|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
90-604 |
1.40e-172 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 500.75 E-value: 1.40e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP------IPEHIDIYHLTREMP-PSDKTPLHCV 162
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdsgevsIPKGLRIGYLPQEPPlDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 MEVDTERAMLEKEAERL----AHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVA 238
Cdd:COG0488 83 LDGDAELRALEAELEELeaklAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRL 318
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 319 ELEENQMKRFHWEQDQIAHMKNYIARFGhGSAKLARQAQSKEKTLQKMMAsglTERVVSDKTLSFYFPPCGKIPPPVIMV 398
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFR-AKARKAKQAQSRIKALEKLER---EEPPRRDKTVEIRFPPPERLGKKVLEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 399 QNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHlQEQLDLDLS 478
Cdd:COG0488 319 EGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-QEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 479 PLEYMMKCYPEIKEKeEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADA 558
Cdd:COG0488 396 VLDELRDGAPGGTEQ-EVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 27881506 559 INEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEH 604
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-607 |
4.13e-157 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 468.57 E-value: 4.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 32 DVVTEPQVAEKNEANGRETTEVDLLTKELeDFEMKKAAARAVT----GVLASH------PNSTDVHIINLSLTFHGQELL 101
Cdd:PLN03073 115 EPDDGPLLSERDLAKIERRKRKEERQREV-QYQAHVAEMEAAKagmpGVYVNHdgngggPAIKDIHMENFSISVGGRDLI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 102 SDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-IPEHIDIYHLTREMPPSDKTPLHCVMEVDTERA-MLEKEAERL 179
Cdd:PLN03073 194 VDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQILHVEQEVVGDDTTALQCVLNTDIERTqLLEEEAQLV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 180 AH----------------------EDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRV 237
Cdd:PLN03073 274 AQqrelefetetgkgkgankdgvdKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 238 ALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTR 317
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 318 LELEENQMKRFHWEQDQIAHMKNYIARFGHgSAKLARQAQSKEKTLQKMmasGLTERVVSDKTLSFYFP-PCGKIPPPVI 396
Cdd:PLN03073 434 EEQLKNQQKAFESNERSRSHMQAFIDKFRY-NAKRASLVQSRIKALDRL---GHVDAVVNDPDYKFEFPtPDDRPGPPII 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 397 MVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLD 476
Cdd:PLN03073 510 SFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLS 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 477 LSPLEYMMKCYPEIKEkEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALA 556
Cdd:PLN03073 589 SNPLLYMMRCFPGVPE-QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 27881506 557 DAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHLKS 607
Cdd:PLN03073 668 QGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQS 718
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
100-605 |
7.95e-100 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 317.50 E-value: 7.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 100 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKRE-------VPIPEHIDIYHLTREMPPSDKTPLHCVMEVDTERAML 172
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALL-KNEisadggsYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 173 EKEAErLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLL 252
Cdd:PRK10636 95 EAQLH-DANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 253 DEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQ 332
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 333 DQIAHMKNYIARFGHGSAKlARQAQSKEKTLQKMmasgltERVV---SDKTLSFYFPPCGKIPPPVIMVQNVSFKYTKDg 409
Cdd:PRK10636 254 ERVAHLQSYIDRFRAKATK-AKQAQSRIKMLERM------ELIApahVDNPFHFSFRAPESLPNPLLKMEKVSAGYGDR- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 410 pCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPE 489
Cdd:PRK10636 326 -IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 490 IKEkEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLV 569
Cdd:PRK10636 405 ELE-QKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVV 483
|
490 500 510
....*....|....*....|....*....|....*.
gi 27881506 570 SHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHL 605
Cdd:PRK10636 484 SHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWL 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
90-611 |
3.72e-70 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 236.33 E-value: 3.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTR-------EMPPSDKTPLHCV 162
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERlgklrqdQFAFEEFTVLDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 MEVDTERAMLEKEAERL-AHEDAECEKLM---ELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVA 238
Cdd:PRK15064 86 IMGHTELWEVKQERDRIyALPEMSEEDGMkvaDLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRL 318
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 319 ELEENQMKRFHWEQDQIAHMKNYIARFGHGSAKlARQAQSKEKTLQKMMasgLTE-RVVSDKTLSFYFPPCGKIPPPVIM 397
Cdd:PRK15064 246 QARERLLADNAKKKAQIAELQSFVSRFSANASK-AKQATSRAKQIDKIK---LEEvKPSSRQNPFIRFEQDKKLHRNALE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDL 477
Cdd:PRK15064 322 VENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 478 SPLEYMMKcYPEIKEKEEM-RKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALA 556
Cdd:PRK15064 400 TLFDWMSQ-WRQEGDDEQAvRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLN 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 557 DAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDilaYKEHLKSKLVD 611
Cdd:PRK15064 479 MALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGT---YEEYLRSQGIE 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
97-612 |
3.13e-61 |
|
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: 212.87 E-value: 3.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 97 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLL---SAIGKR---EVPIPEHIDIYHLTREmPPSD--KTPLHCVME-VDT 167
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLrimAGVDKDfngEARPQPGIKVGYLPQE-PQLDptKTVRENVEEgVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 168 ERAMLEKEAE---RLAHEDAECEKLMELYERLEE-LDADKA---EMRASRILHGLGFTPAMQrkKLKDFSGGWRMRVALA 240
Cdd:TIGR03719 96 IKDALDRFNEisaKYAEPDADFDKLAAEQAELQEiIDAADAwdlDSQLEIAMDALRCPPWDA--DVTKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 241 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYV---KTR 317
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLeqkQKR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 318 LELEENQ----MKRFHWEQDQIAHmknyiarfghgSAKlARQAQSKEK--TLQKMMASGLTERvvsDKTLSFYFPPCGKI 391
Cdd:TIGR03719 254 LEQEEKEesarQKTLKRELEWVRQ-----------SPK-GRQAKSKARlaRYEELLSQEFQKR---NETAEIYIPPGPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHlQE 471
