQERERIYSLPEMSeeeglrvadlevkfgemdgYtvesragellLNVGIPLEQHNGPMSEV-APGWKLRVLLAQAL 170
Cdd:cd03223 59 ---GMPEGEDLLFLPQRP-------------------Y----------LPLGTLREQLIYPWDDVlSGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 171 FADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHdRHFLNMVCTHMADLDYGG 229
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
6.85e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLAP---TSGNVFLDPNErlgklkqdqfA 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHN----------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 76 YEEFTvlDTVimghaelwEIKQERERIYSLPE---MSEEE----GLRVAdlevkfGEMDGYTVESRAGELLLNVGIPLE- 147
Cdd:PRK14239 75 YSPRT--DTV--------DLRKEIGMVFQQPNpfpMSIYEnvvyGLRLK------GIKDKQVLDEAVEKSLKGASIWDEv 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 148 ---QHNGPMSeVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:PRK14239 139 kdrLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGlkDDYTMLLVTR 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-239 |
7.16e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLK----QDQFAY 76
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKpeiyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 EEFT-VL--DTVIMGHAELWEIKQEReriyslPEMSeeeglRVADLEVKFgemdgytvesragelllnvGIPLEQHNGPM 153
Cdd:PRK10247 86 CAQTpTLfgDTVYDNLIFPWQIRNQQ------PDPA-----IFLDDLERF-------------------ALPDTILTKNI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIR----WLEQTLNERNSTMIIISHDRHFLNmvctHmADlDYGG 229
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDKDEIN----H-AD-KVIT 209
|
250
....*....|
gi 490363216 230 LTVHPGNYDE 239
Cdd:PRK10247 210 LQPHAGEMQE 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-210 |
7.46e-08 |
|
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: 52.80 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDP-----------NERLGKLKQ 71
Cdd:cd03369 10 ENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 DQfayeeftvldTVIMGHAelweikqeRERIYSLPEMSEEEgLRVAdLEVKFGemdgytvesragelllnvGIPLEQhng 151
Cdd:cd03369 90 DP----------TLFSGTI--------RSNLDPFDEYSDEE-IYGA-LRVSEG------------------GLNLSQ--- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 152 pmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:cd03369 129 -------GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAH 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-211 |
7.49e-08 |
|
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: 55.08 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMK-ILGgdLAPTSGNVFLDpNERLGKLKQDQFayeeftvldtvimghaelweiKQERERI------- 102
Cdd:COG4172 316 GLVGESGSGKSTLGLaLLR--LIPSEGEIRFD-GQDLDGLSRRAL---------------------RPLRRRMqvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 103 Y-SL-PEMSEE----EGLRVADLEvkfgeMDGYTVESRAGELLLNVGIPLE-QHNGPmSEVAPGWKLRVLLAQALFADPD 175
Cdd:COG4172 372 FgSLsPRMTVGqiiaEGLRVHGPG-----LSAAERRARVAEALEEVGLDPAaRHRYP-HEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490363216 176 ILLLDEPTNNLD-------IDTIRWLEQtlnERNSTMIIISHD 211
Cdd:COG4172 446 LLVLDEPTSALDvsvqaqiLDLLRDLQR---EHGLAYLFISHD 485
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
318-495 |
7.52e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEANTPL-FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT-----------I 385
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfeklrkhI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQDHATDFEVDMTVFD---WMSLWMKPEDDEQS-VRSVLGR--LLFSQDDIKKSvkvLSGGEKGRMLFGKLMMQKPN 459
Cdd:PRK13648 86 GIVFQNPDNQFVGSIVKYDvafGLENHAVPYDEMHRrVSEALKQvdMLERADYEPNA---LSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 460 VLIMDEPTNHLDMESIESL-NMALELYQG---TLIFVSHD 495
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLlDLVRKVKSEhniTIISITHD 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-254 |
7.61e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 2 LISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDP--------NER----LGKL 69
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARarrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 70 KQDQFAYEEFTVLDTVImghaELWEIKQereriyslpEMSEEEGlrvadlevkfgemdgytvESRAGELLLNVGIPLEQH 149
Cdd:PRK10895 84 PQEASIFRRLSVYDNLM----AVLQIRD---------DLSAEQR------------------EDRANELMEEFHIEHLRD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 150 NGPMSeVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDtIRWLEQTLNERNSTMIIISHD-RHFLNmVCTHMAD 224
Cdd:PRK10895 133 SMGQS-LSGGERRRVEIARALAANPKFILLDEPFAGVDpisvID-IKRIIEHLRDSGLGVLITDHNvRETLA-VCERAYI 209
|
250 260 270
....*....|....*....|....*....|
gi 490363216 225 LDYGGLTVHpGNYDEyMLAATQARERLLAD 254
Cdd:PRK10895 210 VSQGHLIAH-GTPTE-ILQDEHVKRVYLGE 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-183 |
8.14e-08 |
|
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: 53.21 E-value: 8.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER----LGKLKQDQFAYEEFTVLDTVIMG--HAELWEIK 96
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpPHERaragIGYVPEGRRIFPELTVEENLLLGayARRRAKRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 97 QERERIYSL-PEMSEEEGlrvadlevkfgemdgytveSRAGELllnvgipleqhNGpmsevapGWKLRVLLAQALFADPD 175
Cdd:cd03224 110 ARLERVYELfPRLKERRK-------------------QLAGTL-----------SG-------GEQQMLAIARALMSRPK 152
|
....*...
gi 490363216 176 ILLLDEPT 183
Cdd:cd03224 153 LLLLDEPS 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-211 |
8.57e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.65 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPnerlgklkqdqfayeeftvLDTVIMGHAELWEIKQ 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 98 ER-----ERIYSLPEMSeeeglrVADlEVKFG-EMDGYTVESR---AGELLLNVGIPLEQHNGPmSEVAPGWKLRVLLAQ 168
Cdd:PRK10070 106 KKiamvfQSFALMPHMT------VLD-NTAFGmELAGINAEERrekALDALRQVGLENYAHSYP-DELSGGMRQRVGLAR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490363216 169 ALFADPDILLLDEPTNNLDIDTIRWLEQTL----NERNSTMIIISHD 211
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-226 |
8.99e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAP-TSGNVFLDPNER-----------LGKLKqDQFAY----E 77
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGARvlflpqrpylpLGTLR-EALLYpataE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 78 EFTvldtvimgHAELWEIkqereriyslpemseeegLRVADLEVKFGEMDgytvESRAGELLLNVGiplEQHngpmseva 157
Cdd:COG4178 454 AFS--------DAELREA------------------LEAVGLGHLAERLD----EEADWDQVLSLG---EQQ-------- 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 158 pgwklRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNER--NSTMIIISHdRHFLNMVCTHMADLD 226
Cdd:COG4178 493 -----RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-224 |
1.02e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPnerlgklkqdqfayeeftvLDTVimGHAELWE 94
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-------------------IDTG--DFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 95 IKQERERIYSLPEmSEEEGlRVADLEVKFGE----MDGYTVESRAGELLLNVGIPLEQHNGPMSeVAPGWKLRVLLAQAL 170
Cdd:PRK13644 75 IRKLVGIVFQNPE-TQFVG-RTVEEDLAFGPenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKT-LSGGQGQCVALAGIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 171 FADPDILLLDEPTNNLDIDT-IRWLE--QTLNERNSTMIIISHdrhflNMVCTHMAD 224
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSgIAVLEriKKLHEKGKTIVYITH-----NLEELHDAD 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
332-523 |
1.02e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENATIGYYAQDHATD--------FE-----V 398
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTvrkrmsmlFQsgalfT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 DMTVFDWMSLWMKPEDD--EQSVRS-VLGRL----LFSQDDIKKSvkVLSGGEKGRMLFGKLMMQKPNVLIMDEP----- 466
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQlpAPLLHStVMMKLeavgLRGAAKLMPS--ELSGGMARRAALARAIALEPDLIMFDEPfvgqd 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 467 --TNHLDMESIESLNMALELyqgTLIFVSHDREFVSSLANRIIEITPEKVTNfQGTYDE 523
Cdd:PRK11831 176 piTMGVLVKLISELNSALGV---TCVVVSHDVPEVLSIADHAYIVADKKIVA-HGSAQA 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
319-507 |
1.06e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFK----DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkwsenaTIGYYAQDHAT 394
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI------TIAGYHITPET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 DFEVDMTVFDWMSLWMK-PE----------------------DDEQSVRSV--LGRLLFSQDDIKKSVKVLSGGEKGRML 449
Cdd:PRK13641 76 GNKNLKKLRKKVSLVFQfPEaqlfentvlkdvefgpknfgfsEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 450 FGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQG---TLIFVSHDREFVSSLANRII 507
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVL 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
335-471 |
1.16e-07 |
|
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: 52.66 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 335 LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPD---NGRV----------KWSENatIGYYAQDhatDFEVD-M 400