Cdd:TIGR03719 319 GDKVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS-RD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 472 QLDLDLSPLEYMMKCYPEIK-EKEEM--RKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKlGKREIpsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 549 IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKW-PGDILAYKEHLKSKLVDE 612
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWfEGNFSEYEEDKKRRLGED 540
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
86-587 |
2.18e-57 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 204.41 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrEVPIPEHIDIYH----LTR--EMPPSDK--T 157
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLLDDGRIIYEqdliVARlqQDPPRNVegT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 158 PLHCVMEVDTERAMLEKEAERLAHE------DAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAmqrKKLKDFSG 231
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLvetdpsEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 232 GWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYD 311
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 312 QYVKTR---LELEENQMKRFhweQDQIAHMKNYI-----ARF----GHGSA-KLARQAQSKEKTLQ---KMMasglterv 375
Cdd:PRK11147 240 QYLLEKeeaLRVEELQNAEF---DRKLAQEEVWIrqgikARRtrneGRVRAlKALRRERSERREVMgtaKMQ-------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 376 VSDKTLSfyfppcGKIpppVIMVQNVSfkYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR 455
Cdd:PRK11147 309 VEEASRS------GKI---VFEMENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 456 KHSHVKIGRYHQHlQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIG---RYGLTGKQQVSPIRNLSDGQKCRVCLAWLAW 532
Cdd:PRK11147 378 CGTKLEVAYFDQH-RAELDPEKTVMDNLAEGKQEVMVNGRPRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFL 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 533 QNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCE 587
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFE 511
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
115-572 |
1.96e-49 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 180.70 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 115 GLIGLNGIGKSMLL---SAIGKR---EVPIPEHIDIYHLTREmPPSD--KTPLHCVME-VDTERAMLEK--E-AERLAHE 182
Cdd:PRK11819 37 GVLGLNGAGKSTLLrimAGVDKEfegEARPAPGIKVGYLPQE-PQLDpeKTVRENVEEgVAEVKAALDRfnEiYAAYAEP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 183 DAECEKLME----LYERLEELDADKAEMRASRILHGLGFTPAMQrkKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNH 258
Cdd:PRK11819 116 DADFDALAAeqgeLQEIIDAADAWDLDSQLEIAMDALRCPPWDA--KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 259 LDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKT---RLELEENQ----MKRFHWE 331
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQkakRLAQEEKQeaarQKALKRE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 332 QDQIAHmknyiarfghgSAKlARQAQSKE--KTLQKMMASGLTERvvsDKTLSFYfppcgkIPPP------VIMVQNVSF 403
Cdd:PRK11819 274 LEWVRQ-----------SPK-ARQAKSKArlARYEELLSEEYQKR---NETNEIF------IPPGprlgdkVIEAENLSK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 404 KYtkDGPCIYNNLEF-----GIdldtrVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHlQEQLDLDLS 478
Cdd:PRK11819 333 SF--GDRLLIDDLSFslppgGI-----VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-RDALDPNKT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 479 PLEymmkcypEIKE--------KEEM--RKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:PRK11819 405 VWE-------EISGgldiikvgNREIpsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
490 500
....*....|....*....|....
gi 27881506 549 IETIDALADAINEFEGGMMLVSHD 572
Cdd:PRK11819 478 VETLRALEEALLEFPGCAVVISHD 501
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
86-302 |
8.14e-48 |
|
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: 164.16 E-value: 8.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHltremppsdktplhcvmev 165
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 dteramlekeAERLAHedaeceklmelYERLeeldadkaemrasrilhglgftpamqrkklkdfSGGWRMRVALARALFI 245
Cdd:cd03221 62 ----------TVKIGY-----------FEQL---------------------------------SGGEKMRLALAKLLLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 246 RPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKK 302
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
396-590 |
9.48e-47 |
|
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: 161.46 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQhlqeqldl 475
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 476 dlspleymmkcypeikekeemrkiigrygltgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDAL 555
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 27881506 556 ADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQT 590
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
88-319 |
2.29e-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: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppSDKTPLHCVMEVDT 167
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI---------DGEDVRKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 168 ERAMLEkeAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRP 247
Cdd:COG4555 75 QIGVLP--DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 248 FMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKLKYY---TGNYDQYVKTRLE 319
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVILHKGKVVAQgslDELREEIGEENLE 229
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
296-366 |
6.21e-25 |
|
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: 98.80 E-value: 6.21e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 296 IHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGsAKLARQAQSKEKTLQKM 366
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAK-ASKAKQAQSRIKALEKM 70
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
101-257 |
5.82e-23 |
|
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: 95.41 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhLTREMPPSDKTPLHcvmevdTERAMLEKEAERLA 180
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL--DGQDLTDDERKSLR------KEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 181 HEDAEcEKLMElYERLEELDADKAEMRASRILHGLGFTPAMQRK---KLKDFSGGWRMRVALARALFIRPFMLLLDEPTN 257
Cdd:pfam00005 73 RLTVR-ENLRL-GLLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
86-585 |
2.67e-22 |
|
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: 100.75 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKREVPIPEHIDIYHL-----TREMPPSDKTP 158
Cdd:COG1123 5 LEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRISGEVLldgrdLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 159 LHCVMEVDTERAMLekeAERLAHEDAECeklmelyerLEELDADKAEM--RASRILHGLGFtPAMQRKKLKDFSGGWRMR 236
Cdd:COG1123 84 RIGMVFQDPMTQLN---PVTVGDQIAEA---------LENLGLSRAEAraRVLELLEAVGL-ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 237 VALARALFIRPFMLLLDEPTNHLD-------LDACVWLEEELKTfkrILVLVSHSQDFLNGVCTNIIHMHNKKLkYYTGN 309
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDvttqaeiLDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVMDDGRI-VEDGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 310 YDQYVKTRLELEEnqmkrfhweqdqiahmknyIARFGHGSAKLARQAQSKEKTLQkmmasgltervVSDktLSFYFPPCG 389
Cdd:COG1123 227 PEEILAAPQALAA-------------------VPRLGAARGRAAPAAAAAEPLLE-----------VRN--LSKRYPVRG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 390 KIPPPVimVQNVSFKytkdgpciynnLEFGidldTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKI 462
Cdd:COG1123 275 KGGVRA--VDDVSLT-----------LRRG----ETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltKLSRRSL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQHLQ-------EQLDldlsP-------LEYMMKCYPEIKEKEEMRKI---IGRYGLTGKQQVSPIRNLSDGQKCRV 525
Cdd:COG1123 338 RELRRRVQmvfqdpySSLN----PrmtvgdiIAEPLRLHGLLSRAERRERVaelLERVGLPPDLADRYPHELSGGQRQRV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 526 CLA-WLAwQNPHMLFLDEPTNHLDIET----IDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:COG1123 414 AIArALA-LEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAV 477
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
88-303 |
6.15e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.42 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGkrevpipeHIDIYH----LTREMPPSDKTPLHCVM 163
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA--------DLDPPTsgeiYLDGKPLSAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 EV-----------DTERAMLEkEAERLAHEDAECEKLMELYERLeeldadkaemrasrilhglGFTPAMQRKKLKDFSGG 232
Cdd:COG4619 75 QVayvpqepalwgGTVRDNLP-FPFQLRERKFDRERALELLERL-------------------GLPPDILDKPVERLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 233 WRMRVALARALFIRPFMLLLDEPTNHLDLD--ACV--WLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:COG4619 135 ERQRLALIRALLLQPDVLLLDEPTSALDPEntRRVeeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
87-302 |
7.49e-21 |
|
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: 89.61 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 87 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsdktplhcvmevd 166
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 167 teramlekeaerlahedaeceklmelyerleeLDADKAEMRASRILHGLGFTPamqrkklkDFSGGWRMRVALARALFIR 246
Cdd:cd00267 59 --------------------------------DGKDIAKLPLEELRRRIGYVP--------QLSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 247 PFMLLLDEPTNHLDLDACVWLEEELKTF---KRILVLVSHSQDFLNGVCTNIIHMHNKK 302
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
90-579 |
2.33e-20 |
|
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: 94.87 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GKREVPIPEHIDIYHLTR-------EMPPSDKTPL-H 160
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrGMDQYEPTSGRIIYHVALcekcgyvERPSKVGEPCpV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 161 C-----VMEVD------TERAMLEKEA----ER---LAHEDAECEKLMELYERLEeLDADKAEMRASRILHGLGFTPAMQ 222
Cdd:TIGR03269 85 CggtlePEEVDfwnlsdKLRRRIRKRIaimlQRtfaLYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 223 RKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVW----LEEELKTFKRILVLVSHSQDFLNGVCTNIIHM 298
Cdd:TIGR03269 164 HIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 299 HNKKLKYyTGNYDQYVKTRLELEENqmkrfhWEQDQIAHMKNYIARFghgsaklarqaqskeKTLQKMMASglTERVVsd 378
Cdd:TIGR03269 243 ENGEIKE-EGTPDEVVAVFMEGVSE------VEKECEVEVGEPIIKV---------------RNVSKRYIS--VDRGV-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 379 ktlsfyfppcgkipppVIMVQNVSFKytkdgpcIYNNLEFGIdldtrvalVGPNGAGKSTLLKLLTGELLPTDG------ 452
Cdd:TIGR03269 297 ----------------VKAVDNVSLE-------VKEGEIFGI--------VGTSGAGKTTLSKIIAGVLEPTSGevnvrv 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 453 ------------MIRKHSHVKIGRYHQ------------HLQEQLDLDLsPLEY-MMKCYPEIK----EKEEMRKIIGRY 503
Cdd:TIGR03269 346 gdewvdmtkpgpDGRGRAKRYIGILHQeydlyphrtvldNLTEAIGLEL-PDELaRMKAVITLKmvgfDEEKAEEILDKY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 504 GLTgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDFRLIQQV 579
Cdd:TIGR03269 425 PDE----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDV 494
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
398-588 |
3.72e-20 |
|
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: 89.06 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRYH----- 466
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdlTKLSLKELRRKvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 467 QHLQEQL-------DLDLSPLEYMMkcypeikEKEEMRKIIG----RYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNP 535
Cdd:cd03225 82 QNPDDQFfgptveeEVAFGLENLGL-------PEEEIEERVEealeLVGLEGLRDRSP-FTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 536 HMLFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEIWVCEK 588
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLkAEGKtiIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
398-572 |
9.59e-20 |
|
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: 87.97 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRYHQHLQE 471
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 472 QLDLDLSPLEY-MMKCYPEI--------KEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDE 542
Cdd:cd03235 80 DRDFPISVRDVvLMGLYGHKglfrrlskADKAKVDEALERVGLSELAD-RQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|...
gi 27881506 543 PTNHLDIETIDALADAINEF--EG-GMMLVSHD 572
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrrEGmTILVVTHD 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
396-607 |
1.62e-19 |
|
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: 87.77 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRY--- 465
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditKKNLRELRRKvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 -HQHLQEQL-------DLDLSPLEYMMkcypeikEKEEMRKII----GRYGLTGKQQVSPiRNLSDGQKCRVCLAW-LAw 532
Cdd:COG1122 80 vFQNPDDQLfaptveeDVAFGPENLGL-------PREEIRERVeealELVGLEHLADRPP-HELSGGQKQRVAIAGvLA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 533 QNPHMLFLDEPTNHLDIETIDALADAINEF--EG-GMMLVSHDFRLIQQVAQEIWVCEKQTITKW--PGDILAYKEHLKS 607
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGRIVADgtPREVFSDYELLEE 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
86-291 |
1.89e-19 |
|
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: 87.15 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKRevpipehidiyhltreMPPSDKTPLHCVMEV 165
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGL----------------LPPSAGEVLWNGEPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERAMLEKEAERLAHEDAeceklmeLYERL---EELD-------ADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRM 235
Cdd:COG4133 67 RDAREDYRRRLAYLGHADG-------LKPELtvrENLRfwaalygLRADREAIDEALEAVGLAGLADLP-VRQLSAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 236 RVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGV 291
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
396-572 |
4.96e-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: 86.02 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG--MIRKHS--------HVKIGRY 465
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 HQHlqEQLDLDLSPLEYM-----MKCYPEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFL 540
Cdd:cd03263 81 PQF--DALFDELTVREHLrfyarLKGLPKSEIKEEVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190
....*....|....*....|....*....|....