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprkpdQFQKC--VAYVRQD---DILLPgL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 401 TVFD---WMSLWMKPEDDEQSVRS-----VLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD 471
Cdd:cd03234 97 TVREtltYTAILRLPRKSSDAIRKkrvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-210 |
1.69e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.95 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGS-KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--PNERLGK--LKQDQFAYEEf 79
Cdd:PRK10790 344 DNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrPLSSLSHsvLRQGVAMVQQ- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 tvlDTVIMGHAELWEIKQEREriyslpeMSEE------EGLRVADLEVKFGemDGytVESRAGElllnvgipleQHNgpm 153
Cdd:PRK10790 423 ---DPVVLADTFLANVTLGRD-------ISEEqvwqalETVQLAELARSLP--DG--LYTPLGE----------QGN--- 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 154 sEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:PRK10790 476 -NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAvrEHTTLVVIAH 533
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-210 |
1.77e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQF-GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAPT---SGNVFLDPNERlgklkqdQF----AYE 77
Cdd:NF040905 6 GITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVC-------RFkdirDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 78 EFTVldtVIMgHAELWEIkqereriyslPEMSEEEGLRVADLEVKFGEMDGYTVESRAGELLLNVGIPlEQHNGPMSEVA 157
Cdd:NF040905 77 ALGI---VII-HQELALI----------PYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLD-ESPDTLVTDIG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 158 PGWKLRVLLAQALFADPDILLLDEPTNNL-DIDTIRWLE--QTLNERNSTMIIISH 210
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDllLELKAQGITSIIISH 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
319-530 |
1.77e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANT--PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNG-------------RVKWSENA 383
Cdd:PLN03232 614 AISIKNGYFSWDSKTskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETssvvirgsvayvpQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 384 TIgyyaQDH---ATDFEVDMTvfdWMSLwmkpedDEQSVRSVLGrlLFSQDDI----KKSVKVlSGGEKGRMLFGKLMMQ 456
Cdd:PLN03232 694 TV----RENilfGSDFESERY---WRAI------DVTALQHDLD--LLPGRDLteigERGVNI-SGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 457 KPNVLIMDEPTNHLDMESIESL---NMALELYQGTLIFVSHDREFVsSLANRIIEITpEKVTNFQGTYDEfLAKKGI 530
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVfdsCMKDELKGKTRVLVTNQLHFL-PLMDRIILVS-EGMIKEEGTFAE-LSKSGS 831
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
1.94e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNErlgkLKQDQFAYeeft 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD----ITDWQTAK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 vldtvIMghAELWEIKQERERIYSlpEMSEEEGLRVADLevkFGEMDGYTVE-SRAGELLLNVGIPLEQHNGPMSEvapG 159
Cdd:PRK11614 77 -----IM--REAVAIVPEGRRVFS--RMTVEENLAMGGF---FAERDQFQERiKWVYELFPRLHERRIQRAGTMSG---G 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 160 WKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQT-----LNERNSTMIIISHDRHFL 215
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPSLGLApiiiqqiFDTIEQLREQgmtifLVEQNANQALKLADRGYV 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
318-507 |
2.41e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 318 NALEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWS---------ENATIGYY 388
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVL-KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdKDGQLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 389 AQDHATDFEVDMT-VFDWMSLW-------------------MKPEDDEQSVRsVLGRLLFSQDDIKKSVKVLSGGEKGRM 448
Cdd:PRK10619 83 DKNQLRLLRTRLTmVFQHFNLWshmtvlenvmeapiqvlglSKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 449 LFGKLMMQKPNVLIMDEPTNHLDMESI-ESLNMALELYQ--GTLIFVSHDREFVSSLANRII 507
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVI 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
334-494 |
2.50e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 334 PLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSE---NATIGYYAQD-----HATDFEVDMTVFDW 405
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHQDllylgHQPGIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 406 MSLWMK--PEDDEQSVRSVLGRL-LFSQDDIkkSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMAL 482
Cdd:PRK13538 95 LRFYQRlhGPGDDEALWEALAQVgLAGFEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*
gi 490363216 483 E--LYQ-GTLIFVSH 494
Cdd:PRK13538 173 AqhAEQgGMVILTTH 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
2.90e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVfldpnerlgklkqdQFAYEEFT 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------------HYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 81 VLDTVIMGHAEL-------WEIKQERERiyslpemseeEGLRvadLEVKFGemdgytveSRAGELLLNVGiplEQHNGPM 153
Cdd:PRK11701 72 LRDLYALSEAERrrllrteWGFVHQHPR----------DGLR---MQVSAG--------GNIGERLMAVG---ARHYGDI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 154 SEVAPGWKLRVLLAQA----------------------LFADPDILLLDEPTNNLDI-------DTIRWLeqtLNERNST 204
Cdd:PRK11701 128 RATAGDWLERVEIDAAriddlpttfsggmqqrlqiarnLVTHPRLVFMDEPTGGLDVsvqarllDLLRGL---VRELGLA 204
|
....*..
gi 490363216 205 MIIISHD 211
Cdd:PRK11701 205 VVIVTHD 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-513 |
3.08e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIaKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTL--VGELTPD---NGRVK------WSENATI 385
Cdd:PRK14267 2 KFAIETVNL-RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEarvEGEVRlfgrniYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 386 GYYAQDHATDFEV-----DMTVFDWMSLWMKpeddeqsvrsvLGRLLFSQDDIKKSVK---------------------V 439
Cdd:PRK14267 81 IEVRREVGMVFQYpnpfpHLTIYDNVAIGVK-----------LNGLVKSKKELDERVEwalkkaalwdevkdrlndypsN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 440 LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD---MESIESLNMALElYQGTLIFVSHDREFVSSLAN--------RIIE 508
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELK-KEYTIVLVTHSPAQAARVSDyvaflylgKLIE 228
|
....*
gi 490363216 509 ITPEK 513
Cdd:PRK14267 229 VGPTR 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-210 |
3.13e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.51 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKfgGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQ 71
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttpPSRRpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 DQFAYEEFTVLDTVIMG-HAELWEIKQERERiysLPEMSEEEGLrvadlevkfgemdgytvesragELLLNvGIPleqhn 150
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlNPGLKLNAAQREK---LHAIARQMGI----------------------EDLLA-RLP----- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 151 gpmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISH 210
Cdd:PRK10771 128 ---GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-506 |
3.20e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIAKGYE--ANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKwsENATIGYYAQDhat 394
Cdd:PRK14246 5 KSAEDVFNISRLYLyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 DFEVD--------------------MTVFDWMSLWMKPE--DDEQSVRSVLGRLLFS-------QDDIKKSVKVLSGGEK 445
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfphLSIYDNIAYPLKSHgiKEKREIKKIVEECLRKvglwkevYDRLNSPASQLSGGQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363216 446 GRMLFGKLMMQKPNVLIMDEPTNHLDM---ESIESLNMALElYQGTLIFVSHDREFVSSLANRI 506
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELK-NEIAIVIVSHNPQQVARVADYV 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-187 |
3.35e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.63 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGS-----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD-------PNER--- 65
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklPEYKrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 66 -LGKLKQDQFayeeftvldtviMGHAelweikqereriyslPEMSEEEGLRVADLEVK-FGEMDGYTVESRA--GELLLN 141
Cdd:COG1101 81 yIGRVFQDPM------------MGTA---------------PSMTIEENLALAYRRGKrRGLRRGLTKKRRElfRELLAT 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 142 VGIPLEQH-NGPMSevapgwklrvLLA----QAL------FADPDILLLDEPTNNLD 187
Cdd:COG1101 134 LGLGLENRlDTKVG----------LLSggqrQALsllmatLTKPKLLLLDEHTAALD 180
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-213 |
3.86e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGgDLAPTSGNVFLDpnerlGKLKQ-DQFAYEEftvld 83
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVE-----GRVEFfNQNIYER----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 tvimgHAELWEIKQERERIYSLPE---MSEEE----GLRVADLEVKFgEMDGyTVES--RAGELLLNVGIPLeqHNGPMs 154