gi 27881506 541 DEPTNHLDIETIDALADAINEFEGG--MMLVSHD 572
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGrsIILTTHS 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
415-608 |
7.95e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.39 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 415 NLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQ-------------------HLQEQL-- 473
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydfvaegieEQAEYLkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 474 ------DLDLSPLEYMMKCYPEIKEKEE----------MRKIIGRYGLTGKQQVSpirNLSDGQKCRVCLAWLAWQNPHM 537
Cdd:PRK11147 101 yhdishLVETDPSEKNLNELAKLQEQLDhhnlwqlenrINEVLAQLGLDPDAALS---SLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 538 LFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDilaYKEHLKSK 608
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN---YDQYLLEK 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
396-588 |
1.11e-18 |
|
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: 83.59 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkIGryhqhlqeqlDL 475
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------ID----------GV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 476 DLSPLeymmkcypeikEKEEMRKIIG-------RYGLTgkqqvspIRN--LSDGQKCRVCLAWLAWQNPHMLFLDEPTNH 546
Cdd:cd03228 65 DLRDL-----------DLESLRKNIAyvpqdpfLFSGT-------IREniLSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881506 547 LDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEK 588
Cdd:cd03228 127 LDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
398-585 |
1.31e-18 |
|
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: 83.06 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhlqeqldLDL 477
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------------------IDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 478 SPLEYmmkcypeiKEKEEMRKIIGRygltgkqqvspIRNLSDGQKCRVCLAwLAW-QNPHMLFLDEPTNHLDIETIDALA 556
Cdd:cd00267 61 KDIAK--------LPLEELRRRIGY-----------VPQLSGGQRQRVALA-RALlLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|..
gi 27881506 557 DAINEF-EGGMM--LVSHDFRLIQQVAQEIWV 585
Cdd:cd00267 121 ELLRELaEEGRTviIVTHDPELAELAADRVIV 152
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
86-303 |
1.32e-18 |
|
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: 84.88 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsDKTPLHCVMEV 165
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI----------DGRDVTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERAMLEKEAERLAHedaeceklMELYE------RLEELDADKAEMRASRILHGLGFTPAMQRK--KLkdfSGGWRMRV 237
Cdd:cd03259 71 RRNIGMVFQDYALFPH--------LTVAEniafglKLRGVPKAEIRARVRELLELVGLEGLLNRYphEL---SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 238 ALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKT----FKRILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
86-303 |
1.60e-18 |
|
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: 83.22 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehidiyhLTREMPPSDktplhcvmEV 165
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII---------------LGLLKPDSG--------EI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 dteramlekeaerlahedaeceklmelyeRLEELDADKAEMRASRIL----HGLGFTPAMQRKKLKDFSGGWRMRVALAR 241
Cdd:cd03230 58 -----------------------------KVLGKDIKKEPEEVKRRIgylpEEPSLYENLTVRENLKLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 242 ALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
392-580 |
2.49e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.76 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGrY 465
Cdd:COG1121 3 MMPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIG-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 -HQHLQEQLDLDLSPLEY-MMKCYPEI--------KEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLA-WLAwQN 534
Cdd:COG1121 80 vPQRAEVDWDFPITVRDVvLMGRYGRRglfrrpsrADREAVDEALERVGLEDLAD-RPIGELSGGQQQRVLLArALA-QD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881506 535 PHMLFLDEPTNHLDIETIDALADAINEF--EG-GMMLVSHDFRLIQQVA 580
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYF 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
394-572 |
4.24e-18 |
|
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: 82.91 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVKIGRYHQHL- 469
Cdd:COG4133 1 MMLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngEPIRDAREDYRRRLa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 470 ----QEQLDLDLSPLEYM---MKCYPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLA--WLAwqNPHMLFL 540
Cdd:COG4133 79 ylghADGLKPELTVRENLrfwAALYGLRADREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALArlLLS--PAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 27881506 541 DEPTNHLDIETIDALADAINEF--EGGM-MLVSHD 572
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHlaRGGAvLLTTHQ 190
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
86-319 |
6.36e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 83.19 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTREMPPSDKTPLHCVMEV 165
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIR----------------MLLGLLRPTSGEVRVLGEDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERA--------MLEKEAerlAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMqRKKLKDFSGGWRMRV 237
Cdd:COG1131 65 ARDPAevrrrigyVPQEPA---LYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 238 ALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKLKyYTGNYDQYV 314
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAaegKTVLLSTHYLEEAERLCDRVAIIDKGRIV-ADGTPDELK 219
|
....*
gi 27881506 315 KTRLE 319
Cdd:COG1131 220 ARLLE 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
86-300 |
7.98e-18 |
|
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: 81.46 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSDKTPlh 160
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgeDLTDLEDELPPLRRRI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 161 cvmevdterAMLEKEAErlahedaeceklmeLYERLEELDadkaemrasRILHGLgftpamqrkklkdfSGGWRMRVALA 240
Cdd:cd03229 79 ---------GMVFQDFA--------------LFPHLTVLE---------NIALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 241 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKT----FKRILVLVSHSQDFLNGVCTNIIHMHN 300
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
413-545 |
1.63e-17 |
|
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: 79.61 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 413 YNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-----------RKHSHVKIGRYHQHLqeQLDLDLSPLE 481
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 482 YM-----MKCYPEIKEKEEMRKIIGRYGLTGKQ---QVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTN 545
Cdd:pfam00005 79 NLrlgllLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
90-302 |
1.90e-17 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 81.36 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltREMPPSDKTPLHCVMEV-- 165
Cdd:cd03225 4 NLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----DGKDLTKLSLKELRRKVgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 ---DTERAMLEKEAErlahEDAE--CEKLMelyerleeLDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALA 240
Cdd:cd03225 80 vfqNPDDQFFGPTVE----EEVAfgLENLG--------LPEEEIEERVEEALELVGLEGLRDRS-PFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 241 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKK 302
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
90-303 |
2.80e-17 |
|
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: 79.79 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPS------DKTPLHcvm 163
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL----------------AGLLKPSsgeillDGKDLA--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 evdterAMLEKE-AERLAHedaeceklmeLYERLEELD-ADKAEmrasRILHGLgftpamqrkklkdfSGGWRMRVALAR 241
Cdd:cd03214 65 ------SLSPKElARKIAY----------VPQALELLGlAHLAD----RPFNEL--------------SGGERQRVLLAR 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 242 ALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR----ILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
398-585 |
4.26e-17 |
|
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: 79.36 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYtKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGmirkhsHVKIgryhqhlqeqLDLDL 477
Cdd:cd03230 3 VRNLSKRY-GKKTAL-DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG------EIKV----------LGKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 478 spleymmkcypeIKEKEEMRKIIGrY---------GLTGKQQVspirNLSDGQKCRVCLAwlawQ----NPHMLFLDEPT 544
Cdd:cd03230 65 ------------KKEPEEVKRRIG-YlpeepslyeNLTVRENL----KLSGGMKQRLALA----QallhDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881506 545 NHLDIETIDALADAINEF--EGG-MMLVSHDFRLIQQVAQEIWV 585
Cdd:cd03230 124 SGLDPESRREFWELLRELkkEGKtILLSSHILEEAERLCDRVAI 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
398-585 |
5.55e-17 |
|
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: 79.02 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigryhqHLQEQLDLDL 477
Cdd:cd03214 2 VENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------------LLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 478 SPLE------YMmkcyPEIKEKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI-- 549
Cdd:cd03214 67 SPKElarkiaYV----PQALELLGLAHLADR----------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIah 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881506 550 --ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:cd03214 133 qiELLELLRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
396-591 |
2.07e-16 |
|
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: 77.26 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhlqeqLD- 474
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----------------LDg 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 475 LDLSPLeymmkcypeikEKEEMRKIIGryglTGKQQV-----SPIRN-LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:cd03246 64 ADISQW-----------DPNELGDHVG----YLPQDDelfsgSIAENiLSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881506 549 IETIDALADAINEFEGGM---MLVSHDFRLIQQvAQEIWVCEKQTI 591
Cdd:cd03246 129 VEGERALNQAIAALKAAGatrIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
396-583 |
7.71e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 77.41 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDgpCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHvkigRYHQH 468
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvaRDPA----EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 L----QE-QLDLDLSP---LEYMMKCY--PEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAwLA-WQNPHM 537
Cdd:COG1131 75 IgyvpQEpALYPDLTVrenLRFFARLYglPRKEARERIDELLELFGLTDAAD-RKVGTLSGGMKQRLGLA-LAlLHDPEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881506 538 LFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEI 583
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELaAEGKtvLLSTHYLEEAERLCDRV 201
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
398-580 |
8.34e-16 |
|
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: 76.53 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVK-----IGRYHQHL 469
Cdd:cd03226 2 IENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKerrksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 470 QEQLDLD--LSPLEYMMKCYPEikEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHL 547
Cdd:cd03226 81 DYQLFTDsvREELLLGLKELDA--GNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881506 548 DIETIDALADAINEF--EGGMMLV-SHDFRLIQQVA 580
Cdd:cd03226 158 DYKNMERVGELIRELaaQGKAVIViTHDYEFLAKVC 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
84-304 |
1.12e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.32 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 84 TDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI----YHLTR----EMPPSD 155
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtINLVRdkdgQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 156 KTPLHCVMevdTERAMLEKEAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRM 235
Cdd:PRK10619 84 KNQLRLLR---TRLTMVFQHFNLWSHMTV-LENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 236 RVALARALFIRPFMLLLDEPTNHLD-------LDACVWLEEELKTfkriLVLVSHSQDFLNGVCTNIIHMHNKKLK 304
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDpelvgevLRIMQQLAEEGKT----MVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
395-583 |
1.61e-15 |
|
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: 76.43 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkHSHVKIGRYHQHLQEQ-- 472
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIL-IDGEDVRKEPREARRQig 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 473 -------LDLDLSPLEYMMKCYP-------EIKEKEEmrKIIGRYGLTGKqQVSPIRNLSDGQKCRVCLAWLAWQNPHML 538
Cdd:COG4555 78 vlpdergLYDRLTVRENIRYFAElyglfdeELKKRIE--ELIELLGLEEF-LDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881506 539 FLDEPTNHLDIETIDALADAINEF--EGGMMLVS-HDFRLIQQVAQEI 583
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRV 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
100-381 |
1.73e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 79.83 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 100 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTR---------EMPPSDKTPL-HCVmevdter 169
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKlgyfaqhqlEFLRADESPLqHLA------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 amlekeaeRLAHEDAEcEKLMELyerleeldadkaemrasriLHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFM 249
Cdd:PRK10636 400 --------RLAPQELE-QKLRDY-------------------LGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 250 LLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFH 329
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDE 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 330 WEQDQIAH-------MKNYIARFGHGSAKLARQAQSKEKTLQKMMA--SGLTERvVSDKTL 381
Cdd:PRK10636 532 APKENNANsaqarkdQKRREAELRTQTQPLRKEIARLEKEMEKLNAqlAQAEEK-LGDSEL 591
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
90-303 |
4.83e-15 |
|
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: 74.18 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVPIPEHIDIYHLTREMPpsdktplhc 161
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlglikpdsGEITFDGKSYQKNIEALRRIG--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 162 vmevdterAMLEKEA---ERLAHEDaeceklMELYERLeeldADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVA 238
Cdd:cd03268 76 --------ALIEAPGfypNLTAREN------LRLLARL----LGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLV-SHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
395-585 |
7.14e-15 |
|
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: 74.69 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRY-- 465
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaSLSRRELARRia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 --HQHLqeQLDLDLSPLEY-MMKCYPEIK----EKEEMRKIIGRY----GLTGKQQvSPIRNLSDGQKCRVCLAW-LAwQ 533
Cdd:COG1120 79 yvPQEP--PAPFGLTVRELvALGRYPHLGlfgrPSAEDREAVEEAlertGLEHLAD-RPVDELSGGERQRVLIARaLA-Q 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 534 NPHMLFLDEPTNHLDI----ETIDALADaINEFEG-GMMLVSHDFRLIQQVAQEIWV 585