Cdd:PRK14258 80 -----RVNLNRLRRQVSMVHPKPNlfpMSVYDnvayGVKIVGWRPKL-EIDD-IVESalKDADLWDEIKHKI--HKSAL- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQTLNERNS-TMIIISHDRH 213
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSElTMVIVSHNLH 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-210 |
3.90e-07 |
|
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: 50.96 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDP-----------NERLGKLKQ 71
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 DQFAYEEfTV---LDtvIMGH---AELWEIKQE---RERIYSLPEmseeeGLrvaDLEVKfgemdgytvesrAGELLLNV 142
Cdd:cd03244 86 DPVLFSG-TIrsnLD--PFGEysdEELWQALERvglKEFVESLPG-----GL---DTVVE------------EGGENLSV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 143 GIpleqhngpmsevapgwklRVL--LAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:cd03244 143 GQ------------------RQLlcLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-507 |
5.03e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNV-FLDPNERLGKLKQDQfayeeftvldtvimgHAELWEIKQERERIyslPEMS 109
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSSQ---------------EAGIGIIHQELNLI---PQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 110 EEEGLRVA-DLEVKFGEMDGYTVESRAGELLLNVGIPLEQHNgPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNL-D 187
Cdd:PRK10762 96 IAENIFLGrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDK-LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 188 IDT------IRwleqTLNERNSTMIIISHDRHFLNMVCTHMADLDYGGLTvhpgnyDEYMLAATQaRERLLadnakkkaq 261
Cdd:PRK10762 175 TETeslfrvIR----ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI------AEREVADLT-EDSLI--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 262 iselQSFVSRfsanasksrqatsrakqiekiQLTEvkassrQNPfiRFEQEKKLFRnaLEVENIAKgyeantPLFKDVNM 341
Cdd:PRK10762 235 ----EMMVGR---------------------KLED------QYP--RLDKAPGEVR--LKVDNLSG------PGVNDVSF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 342 MLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENAT------------IGYYAQDHATDFEV-DMTVFDWMSL 408
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqdglangIVYISEDRKRDGLVlGMSVKENMSL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 409 -----------WMKPEDDEQSVRSVLGrlLF-----SQDDIkksVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDM 472
Cdd:PRK10762 354 talryfsraggSLKHADEQQAVSDFIR--LFniktpSMEQA---IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490363216 473 ESIEslnmalELYQ--------G-TLIFVSHDREFVSSLANRII 507
Cdd:PRK10762 429 GAKK------EIYQlinqfkaeGlSIILVSSEMPEVLGMSDRIL 466
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
5.23e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.14 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE----------RLGKLK 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiaRMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 71 --QDQFAYEEFTVLDTVIMGH---------AELWEIKQEREriyslpemSEEEGLrvadlevkfgemdgytveSRAGELL 139
Cdd:PRK11300 85 tfQHVRLFREMTVIENLLVAQhqqlktglfSGLLKTPAFRR--------AESEAL------------------DRAATWL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 140 LNVGIpLEQHNGPMSEVAPGWKLRVLLAQALFADPDILLLDEP--------TNNLD--IDTIRwleqtlNERNSTMIIIS 209
Cdd:PRK11300 139 ERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPaaglnpkeTKELDelIAELR------NEHNVTVLLIE 211
|
..
gi 490363216 210 HD 211
Cdd:PRK11300 212 HD 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
320-504 |
5.93e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFK---------DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYyaq 390
Cdd:PRK11308 6 LQAIDLKKHYPVKRGLFKperlvkaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHATDF----EVDMtVFD--WMSLwmkpeDDEQSVRSVLGRLLFSQDDIKKS---VKVL--------------------S 441
Cdd:PRK11308 83 DPEAQKllrqKIQI-VFQnpYGSL-----NPRKKVGQILEEPLLINTSLSAAerrEKALammakvglrpehydryphmfS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 442 GGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMeSIES--LNMALELYQ--GT-LIFVSHDREFVSSLAN 504
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAqvLNLMMDLQQelGLsYVFISHDLSVVEHIAD 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
333-494 |
6.20e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 333 TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW-SENATIGYYAQ-----DHATDFEVDMTVFDWM 406
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRSRfmaylGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 407 SLW-----MKPEDDEQSVRSVLGRLLFSQddikKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMA 481
Cdd:PRK13543 104 HFLcglhgRRAKQMPGSALAIVGLAGYED----TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 490363216 482 LELY---QGTLIFVSH 494
Cdd:PRK13543 180 ISAHlrgGGAALVTTH 195
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-224 |
8.80e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.22 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAPTSGNVFLD-------PNERLGK----LKQDQ---FAYEEFTVLDTv 85
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNgrplsdwSAAELARhrayLSQQQsppFAMPVFQYLAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 86 imgHaelweikqereriYSLPEMSEEEGLRVADLEVKFGEMDGYtveSRagelllnvgiPLEQHNGpmsevapG-WKlRV 164
Cdd:COG4138 93 ---H-------------QPAGASSEAVEQLLAQLAEALGLEDKL---SR----------PLTQLSG-------GeWQ-RV 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 165 LLAQALF-----ADPD--ILLLDEPTNNLDI------DtiRWLEQtLNERNSTMIIISHDrhfLNMVCTHmAD 224
Cdd:COG4138 136 RLAAVLLqvwptINPEgqLLLLDEPMNSLDVaqqaalD--RLLRE-LCQQGITVVMSSHD---LNHTLRH-AD 201
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-183 |
9.07e-07 |
|
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: 49.98 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQ---------------FAyeEFTVLDTVIMG---HAEL 92
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRiarlgigyvpegrriFP--SLTVEENLLLGayaRRDR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 93 WEIKQERERIYSL-PEMSEeeglRvadLEVKFGEMDGytvesraGElllnvgiplEQhngpMseVApgwklrvlLAQALF 171
Cdd:COG0410 110 AEVRADLERVYELfPRLKE----R---RRQRAGTLSG-------GE---------QQ----M--LA--------IGRALM 152
|
170
....*....|..
gi 490363216 172 ADPDILLLDEPT 183
Cdd:COG0410 153 SRPKLLLLDEPS 164
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
319-474 |
9.81e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.27 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 319 ALEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENATIGYYAQ 390
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 391 DHATDFEVDMTVFDWMSL-------WMK--PEDDEQSVRSVLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 461
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMgryghmgWLRraKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170
....*....|...
gi 490363216 462 IMDEPTNHLDMES 474
Cdd:PRK15056 165 LLDEPFTGVDVKT 177
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-218 |
1.08e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLA--PTSGNVF--------LDPNER--LGK 68
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILfkgesildLEPEERahLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 69 LKQDQFAYEeftvldtvIMG--HAELWEIK-QERERIYSLPEMSEEEGLRVADLEVKFGEMDGyTVESRagelllNVGip 145
Cdd:CHL00131 87 FLAFQYPIE--------IPGvsNADFLRLAyNSKRKFQGLPELDPLEFLEIINEKLKLVGMDP-SFLSR------NVN-- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 146 lEQHNGpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN---ERNSTMIIISHDRHFLNMV 218
Cdd:CHL00131 150 -EGFSG-------GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINklmTSENSIILITHYQRLLDYI 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
337-525 |
1.09e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.80 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 337 KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENATIGYYAQDHATDFEV-----DMTVF 403
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVRRKKIAMVFQSfalmpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 404 DWMSLWMK----PEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD----MESI 475
Cdd:PRK10070 125 DNTAFGMElagiNAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQ 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 476 ESLNMALELYQGTLIFVSHDREFVSSLANRIIEITPEKVTNFqGTYDEFL 525
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV-GTPDEIL 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
344-509 |
1.18e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.58 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 344 EVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENatigyyaQDHAT----DFEVDM-----------TVFDWMSL 408
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNG-------QDHTTtppsRRPVSMlfqennlfshlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 409 WMKP-----EDDEQSVRSVLGRlLFSQDDIKKSVKVLSGGEKGRMLFGK-LMMQKPnVLIMDEPTNHLD----MESIESL 478
Cdd:PRK10771 95 GLNPglklnAAQREKLHAIARQ-MGIEDLLARLPGQLSGGQRQRVALARcLVREQP-ILLLDEPFSALDpalrQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|.
gi 490363216 479 NMALELYQGTLIFVSHDREFVSSLANRIIEI 509
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVV 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-210 |
1.26e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERLGKL--KQDQFAYEEFTVL--------DT 84
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMtnEQDYQGDEEQNVGmknvnefsLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAELWEIKQERERI---------YSLPEM-------SEEEGLRVADL--EVKFGEMDGyTVE--SRA------GEL 138
Cdd:PTZ00265 1262 KEGGSGEDSTVFKNSGKIlldgvdicdYNLKDLrnlfsivSQEPMLFNMSIyeNIKFGKEDA-TREdvKRAckfaaiDEF 1340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 139 LLNVGIPLEQHNGPMSE-VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTL----NERNSTMIIISH 210
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-377 |
1.27e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 1.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 320 LEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV 377
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-471 |
1.67e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENA-------------TIGYYAQD-----HA 393
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQVATVFQDpeqqiFY 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 394 TDFEVDMTvFDWMSLWMKPEDDEQSVRSVLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD 471
Cdd:PRK13638 93 TDIDSDIA-FSLRNLGVPEAEITRRVDEAL-TLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-494 |
1.80e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIAKGYeANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTL--VGELTPDnGRVKwsenatiGYYAQDHAT 394
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPE-ARVS-------GEVYLDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 DFEVD--------------------MTVFDWMSLWMK-------PEDDEQSVRSVLGRLLFsQDDIKKSVKV----LSGG 443
Cdd:PRK14247 72 IFKMDvielrrrvqmvfqipnpipnLSIFENVALGLKlnrlvksKKELQERVRWALEKAQL-WDEVKDRLDApagkLSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 444 EKGRMLFGKLMMQKPNVLIMDEPTNHLDMES---IESLNMALElYQGTLIFVSH 494
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELK-KDMTIVLVTH 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
332-481 |
1.83e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.80 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGeLTPDNGRVkwseNATIGYYAQDHATDFEVdmtvFDWMSLWMK 411
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSV----EGDIHYNGIPYKEFAEK----YPGEIIYVS 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 412 PEDDEQSVRSVLGRLLFS---QDDikKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDmeSIESLNMA 481
Cdd:cd03233 90 EEDVHFPTLTVRETLDFAlrcKGN--EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTALEIL 158
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-78 |
1.87e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 1.87e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNerlgKLKQDQFAYEE 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ----SIKKDLCTYQK 74
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
335-506 |
2.03e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 335 LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELT----PDNGRV-----------------KWSENATIGYYAQDHA 393
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaPRGARVtgdvtlngeplaaidapRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 394 TDFEVDMTVfdwmSLWMKPE-----DDEQSVRSVLGRLLFSQDD---IKKSVKVLSGGEKGRMLFGKLMMQ--------- 456
Cdd:PRK13547 96 FAFSAREIV----LLGRYPHarragALTHRDGEIAWQALALAGAtalVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 457 KPNVLIMDEPTNHLDMESIESL-----NMALELYQGTLIFVsHDREFVSSLANRI 506
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLldtvrRLARDWNLGVLAIV-HDPNLAARHADRI 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-506 |
2.08e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGYYAQDhATDFEV- 398
Cdd:PRK11288 5 LSFDGIGKTFPGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-ALAAGVa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 399 ----------DMTVFDWMSLWMKPE-----DDEQSVRSVLGRLLFSQDDIKKSVKV--LSGGEKGRMLFGKLMMQKPNVL 461
Cdd:PRK11288 83 iiyqelhlvpEMTVAENLYLGQLPHkggivNRRLLNYEAREQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490363216 462 IMDEPTNHLDMESIESLnMAL--ELY-QGT-LIFVSHDREFVSSLANRI 506
Cdd:PRK11288 163 AFDEPTSSLSAREIEQL-FRVirELRaEGRvILYVSHRMEEIFALCDAI 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
335-495 |
2.20e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.40 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 335 LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENA---TIGYYAQD-HATDfevDMTV 402
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSKAfarKVAYLPQQlPAAE---GMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 403 FDWMSLWMKPEddeqsvRSVLGRllFSQDDIKKS----------------VKVLSGGEKGRMLFGKLMMQKPNVLIMDEP 466
Cdd:PRK10575 103 RELVAIGRYPW------HGALGR--FGAADREKVeeaislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190
....*....|....*....|....*....|...
gi 490363216 467 TNHLDM-ESIESLNMALELYQG---TLIFVSHD 495
Cdd:PRK10575 175 TSALDIaHQVDVLALVHRLSQErglTVIAVLHD 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-219 |
2.22e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTF-MKILggDLAPTSGNVFLD--PNERLGKLKQDQFayeeftvldtvimg 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALL--RLINSQGEIWFDgqPLHNLNRRQLLPV-------------- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 89 haelweikqeRERIY--------SL-PEMSE----EEGLRVADLEVKFGEmdgytVESRAGELLLNVGI-PLEQHNGPmS 154
Cdd:PRK15134 361 ----------RHRIQvvfqdpnsSLnPRLNVlqiiEEGLRVHQPTLSAAQ-----REQQVIAVMEEVGLdPETRHRYP-A 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQTLNERNS-TMIIISHDRHFLNMVC 219
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLQQKHQlAYLFISHDLHVVRALC 493
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
332-507 |
2.30e-06 |
|
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: 48.62 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 332 NTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSENATIGY---YAQDHATDFEVDMTVF----- 403
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkYLHSKVSLVGQEPVLFarslq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 404 DWMSLWMKPEDDEQSVRSVLGRLLFS---------QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES 474
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKAHAHSfiselasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 490363216 475 IESLNMAleLYQG----TLIFVSHDREFVSSlANRII 507
Cdd:cd03248 186 EQQVQQA--LYDWperrTVLVIAHRLSTVER-ADQIL 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
2.32e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.36 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLF--ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlgklkqdqfayeeftvl 82
Cdd:PRK13648 11 KNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 83 DTVIMGHaELWEIKQERERIYSLPEmSEEEGLRVAdLEVKFGeMDGYTV-----ESRAGELLLNVGIpLEQHNGPMSEVA 157
Cdd:PRK13648 70 NQAITDD-NFEKLRKHIGIVFQNPD-NQFVGSIVK-YDVAFG-LENHAVpydemHRRVSEALKQVDM-LERADYEPNALS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363216 158 PGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQtlnERNSTMIIISHD 211
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDpdarqnlLDLVRKVKS---EHNITIISITHD 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-217 |
2.36e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.88 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 11 FGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLAP---TSGNVFL----------DPNE---RLGKLKQ- 71
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPgarVEGEILLdgediydpdvDVVElrrRVGMVFQk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 72 -DQFAyeeFTVLDTVIMGhAELWEIKQEREriyslpeMSE--EEGLRVADL--EVKfgemDgytvesRagellLNvgipl 146
Cdd:COG1117 101 pNPFP---KSIYDNVAYG-LRLHGIKSKSE-------LDEivEESLRKAALwdEVK----D------R-----LK----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 147 eqhngpmsevAPGWKL------RVLLAQALFADPDILLLDEPTNNLD-IDTIRwLEQTLNE--RNSTMIIISHdrhflNM 217
Cdd:COG1117 150 ----------KSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILElkKDYTIVIVTH-----NM 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-210 |
2.62e-06 |
|
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: 47.93 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAP--TSGNVFLD--------PNERLGKLKQDQFAYEEFTV 81
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgrpldkrsFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 82 LDTvIMGHAELweikqereriyslpemseeEGLrvadlevkfgemdgytvesRAGElllnvgipleqhngpmsevapgwK 161
Cdd:cd03213 100 RET-LMFAAKL-------------------RGL-------------------SGGE-----------------------R 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQTlnerNSTMIIISH 210
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIH 169
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-187 |
2.63e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.01 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLAPTSGNVFLDpnerlGKLKQDQFayeeftvldTVIMGH 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILIN-----GRPLDKNF---------QRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 90 AELWEIKqereriysLPEMSEEEGLRV-ADLEvkfgemdgytvesragelllnvGIPLEQhngpmsevapgwKLRVLLAQ 168
Cdd:cd03232 84 VEQQDVH--------SPNLTVREALRFsALLR----------------------GLSVEQ------------RKRLTIGV 121
|
170
....*....|....*....
gi 490363216 169 ALFADPDILLLDEPTNNLD 187
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLD 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-210 |
2.75e-06 |
|
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: 50.29 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILgGDLAPTSGNVFLDpnerlgKLKQDQFAYEE---- 78
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQID------GVSWNSVTLQTwrka 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 79 FTVLDTVIMGHAELWeikqeRERIYSLPEMSEEEGLRVADlEVKFGEMdgytVESRAGEL---LLNVGIPLEQhngpmse 155
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTF-----RKNLDPYEQWSDEEIWKVAE-EVGLKSV----IEQFPDKLdfvLVDGGYVLSN------- 1356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363216 156 vapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:TIGR01271 1357 ---GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsfSNCTVILSEH 1410
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
350-507 |
2.81e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 49.33 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 350 AILGTNGVGKSTMIKTLVGELTPDNGRVK-----WSENAT----------IGYYAQDHAtdfevdmtVFDWMS------- 407
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSARgiflpphrrrIGYVFQEAR--------LFPHLSvrgnlly 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 408 -LW-MKPEDDEQSVRSV-----LGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES------ 474
Cdd:COG4148 101 gRKrAPRAERRISFDEVvellgIGHLL------DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeilp 174
|
170 180 190
....*....|....*....|....*....|....