Cdd:COG1120 155 EPPLLLLDEPTSHLDLahqlEVLELLRR-LARERGrTVVMVLHDLNLAARYADRLVL 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
86-305 |
1.79e-14 |
|
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: 73.14 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQ-ELLSDTKLELNSGRRYGLIGLNGIGKSMLLsaigkrevpipehidiYHLTREMPPSDKTPLhcVME 164
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLL----------------RLLNGLLKPTSGEVL--VDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 165 VDTERAMLEKEAER--LAHEDAEceklMELYER--LEE---------LDADKAEMRASRILHGLGFTPAMQRK--KLkdf 229
Cdd:COG1122 63 KDITKKNLRELRRKvgLVFQNPD----DQLFAPtvEEDvafgpenlgLPREEIRERVEEALELVGLEHLADRPphEL--- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKKLKY 305
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
415-592 |
2.49e-14 |
|
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: 72.75 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 415 NLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHL---------QEQLDLDLSPLE--YM 483
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLrrigvvfgqKTQLWWDLPVIDsfYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 484 MKCYPEIKEKEEMRKIIGRYGLTGKQQV--SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI---ETIDALADA 558
Cdd:cd03267 119 LAAIYDLPPARFKKRLDELSELLDLEELldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKE 198
|
170 180 190
....*....|....*....|....*....|....*
gi 27881506 559 IN-EFEGGMMLVSHDFRLIQQVAQEIWVCEKQTIT 592
Cdd:cd03267 199 YNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
392-585 |
4.13e-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: 75.40 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-----------KHSHV 460
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPAL-RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadaDSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 KIGRYHQH-------LQEQLDLDLspleymmkcyPEIKEkEEMRKIIGRYGLTGKQQVSPI----------RNLSDGQKC 523
Cdd:TIGR02857 397 QIAWVPQHpflfagtIAENIRLAR----------PDASD-AEIREALERAGLDEFVAALPQgldtpigeggAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 524 RVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDfRLIQQVAQEIWV 585
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHR-LALAALADRIVV 528
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
88-300 |
4.91e-14 |
|
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: 72.14 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTF----HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKREVPiPEHIDIYHLTREMPPSDKTPLHCVM 163
Cdd:COG1124 4 VRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRAL-AGLER-PWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 evdterAMLEKEAERLAH-----EDAecekLMELYERLEELDADKaemRASRILHGLGFTPAMQRKKLKDFSGGWRMRVA 238
Cdd:COG1124 82 ------QMVFQDPYASLHprhtvDRI----LAEPLRIHGLPDREE---RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDL--DACVW--LEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHN 300
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
395-585 |
4.97e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.85 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-----------KHSHVKIG 463
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 464 RYHQHLQEQL-------DLDLSPLEyMMKCYPEIKEK-EEMRKIIGRYGLTGKqqvsPIRNLSDGQKCRVCLAWLAWQNP 535
Cdd:PRK13647 83 LVFQDPDDQVfsstvwdDVAFGPVN-MGLDKDEVERRvEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881506 536 HMLFLDEPTNHLD---IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:PRK13647 158 DVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
393-592 |
7.30e-14 |
|
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: 74.41 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 393 PPVIMVQNVSFKYTKDGPcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR----KHSHVKIGRYHQH 468
Cdd:COG4988 334 PPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 --------------LQEQLDL---DLSPleymmkcypeikekEEMRKIIGRYGLTG-----KQQV-SPI----RNLSDGQ 521
Cdd:COG4988 413 iawvpqnpylfagtIRENLRLgrpDASD--------------EELEAALEAAGLDEfvaalPDGLdTPLgeggRGLSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 522 KCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEKQTIT 592
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
87-304 |
7.78e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 70.75 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 87 HIINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrevpipehidiyhLTREM---------PPSDK 156
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-------------LIKESsgsillngkPIKAK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 157 TPLHC---VMEvDTERAMLEKEAERlahedaeceklmELYERLEELDADKAemRASRILHGLGFTPAMQRKKLkDFSGGW 233
Cdd:cd03226 68 ERRKSigyVMQ-DVDYQLFTDSVRE------------ELLLGLKELDAGNE--QAETVLKDLDLYALKERHPL-SLSGGQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 234 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLK 304
Cdd:cd03226 132 KQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGElirELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
90-261 |
1.40e-13 |
|
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: 70.84 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPS------DKTPLH--C 161
Cdd:COG1120 6 NLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRA----------------LAGLLKPSsgevllDGRDLAslS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 162 VMEVDTERAMLEKEAE--------------RLAHedaeceklMELYERLEELDADKAE--MRASRILHglgftpaMQRKK 225
Cdd:COG1120 70 RRELARRIAYVPQEPPapfgltvrelvalgRYPH--------LGLFGRPSAEDREAVEeaLERTGLEH-------LADRP 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881506 226 LKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL 261
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
90-298 |
1.69e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.55 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDKTPLHCVMEVDTER 169
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 AMLEKEAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFM 249
Cdd:PRK11264 88 GFVFQNFNLFPHRTV-LENIIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 250 LLLDEPTNHLD-------LDACVWLEEElktfKRILVLVSHSQDFLNGVCTNIIHM 298
Cdd:PRK11264 166 ILFDEPTSALDpelvgevLNTIRQLAQE----KRTMVIVTHEMSFARDVADRAIFM 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
86-299 |
2.05e-13 |
|
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: 69.48 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDktplhcVMEV 165
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN------INEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERAMLEKEAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFtPAMQRKKLKDFSGGWRMRVALARALFI 245
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTV-LENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 246 RPFMLLLDEPTNHLD-------LDACVWLEEELKTfkriLVLVSHSQDFLNGVCTNIIHMH 299
Cdd:cd03262 153 NPKVMLFDEPTSALDpelvgevLDVMKDLAEEGMT----MVVVTHEMGFAREVADRVIFMD 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
428-591 |
2.31e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 428 LVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSpLEYMMKCYPEIKeKEEMRKIIGRYGlTG 507
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLT-VNRFLRLRPGTK-KEDILPALKRVQ-AG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 508 KQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAIN----EFEGGMMLVSHDFRLIQQVAQEI 583
Cdd:PRK09544 112 HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDqlrrELDCAVLMVSHDLHLVMAKTDEV 191
|
....*...