gi 490363216 475 -IESLNMALELyqgTLIFVSHDREFVSSLANRII 507
Cdd:COG4148 175 yLERLRDELDI---PILYVSHSLDEVARLADHVV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-505 |
2.92e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTL--VGELTPD---------NGRVKWSENA----- 383
Cdd:PRK14239 6 LQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivyNGHNIYSPRTdtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 384 --TIGYYAQdHATDFEvdMTVFDWM--SLWMKPEDDEQSVRSVLGRLLFS-------QDDIKKSVKVLSGGEKGRMLFGK 452
Cdd:PRK14239 85 rkEIGMVFQ-QPNPFP--MSIYENVvyGLRLKGIKDKQVLDEAVEKSLKGasiwdevKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 453 LMMQKPNVLIMDEPTNHLDMES---IESLNMALElYQGTLIFVSHDREFVSSLANR 505
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISagkIEETLLGLK-DDYTMLLVTRSMQQASRISDR 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
339-471 |
4.21e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 339 VNMMLEVGEKVAILGTNGVGKSTMIKTLVGELT---------PDNGRVKWSENATIGYYAQD-----HATDFEVdmTVFd 404
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnftgtilANNRKPTKQILKRTGFVTQDdilypHLTVRET--LVF- 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 405 wMSLWMKPEDDEQSVRSVLGRLLFSQDDIKKS---------VKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD 471
Cdd:PLN03211 164 -CSLLRLPKSLTKQEKILVAESVISELGLTKCentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-248 |
4.81e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.05 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFL-NMVCTHMADldyGGLTVHPGNYDE 239
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHRLTGLeQFDRICVMD---NGQIIEQGTHQE 559
|
....*....
gi 490363216 240 ymLAATQAR 248
Cdd:PRK11160 560 --LLAQQGR 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-213 |
6.28e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.24 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVF---------LDP-NERLGKLKQDQFAYEEFTVLD 83
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLvggkdietnLDAvRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 TVIMgHAELWEIKQERERIySLPEMSEEEGLRvadlevkfgemdgytvesragelllnvgiplEQHNGPMSEVAPGWKLR 163
Cdd:TIGR01257 1023 HILF-YAQLKGRSWEEAQL-EMEAMLEDTGLH-------------------------------HKRNEEAQDLSGGMQRK 1069
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISHDRH 213
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-507 |
9.11e-06 |
|
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: 47.74 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPLFK---DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGeLTPDNGRV------------KWSENA- 383
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITsgeilfdgedllKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 384 ------TIGYYAQDHATDFEVDMTVFDWMS------LWMKPEDDEQSVRSVLGRLlfsqdDIKKSVKV-------LSGGE 444
Cdd:COG0444 81 rkirgrEIQMIFQDPMTSLNPVMTVGDQIAeplrihGGLSKAEARERAIELLERV-----GLPDPERRldrypheLSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDMeSIES--LNMALEL---YQGTLIFVSHDREFVSSLANRII 507
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLNLLKDLqreLGLAILFITHDLGVVAEIADRVA 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-212 |
1.06e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 32 LIGANGSGKSTFMKILGGDLAPTSGNVFLDPNE--------------RLGKLKQDQFAYEEFTVLDTVimghaelweikq 97
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlknrevpflrrQIGMIFQDHHLLMDRTVYDNV------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 98 ereriySLPemseeegLRVADlevkfgeMDGYTVESRAGELLLNVGIPLEQHNGPMsEVAPGWKLRVLLAQALFADPDIL 177
Cdd:PRK10908 101 ------AIP-------LIIAG-------ASGDDIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 490363216 178 LLDEPTNNLD----IDTIRWLEQtLNERNSTMIIISHDR 212
Cdd:PRK10908 160 LADEPTGNLDdalsEGILRLFEE-FNRVGVTVLMATHDI 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
325-526 |
1.10e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 325 IAKGY-----EANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNG-------------RVKWSENATIg 386
Cdd:PLN03130 617 IKNGYfswdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvirgtvayvpQVSWIFNATV- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 yyaQDH---ATDFEvdmtvfdwmslwmkPEDDEQSVR-SVLGR---LLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQK 457
Cdd:PLN03130 696 ---RDNilfGSPFD--------------PERYERAIDvTALQHdldLLPGGDltEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363216 458 PNVLIMDEPTNHLDME-SIESLNMAL--ELYQGTLIFVSHDREFVSSLaNRIIEITPEKVTNfQGTYDEFLA 526
Cdd:PLN03130 759 SDVYIFDDPLSALDAHvGRQVFDKCIkdELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE-EGTYEELSN 828
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
310-530 |
1.14e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 310 EQEK-------KLFRNALEVENIAKGYE-ANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLV-------GELTPDN 374
Cdd:PRK11176 325 EQEKdegkrviERAKGDIEFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEILLDG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 375 GRVK-------------WSENA---------TIGYYAQD--------------HATDFEVDMtvfdwmslwmkpeddEQS 418
Cdd:PRK11176 405 HDLRdytlaslrnqvalVSQNVhlfndtianNIAYARTEqysreqieeaarmaYAMDFINKM---------------DNG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 419 VRSVLGrllfsqddikKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALELYQG--TLIFVSHDR 496
Cdd:PRK11176 470 LDTVIG----------ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRL 539
|
250 260 270
....*....|....*....|....*....|....
gi 490363216 497 EFVSSlANRIIEITPEKVTNfQGTYDEFLAKKGI 530
Cdd:PRK11176 540 STIEK-ADEILVVEDGEIVE-RGTHAELLAQNGV 571
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
351-479 |
1.23e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 351 ILGTNGVGKSTMIKTLVGELTPDNGRVkWSENATIGYYAQ------DHATDFEVDMTVFDWMSLWMKPEDDEQSVRSVLG 424
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNI-YYKNCNINNIAKpyctyiGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIH 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 425 RLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLN 479
Cdd:PRK13541 110 YFKL-HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
320-507 |
1.43e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTP----LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV---------KWSENATIG 386
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 387 YYAQDHATDFE-----VDMtVF--------------DWM----SLWMKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGG 443
Cdd:PRK13631 102 NPYSKKIKNFKelrrrVSM-VFqfpeyqlfkdtiekDIMfgpvALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 444 EKGRMLFGKLMMQKPNVLIMDEPTNHLDMESiESLNMALEL----YQGTLIFVSHDREFVSSLANRII 507
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKG-EHEMMQLILdakaNNKTVFVITHTMEHVLEVADEVI 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
340-516 |
1.90e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 340 NMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--KWSENATIGYYAQDHATDFEVDMTVFDWMSLwmKPEDDEQ 417
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsQFSHITRLSFEQLQKLVSDEWQRNNTDMLSP--GEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 418 SVRSVLgrllfsQDDIKKSV-------------------KVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESL 478
Cdd:PRK10938 101 TTAEII------QDEVKDPArceqlaqqfgitalldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490363216 479 NMALE-LYQG--TLIFVShdrefvsslaNRIIEItPEKVTN 516
Cdd:PRK10938 175 AELLAsLHQSgiTLVLVL----------NRFDEI-PDFVQF 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-215 |
2.01e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 138 LLLNVGI---PLEQhngPMSEVAPGWKLRVLLAQALFADPD--ILLLDEPTNNLDIDTIRWLEQTLNE---RNSTMIIIS 209
Cdd:cd03238 70 FLIDVGLgylTLGQ---KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlidLGNTVILIE 146
|
....*.