gi 27881506 584 wVCEKQTI 591
Cdd:PRK09544 192 -LCLNHHI 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
111-305 |
2.48e-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: 69.70 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 111 GRRYGLIGLNGIGKS----MLLSAI----GKREVpipEHIDIYHLTREMPP-----SDKTPLHCVMevdTERAMLEkeae 177
Cdd:cd03266 31 GEVTGLLGPNGAGKTttlrMLAGLLepdaGFATV---DGFDVVKEPAEARRrlgfvSDSTGLYDRL---TARENLE---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 178 rlahedaeceklmeLYERLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRPFMLLLDEPTN 257
Cdd:cd03266 101 --------------YFAGLYGLKGDELTARLEELADRLGMEELLDRR-VGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881506 258 HLDLDACVWLEEELKTFKRI---LVLVSHSQDFLNGVCTNIIHMHNKKLKY 305
Cdd:cd03266 166 GLDVMATRALREFIRQLRALgkcILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
97-284 |
2.70e-13 |
|
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: 72.78 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 97 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPS------DKTPLHCVMEVDTER- 169
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT----------------LAGLLDPLqgevtlDGVPVSSLDQDEVRRr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 -AMLEKEAE----------RLAHEDAECEKLMELYER--LEELdadkaemrASRILHGLGfTPAMQRKKLkdFSGGWRMR 236
Cdd:TIGR02868 411 vSVCAQDAHlfdttvrenlRLARPDATDEELWAALERvgLADW--------LRALPDGLD-TVLGEGGAR--LSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881506 237 VALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL--KTFKRILVLVSHS 284
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLlaALSGRTVVLITHH 529
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
90-306 |
2.96e-13 |
|
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: 69.10 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHI----DIYHLTREM 151
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkptsgsirvfGKPLEKERKRIgyvpQRRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 152 PPSdktplhcVMEVdterAMLEkeaeRLAHedaeceklMELYERLEELDADKAEmrasrilhglgftPAMQRKKLKDF-- 229
Cdd:cd03235 84 PIS-------VRDV----VLMG----LYGH--------KGLFRRLSKADKAKVD-------------EALERVGLSELad 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 230 ------SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAC---VWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMhN 300
Cdd:cd03235 128 rqigelSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQediYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-N 206
|
....*.
gi 27881506 301 KKLKYY 306
Cdd:cd03235 207 RTVVAS 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
398-585 |
3.37e-13 |
|
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: 72.56 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkIGRY------HQHLQE 471
Cdd:COG2274 476 LENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL------IDGIdlrqidPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 472 QL-----DLDL---SPLEYMMKCYPEIkEKEEMRKIIGRYGLTG---------KQQVSPI-RNLSDGQKCRVCLA--WLa 531
Cdd:COG2274 550 QIgvvlqDVFLfsgTIRENITLGDPDA-TDEEIIEAARLAGLHDfiealpmgyDTVVGEGgSNLSGGQRQRLAIAraLL- 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 532 wQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWV 585
Cdd:COG2274 628 -RNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRL-ADRIIV 681
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
393-571 |
7.72e-13 |
|
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: 68.57 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 393 PPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGM----------------IRK 456
Cdd:COG1119 1 DPLLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 457 HshvkIGRYHQHLQEQLDLDLSPLE------Y-MMKCYPEIKEKEEMR--KIIGRYGLTGKQQvSPIRNLSDGQKCRVCL 527
Cdd:COG1119 79 R----IGLVSPALQLRFPRDETVLDvvlsgfFdSIGLYREPTDEQRERarELLELLGLAHLAD-RPFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 528 --AWLAwqNPHMLFLDEPTNHLD-------IETIDALADainefEGG--MMLVSH 571
Cdd:COG1119 154 arALVK--DPELLILDEPTAGLDlgarellLALLDKLAA-----EGAptLVLVTH 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
86-305 |
1.18e-12 |
|
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: 67.22 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRrYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPSDKTplhcvMEV 165
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRIL----------------ATLTPPSSGT-----IRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERAMLEKEAERlAH-----EDAECEKLMELYE------RLEELDADKAEMRASRILHGLGFTPAmQRKKLKDFSGGWR 234
Cdd:cd03264 59 DGQDVLKQPQKLR-RRigylpQEFGVYPNFTVREfldyiaWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 235 MRVALARALFIRPFMLLLDEPTNHLDldacvwlEEELKTFKRIL--------VLVS-HSQDFLNGVCTNIIHMHNKKLKY 305
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLD-------PEERIRFRNLLselgedriVILStHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
88-303 |
1.23e-12 |
|
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: 67.53 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVpipEHIDIYHLTREM---- 151
Cdd:cd03257 4 VKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsGSIIF---DGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 152 ----------PPSDKTPLH----CVMEVDTERAMLEKEAERLahedaecEKLMELYERLEeLDADKAEMRASRilhglgf 217
Cdd:cd03257 81 rkeiqmvfqdPMSSLNPRMtigeQIAEPLRIHGKLSKKEARK-------EAVLLLLVGVG-LPEEVLNRYPHE------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 218 tpamqrkklkdFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLD--ACVwleeeLKTFKRI-------LVLVSHSQDFL 288
Cdd:cd03257 146 -----------LSGGQRQRVAIARALALNPKLLIADEPTSALDVSvqAQI-----LDLLKKLqeelgltLLFITHDLGVV 209
|
250
....*....|....*
gi 27881506 289 NGVCTNIIHMHNKKL 303
Cdd:cd03257 210 AKIADRVAVMYAGKI 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
428-587 |
1.24e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 428 LVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGrYHQhlQE-QLDLDLSPLEYMMKCYPEIKEK------------- 493
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVG-YLP--QEpQLDPEKTVRENVEEGVAEVKAAldrfneiyaayae 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 494 --EEMRKIIGRYG-LTGK----------QQV-------------SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHL 547
Cdd:PRK11819 115 pdADFDALAAEQGeLQEIidaadawdldSQLeiamdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881506 548 DIETIDALADAINEFEGGMMLVSHDFRLIQQVAQeiWVCE 587
Cdd:PRK11819 195 DAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
95-300 |
2.27e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 95 FHG-QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMPPSDKTplhcVMEVDTERAM 171
Cdd:PRK11124 11 FYGaHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSDKA----IRELRRNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 172 LEKEAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARALFIRPFMLL 251
Cdd:PRK11124 87 VFQQYNLWPHLTV-QQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881506 252 LDEPTNHLDLD---ACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHN 300
Cdd:PRK11124 165 FDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
216-327 |
2.42e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 216 GFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNI 295
Cdd:PRK11819 433 NFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI 512
|
90 100 110
....*....|....*....|....*....|...