gi 490363216 210 HDRHFL 215
Cdd:cd03238 147 HNLDVL 152
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-222 |
2.30e-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: 45.86 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKLKQDQFAYEEFTVLDTvimghaeLWEIKQereRIYSLPEMSE 110
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRDL-------LSSITK---DFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 111 E--EGLRVADLevkfgeMDGYTVESRAGELllnvgipleQhngpmsevapgwklRVLLAQALFADPDILLLDEPTNNLDI 188
Cdd:cd03237 98 EiaKPLQIEQI------LDREVPELSGGEL---------Q--------------RVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490363216 189 dtirwlEQTL----------NERNSTMIIISHDRHFLNMVCTHM 222
Cdd:cd03237 149 ------EQRLmaskvirrfaENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-58 |
2.42e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 2.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490363216 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNV 58
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
440-512 |
2.45e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 2.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 440 LSGGEKGRMLFGKLMMQ--KPNVLIMDEPTNHLDMESIESLNMALE--LYQG-TLIFVSHDREFVSSlANRIIEITPE 512
Cdd:cd03238 88 LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKglIDLGnTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-61 |
2.59e-05 |
|
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: 46.71 E-value: 2.59e-05
10 20 30
....*....|....*....|....*....|
gi 490363216 32 LIGANGSGKSTFMKILGGDLAPTSGNVFLD 61
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
320-508 |
3.06e-05 |
|
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: 45.18 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANTPL-FKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGR-----VKWSenaTIGYYA---- 389
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgVDIS---KIGLHDlrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 390 -----QD----------------HATDFEVdMTVFDWMSLWmkpeddeQSVRSVLGRLlfsQDDIKKSVKVLSGGEKGRM 448
Cdd:cd03244 80 isiipQDpvlfsgtirsnldpfgEYSDEEL-WQALERVGLK-------EFVESLPGGL---DTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 449 LFGKLMMQKPNVLIMDEPTNHLDMESIESLNMAL--ELYQGTLIFVSH--------DREFVSSlANRIIE 508
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIreAFKDCTVLTIAHrldtiidsDRILVLD-KGRVVE 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-248 |
3.15e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 32 LIGANGSGKSTFMKILGGdLAPTSGNVFLDpnerlGKLKQDQFAYEeftvldtviMGHAELWEIKQERErIYSLP----- 106
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIQFA-----GQPLEAWSAAE---------LARHRAYLSQQQTP-PFAMPvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 107 EMSEEEGLRVADLEVKFGEMDGytvesragelLLNVGIPLEQHNGPMS--EvapgWKlRVLLAQA-LFADPDI------L 177
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEVAE----------ALGLDDKLGRSVNQLSggE----WQ-RVRLAAVvLQVWPDInpagqlL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 178 LLDEPTNNLDIDTIRWLEQTLNERNS---TMIIISHDrhfLNMVCTHmAD----LDYGGLTVHpGNYDEYMLAATQAR 248
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD---LNHTLRH-ADrvwlLKQGKLLAS-GRRDEVLTPENLAQ 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-211 |
3.49e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 27 GNRYGLIGANGSGKSTFMKILGGDLAP---TSGNVFLD-------PNERLGKLKQDQFAY---EEFTVLDTVIMGHAELW 93
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNgreilnlPEKELNKLRAEQISMifqDPMTSLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 EIKQERERiyslpeMSE----EEGLRVADlEVKFGE----MDGYTvesragelllnvgipleqHngpmsEVAPGWKLRVL 165
Cdd:PRK09473 122 EVLMLHKG------MSKaeafEESVRMLD-AVKMPEarkrMKMYP------------------H-----EFSGGMRQRVM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363216 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNER----NSTMIIISHD 211
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkrefNTAIIMITHD 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
440-506 |
3.50e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 3.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 440 LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDM-----------ESIESLNMAlelyqgtLIFVSHDREFVSSLANRI 506
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilqllrELQQELNMG-------LLFITHNLSIVRKLADRV 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-216 |
4.19e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDL--APTSGNVfldpnerlgKLKQDQFaYEEFTVLDtvimghae 91
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---------DVPDNQF-GREASLID-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 92 lweikqereRIYSLPEMSEeeglrvadlevkfgemdgytvesrAGELLLNVGI---PLeqHNGPMSEVAPGWKLRVLLAQ 168
Cdd:COG2401 105 ---------AIGRKGDFKD------------------------AVELLNAVGLsdaVL--WLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490363216 169 ALFADPDILLLDEPTNNLDIDTIRWLEQTL----NERNSTMIIISHDRHFLN 216
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLqklaRRAGITLVVATHHYDVID 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
337-506 |
4.33e-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: 45.33 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 337 KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENATIGYYAQDHATDFE-----VDMTVF 403
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaAMSRKELRELRRKKISMVFQsfallPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 404 DWMSLWM------KPEDDEQSVRSVlgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD------ 471
Cdd:cd03294 121 ENVAFGLevqgvpRAEREERAAEAL--ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirre 198
|
170 180 190
....*....|....*....|....*....|....*
gi 490363216 472 MESiESLNMALELyQGTLIFVSHDREFVSSLANRI 506
Cdd:cd03294 199 MQD-ELLRLQAEL-QKTIVFITHDLDEALRLGDRI 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
159-297 |
4.40e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIdTIRwlEQTLN-------ERNSTMIIISHDrhfLNMVcTHMAD---LDYG 228
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDV-SVQ--AQVLNlmmdlqqELGLSYVFISHD---LSVV-EHIADevmVMYL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 229 GLTV-------------HPgnYDEYMLAATqarERLLADNAKKKAQIS-ELQSFVS-----RFSAnasKSRQATSRAKQi 289
Cdd:PRK11308 231 GRCVekgtkeqifnnprHP--YTQALLSAT---PRLNPDDRRERIKLTgELPSPLNpppgcAFNA---RCPRAFGRCRQ- 301
|
....*...
gi 490363216 290 EKIQLTEV 297
Cdd:PRK11308 302 EQPQLRDY 309
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
335-471 |
4.54e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 335 LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVkWSENaTIGYYAQDhatDFEVDMTVFDWMsLWMKPED 414
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAER-SIAYVPQQ---AWIMNATVRGNI-LFFDEED 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 415 D------------EQSVRSVLGRLlfsQDDI-KKSVKvLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLD 471
Cdd:PTZ00243 749 AarladavrvsqlEADLAQLGGGL---ETEIgEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
346-494 |
5.58e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 346 GEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------------SENATIGYYAQD-----HAT---------DFEVD 399
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpksSQEAGIGIIHQElnlipQLTiaeniflgrEFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 400 MTVFDWMSlwMKPEDDEqsvrsVLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHL-DMESiESL 478
Cdd:PRK10762 110 FGRIDWKK--MYAEADK-----LLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESL 180
|
170
....*....|....*....
gi 490363216 479 -NMALEL-YQGT-LIFVSH 494
Cdd:PRK10762 181 fRVIRELkSQGRgIVYISH 199
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-224 |
6.72e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 32 LIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKlKQDQFAYEEFTVLDTVIMGHAELWEIKQERERIYSLPEMSEE 111
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLD-----GK-PVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPANPALVEK 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 112 --EGLRVAD-LEVKFGEmdgytvesragelLLNvgIPLEQhngpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDI 188
Cdd:PRK10522 428 wlERLKMAHkLELEDGR-------------ISN--LKLSK----------GQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 189 DTIRWLEQTL----NERNSTMIIISHDRHFLnmvctHMAD 224
Cdd:PRK10522 483 HFRREFYQVLlpllQEMGKTIFAISHDDHYF-----IHAD 517
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-210 |
8.17e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 16 LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDPNERL------------GKLKQDQFAYEEfTVLD 83
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLkdinlkwwrskiGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 84 TVimgHAELWEIKQererIYSLPEMSEEEG--------LRVADLEVKFGEMDGYTVESRAGELL--------------LN 141
Cdd:PTZ00265 479 NI---KYSLYSLKD----LEALSNYYNEDGndsqenknKRNSCRAKCAGDLNDMSNTTDSNELIemrknyqtikdsevVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 142 VGIPLEQHN--------------GPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLN----ERNS 203
Cdd:PTZ00265 552 VSKKVLIHDfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENR 631
|
....*..
gi 490363216 204 TMIIISH 210
Cdd:PTZ00265 632 ITIIIAH 638
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-211 |
9.27e-05 |
|
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: 43.19 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpnerlGKlkqdqfayeEFTVLDTvimghaelw 93
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-----GK---------PVTRRSP--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 eikqeRERIyslpemseEEGLrvadlevkfgemdGYTVESRAGELLL-------NVGIPL------EQhngpmsevapgw 160
Cdd:cd03215 70 -----RDAI--------RAGI-------------AYVPEDRKREGLVldlsvaeNIALSSllsggnQQ------------ 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490363216 161 klRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE---RNSTMIIISHD 211
Cdd:cd03215 112 --KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREladAGKAVLLISSE 163
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
440-507 |
1.02e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 440 LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMeSIES--LNMALELYQG---TLIFVSHDREFVSSLANRII 507
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQAqiIELLLELQQKenmALVLITHDLALVAEAAHKII 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-271 |
1.08e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 152 PMSEVAPGWKLRVLLAQALFA---DPDILLLDEPTNNL---DIDTIRWLEQTLNERNSTMIIISHDRHFLNmVCTHMADL 225
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLEL 884
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490363216 226 DYGGltvhpGNYDEYMLAATQARERLLADNAKKKAqiseLQSFVSR 271
Cdd:PRK00635 885 GPEG-----GNLGGYLLASCSPEELIHLHTPTAKA----LRPYLSS 921
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-368 |
1.13e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490363216 320 LEVENIAKGYEaNTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVG 368
Cdd:CHL00131 8 LEIKNLHASVN-ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
394-527 |
1.28e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 394 TDFEvDMTVFDWMSLWMKPEDDEQSVRSVL----GRLLFSQD------DIKKSVKVLSGGEKGRMLFGK-LMMQKPNVL- 461
Cdd:PRK00635 422 AEFQ-QMSLQELFIFLSQLPSKSLSIEEVLqglkSRLSILIDlglpylTPERALATLSGGEQERTALAKhLGAELIGITy 500
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 462 IMDEPTNHLDMESIESLNMALELY--QG-TLIFVSHDREFVSsLANRIIEITP-------EKVtnFQGTYDEFLAK 527
Cdd:PRK00635 501 ILDEPSIGLHPQDTHKLINVIKKLrdQGnTVLLVEHDEQMIS-LADRIIDIGPgagifggEVL--FNGSPREFLAK 573
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-255 |
1.38e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.45 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISHDRHFLnmvcthmADLDY-----GGLTVHPG 235
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQLEDL-------AQWDQiwvmqDGQIVQQG 565
|
90 100
....*....|....*....|.
gi 490363216 236 NYDEymLAATQ-ARERLLADN 255
Cdd:PRK11174 566 DYAE--LSQAGgLFATLLAHR 584
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-217 |
1.42e-04 |
|
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: 43.51 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 31 GLIGANGSGKSTFMKILGGDLAPTSGNvFLDPNERLGKLK-------QDQFAyeefTVLD---TVIMGHAELWEI-KQER 99
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDefrgselQNYFT----KLLEgdvKVIVKPQYVDLIpKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 100 ERIYSLPEMSEEEGlrVADLEVKFGEMDGYtvesragelllnvgipLEQHngpMSEVAPGWKLRVLLAQALFADPDILLL 179
Cdd:cd03236 105 GKVGELLKKKDERG--KLDELVDQLELRHV----------------LDRN---IDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490363216 180 DEPTNNLDID---TIRWLEQTLNERNSTMIIISHDRHFLNM 217
Cdd:cd03236 164 DEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDY 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
329-474 |
1.52e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 43.00 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 329 YEANTP-----LFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLV---------GELTPDNGRVKWSENATIGYYAQdhat 394
Cdd:cd03232 11 YTVPVKggkrqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktagvitGEILINGRPLDKNFQRSTGYVEQ---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 395 dfevdMTVFDwmslwmkpedDEQSVRSVLgrlLFSQDdikksVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES 474
Cdd:cd03232 87 -----QDVHS----------PNLTVREAL---RFSAL-----LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
154-210 |
1.79e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--RNSTMIIISH 210
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFElkKEYTIVLVTH 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-211 |
2.01e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.86 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLD--------PNER-LGKLKQDQFAY 76
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmndvpPAERgVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 77 EEFTVLDTvimghaelweikqereriyslpeMSEeeGLRVAdlEVKFGEMDGyTVESRAGelLLNVGIPLEQHNGPMSEv 156
Cdd:PRK11000 88 PHLSVAEN-----------------------MSF--GLKLA--GAKKEEINQ-RVNQVAE--VLQLAHLLDRKPKALSG- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490363216 157 apGWKLRVLLAQALFADPDILLLDEPTNNLD--------IDTIRwLEQTLnerNSTMIIISHD 211
Cdd:PRK11000 137 --GQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIEISR-LHKRL---GRTMIYVTHD 193
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-187 |
2.22e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 16 LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdlAPTSGnvFLDPNERLGKL--KQDQFAYeeftvldtvIMGHAELW 93
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDIRISGFpkKQETFAR---------ISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 94 EIKQE----RER-IYS----LP-EMSEEEGLRVADLEVKFGEMDGYTvESRAGeLLLNVGIPLEQhngpmsevapgwKLR 163
Cdd:PLN03140 962 DIHSPqvtvRESlIYSaflrLPkEVSKEEKMMFVDEVMELVELDNLK-DAIVG-LPGVTGLSTEQ------------RKR 1027
|
170 180
....*....|....*....|....
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLD 187
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
438-526 |
2.68e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 438 KVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESieslnmaLELYQGTLIFVSH--DREFVsSLANRIIEI------ 509
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-------EKLIEKTIVDIKDkaDKTII-TIAHRIASIkrsdki 1428
|
90 100
....*....|....*....|....
gi 490363216 510 ----TPEKVTNF---QGTYDEFLA 526
Cdd:PTZ00265 1429 vvfnNPDRTGSFvqaHGTHEELLS 1452
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
317-507 |
2.78e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 317 RNALEVENIAKGYEAN---TPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVK--------------- 378
Cdd:PRK10261 10 RDVLAVENLNIAFMQEqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 379 ---WSENATIGYYAQDHATDFEVDMTVFDwmSLWMKPEDDEQSVRSVLG-----------------RLLFSQDDIKKSVK 438
Cdd:PRK10261 90 lseQSAAQMRHVRGADMAMIFQEPMTSLN--PVFTVGEQIAESIRLHQGasreeamveakrmldqvRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 439 VLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMeSIESLNMAL------ELYQGtLIFVSHDREFVSSLANRII 507
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLikvlqkEMSMG-VIFITHDMGVVAEIADRVL 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-241 |
2.95e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.92 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 5 NNITMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLdpnerlgklkQDQFAYEEF 79
Cdd:PRK13631 25 KNLYCVFDEKQENElvalnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV----------GDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 80 TVLDTVIMGHA-ELWEIKQERERIYSLPEMSEEEGLR-VADLEVKFGEMDGYTVESRAGEL----LLNVGIpleqhNGPM 153
Cdd:PRK13631 95 NNHELITNPYSkKIKNFKELRRRVSMVFQFPEYQLFKdTIEKDIMFGPVALGVKKSEAKKLakfyLNKMGL-----DDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 154 SEVAP-----GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE---RNSTMIIISHDRHFLNMVCTHMADL 225
Cdd:PRK13631 170 LERSPfglsgGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDakaNNKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*.
gi 490363216 226 DYGGLTVHPGNYDEYM 241
Cdd:PRK13631 250 DKGKILKTGTPYEIFT 265
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-211 |
3.52e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.77 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLDpNERLGKlkqdqfayeeftvldtvimghAELWEIKQER 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID-GELLTA---------------------ENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 100 ERIYSLPEmSEEEGLRVADlEVKFG-EMDGYTVES---RAGELLLNVGIpLEQHNGPMSEVAPGWKLRVLLAQALFADPD 175
Cdd:PRK13642 84 GMVFQNPD-NQFVGATVED-DVAFGmENQGIPREEmikRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 176 ILLLDEPTNNLD----IDTIRWLEQTLNERNSTMIIISHD 211
Cdd:PRK13642 161 IIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
410-495 |
4.74e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 410 MKPEDDEQSVRSVLGRLLFSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES---IESLNMALEl 484
Cdd:PRK14243 120 YKGDMDELVERSLRQAALWDEvkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELK- 198
|
90
....*....|.
gi 490363216 485 YQGTLIFVSHD 495
Cdd:PRK14243 199 EQYTIIIVTHN 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-210 |
4.85e-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: 42.81 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 16 LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLAPTSGNVFLDPNErlGKLkqdqfayeeFTVLDTVIMGHAELwei 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRLTKPAK--GKL---------FYVPQRPYMTLGTL--- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 96 kqeRER-IYslPEMSEE---EGLRVADLEVKFGEMD-GYTVESRAGelllnvgipLEQHNGPMSEVAPGWKLRVLLAQAL 170
Cdd:TIGR00954 532 ---RDQiIY--PDSSEDmkrRGLSDKDLEQILDNVQlTHILEREGG---------WSAVQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363216 171 FADPDILLLDEPTNNLDIDTIRWLEQTLNERNSTMIIISH 210
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
159-210 |
6.02e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.17 E-value: 6.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIR----WLEQTLNERNSTMIIISH 210
Cdd:PRK11144 132 GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRellpYLERLAREINIPILYVSH 187
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-215 |
6.25e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 27 GNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFldpnerlgklkqdqfayeeftVLDTVIMGHAELWEIKQERERIYSLP 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------YIDGEDILEEVLDQLLLIIVGGKKAS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 107 EMSEEeglrvadlevkfgemdgytvesragelllnvgipleqhngpmsevapgwKLRVLLAQALFADPDILLLDEPTNNL 186
Cdd:smart00382 61 GSGEL-------------------------------------------------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190
....*....|....*....|....*....|....*...
gi 490363216 187 DIDT---------IRWLEQTLNERNSTMIIISHDRHFL 215
Cdd:smart00382 92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
338-527 |
7.94e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 338 DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV-KWSENATIGYYAQDHATDFEVDMTVFDWMSLWMKPEDDE 416
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 417 QSVRSVLGrllFSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDME-SIESLNMALELYQG--TLIF 491
Cdd:PRK13546 122 AMTPKIIE---FSElgEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQKCLDKIYEFKEQnkTIFF 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 490363216 492 VSHDREFVSSLANRIIEITPEKVTNFqGTYDEFLAK 527
Cdd:PRK13546 199 VSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVLPK 233
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-218 |
1.41e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 1.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490363216 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQTLNE--------RNSTMIIISHDRHFLNMV 218
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEiiksrsqqRNFQLLVITHDEDFVELL 1276
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
423-512 |
1.56e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 423 LGRLLFSqddikksvkvLSGGEKGRM-LFGKLM--MQKPNVLIMDEPTNHLDMESIESLNMALE--LYQG-TLIFVSHDR 496
Cdd:PRK00635 803 LGRPLSS----------LSGGEIQRLkLAYELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQslTHQGhTVVIIEHNM 872
|
90
....*....|....*.
gi 490363216 497 EFVsSLANRIIEITPE 512
Cdd:PRK00635 873 HVV-KVADYVLELGPE 887
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-188 |
1.70e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.16 E-value: 1.70e-03
10 20
....*....|....*....|....*
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDI 188
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
159-211 |
1.75e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.15 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490363216 159 GWKLRVLLAQALFADPDILLLDEPTNNLD-IDTIRwLEQTLNE--RNSTMIIISHD 211
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHElkEQYTIIIVTHN 209
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-59 |
1.81e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363216 1 MLISNNITMQFGSKPLFeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVF 59
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY 58
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
288-377 |
1.94e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.73 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 288 QIEKIQLTEVKAS-SRQNPFIRFEQekklfrnaLEVENIAKGYEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTL 366
Cdd:PRK10522 298 KLNKLALAPYKAEfPRPQAFPDWQT--------LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLL 369
|
90
....*....|.
gi 490363216 367 VGELTPDNGRV 377
Cdd:PRK10522 370 TGLYQPQSGEI 380
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
321-505 |
1.98e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 321 EVENIAKGYEANTPLF---KDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRV--------KWSENA------ 383
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKElrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 384 TIGYYAQdHatdFEV--DMTVFDWMSLWMKpeddeqsvrsvLGRLlfSQDDIKKSV-----------------KVLSGGE 444
Cdd:PRK11153 83 QIGMIFQ-H---FNLlsSRTVFDNVALPLE-----------LAGT--PKAEIKARVtellelvglsdkadrypAQLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490363216 445 KGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLnmaLELYQG-------TLIFVSHDREFVSSLANR 505
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDinrelglTIVLITHEMDVVKRICDR 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
320-476 |
2.13e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 320 LEVENIAKGYEANtPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVG--ELTPDNGRVKWSENATIGYYAQDHATD-- 395
Cdd:PRK09580 2 LSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAGEgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 396 -----FEVDM----------TVFDWMSLWMKPE-----DDEQSVRSVLGRLLFSQDDIKKSVKV-LSGGEKGRMLFGKLM 454
Cdd:PRK09580 81 fmafqYPVEIpgvsnqfflqTALNAVRSYRGQEpldrfDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMA 160
|
170 180
....*....|....*....|..
gi 490363216 455 MQKPNVLIMDEPTNHLDMESIE 476
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALK 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-368 |
2.96e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490363216 320 LEVENIAKGYEANTPLfKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVG 368
Cdd:PRK13549 6 LEMKNITKTFGGVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-188 |
3.45e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.45e-03
10 20
....*....|....*....|....*
gi 490363216 164 VLLAQALFADPDILLLDEPTNNLDI 188
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
429-509 |
6.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 429 SQDDIKKSVKVLSGGEKG------RMLFGKLMMQKPNVLIMDEPTNHLDMESIESLNMALE--LYQGT----LIFVSHDR 496
Cdd:PRK01156 791 SRGGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEysLKDSSdipqVIMISHHR 870
|
90
....*....|...
gi 490363216 497 EFVSSlANRIIEI 509
Cdd:PRK01156 871 ELLSV-ADVAYEV 882
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-237 |
8.35e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.23 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 1 MLISNNITMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLAPTSGNVF--------LDPNERLGKLK 70
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEfkgkdlleLSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 71 QDQFAYE-EFTVLDTVIMGHAELWEIKQEReriyslpemsEEEGLRVADLEvKFGEmDGYTVESRAGELL---LNVGIpl 146
Cdd:PRK09580 81 FMAFQYPvEIPGVSNQFFLQTALNAVRSYR----------GQEPLDRFDFQ-DLME-EKIALLKMPEDLLtrsVNVGF-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 147 eqhngpmsevAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQ---TLNERNSTMIIISHDRHFLNMVCTHMA 223
Cdd:PRK09580 147 ----------SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYIKPDYV 216
|
250
....*....|....
gi 490363216 224 DLDYGGLTVHPGNY 237
Cdd:PRK09580 217 HVLYQGRIVKSGDF 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
338-506 |
8.72e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 338 DVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKWSeNATIGYYAQDHATDFEVDM-----------TVFDWM 406
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ-GKEIDFKSSKEALENGISMvhqelnlvlqrSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 407 SLWMKPE-----DDEQSVRSVlgRLLFSQDDI----KKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIES 477
Cdd:PRK10982 95 WLGRYPTkgmfvDQDKMYRDT--KAIFDELDIdidpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180 190
....*....|....*....|....*....|..
gi 490363216 478 LNMALELYQGT---LIFVSHDREFVSSLANRI 506
Cdd:PRK10982 173 LFTIIRKLKERgcgIVYISHKMEEIFQLCDEI 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
440-474 |
8.83e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.86 E-value: 8.83e-03
10 20 30
....*....|....*....|....*....|....*
gi 490363216 440 LSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMES 474
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
430-509 |
8.86e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 38.15 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 430 QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLIMDEPTNHLDMESIESLnmalelyqgtlifvshdREFVSSLANRIIEI 509
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-----------------EEFIRSLADRLTVI 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-472 |
9.50e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 6 NITMQF-GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLAPTSGNVFLdpnerLGklKQDQFAYEEFTVLDT 84
Cdd:PRK10982 3 NISKSFpGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-----QG--KEIDFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 85 VIMGHAELWEIKQeRERI-------YSLPEMSEEEGLRVADLEVKFGEMDgytVESRAGELLLNVGIPLEQhngpMSEVa 157
Cdd:PRK10982 75 ISMVHQELNLVLQ-RSVMdnmwlgrYPTKGMFVDQDKMYRDTKAIFDELD---IDIDPRAKVATLSVSQMQ----MIEI- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 158 pgwklrvllAQALFADPDILLLDEPTNNL---DIDTIRWLEQTLNERNSTMIIISHDRHFLNMVCTHMADLDYGgltvhp 234
Cdd:PRK10982 146 ---------AKAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 235 gnydeyMLAATQARERLLADnakkkaQISEL---QSFVSRFSanasksrQATSRAKQIekiqltevkassrqnpfirfeq 311
Cdd:PRK10982 211 ------QWIATQPLAGLTMD------KIIAMmvgRSLTQRFP-------DKENKPGEV---------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 312 ekklfrnALEVENIAkgyEANTPLFKDVNMMLEVGEKVAILGTNGVGKSTMIKTLVGELTPDNGRVKW------------ 379
Cdd:PRK10982 250 -------ILEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhgkkinnhnane 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363216 380 ----------SENATIGYYAQDHATDFEVDMTVFDWMSLW--MKPEDDEQSVRSVLGRLLFSQDDIKKSVKVLSGGEKGR 447
Cdd:PRK10982 320 ainhgfalvtEERRSTGIYAYLDIGFNSLISNIRNYKNKVglLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQK 399
|
490 500
....*....|....*....|....*
gi 490363216 448 MLFGKLMMQKPNVLIMDEPTNHLDM 472
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| |