gi 27881506 296 IHMH-NKKLKYYTGNYDQYvktrlelEENQMKR 327
Cdd:PRK11819 513 LAFEgDSQVEWFEGNFQEY-------EEDKKRR 538
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
419-572 |
2.64e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYM-MKCYPEI--- 490
Cdd:NF040873 10 GVDLTIPagslTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVaMGRWARRglw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 491 -KEKEEMRKIIG----RYGLTGkQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEG- 564
Cdd:NF040873 90 rRLTRDDRAAVDdaleRVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
|
170
....*....|
gi 27881506 565 --GMMLVSHD 572
Cdd:NF040873 169 gaTVVVVTHD 178
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
87-298 |
3.30e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 66.30 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 87 HIINLSLTF-----HGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREmppsdktpl 159
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGW--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 160 hcvmeVD----TERAMLE-KEAE------------RLAHEDAECEKLMELyerleELDADKAEMRASRILHGLGFtpamq 222
Cdd:COG4778 77 -----VDlaqaSPREILAlRRRTigyvsqflrvipRVSALDVVAEPLLER-----GVDREEARARARELLARLNL----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 223 RKKLKD-----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDL---DACVWLEEELKTFKRILVLVSHSQDFLNGVCTN 294
Cdd:COG4778 142 PERLWDlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
....
gi 27881506 295 IIHM 298
Cdd:COG4778 222 VVDV 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
90-310 |
3.35e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLS-AIGKREvpipehidiyhltremPPSDKtpLHC--VMEV- 165
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ----------------ADSGR--IHCgtKLEVa 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 --DTERAMLEKEA---ERLAhedaeceklmelyerleelDADKAEMRASRILHGLG------FTPAMQRKKLKDFSGGWR 234
Cdd:PRK11147 386 yfDQHRAELDPEKtvmDNLA-------------------EGKQEVMVNGRPRHVLGylqdflFHPKRAMTPVKALSGGER 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 235 MRVALARaLFIRPFMLL-LDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFL-NGVCTNIIHMHNKKLKYYTGNY 310
Cdd:PRK11147 447 NRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGGY 523
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
229-283 |
3.40e-12 |
|
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: 64.93 E-value: 3.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSH 283
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAH 154
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
90-303 |
3.49e-12 |
|
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: 66.07 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIyhltREMPPSD-KTPLHC 161
Cdd:cd03245 7 NVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtDI----RQLDPADlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 162 VMEVDTERAMLEKEAERLAHEDAECEKLMELYER--LEELDADkaemrasrilHGLGFtpAMQ-RKKLKDFSGGWRMRVA 238
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELagVTDFVNK----------HPNGL--DLQiGERGRGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK--RILVLVSHSQDFLNgVCTNIIHMHNKKL 303
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
395-588 |
3.73e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.23 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------KHSHV----- 460
Cdd:COG2884 1 MIRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 KIGRYHQ--HLqeqLDlDLS-------PLEYMMKCYPEIKEKeeMRKIIGRYGLTGKQQVSPIrNLSDGQKCRVCLAwla 531
Cdd:COG2884 80 RIGVVFQdfRL---LP-DRTvyenvalPLRVTGKSRKEIRRR--VREVLDLVGLSDKAKALPH-ELSGGEQQRVAIAral 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 532 wqNPHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLV-SHDFRLIQQVAQEIWVCEK 588
Cdd:COG2884 153 vnRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLELED 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
396-579 |
4.81e-12 |
|
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: 65.69 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKHshv 460
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpadlRRN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 kIGRYHQH-------LQEQLDLDlspleymmkcYPEIKEKEEMR--KIIGRYGLTGKQ------QVSPI-RNLSDGQKCR 524
Cdd:cd03245 80 -IGYVPQDvtlfygtLRDNITLG----------APLADDERILRaaELAGVTDFVNKHpngldlQIGERgRGLSGGQRQA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 525 VCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQV 579
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLV 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
396-591 |
4.98e-12 |
|
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: 66.10 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH----VKIGRYHQHL-- 469
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdYTLASLRRQIgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 470 --QEQLDLDLSPLEYMMKCYPEIKEKEEMR-------------------KIIGRYGLtgkqqvspirNLSDGQKCRVCLA 528
Cdd:cd03251 81 vsQDVFLFNDTVAENIAYGRPGATREEVEEaaraanahefimelpegydTVIGERGV----------KLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 529 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEKQTI 591
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
366-588 |
5.09e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 366 MMASGLTERVVS--DKTLSFyfPPCGKIPPP----VIMVQNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKST 438
Cdd:TIGR00958 445 MQAVGASEKVFEylDRKPNI--PLTGTLAPLnlegLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 439 LLKLLTGELLPTDGM-------IRKHSHVkigRYHQHL----QEQL------------DLDLSPLEYMMK------CYPE 489
Cdd:TIGR00958 523 VAALLQNLYQPTGGQvlldgvpLVQYDHH---YLHRQValvgQEPVlfsgsvreniayGLTDTPDEEIMAaakaanAHDF 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 490 IKEKEEmrKIIGRYGLTGKQqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLV 569
Cdd:TIGR00958 600 IMEFPN--GYDTEVGEKGSQ-------LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLI 670
|
250
....*....|....*....
gi 27881506 570 SHDFRLIQQvAQEIWVCEK 588
Cdd:TIGR00958 671 AHRLSTVER-ADQILVLKK 688
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-585 |
5.74e-12 |
|
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: 68.39 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTgellptdGMIRKHSHVKiGRYHQHLQEQL 473
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM-------GLLPHGGRIS-GEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 474 DLDLS---------PLEYM-----MKCYPEIKE--------KEEMRKII----GRYGLTGKQQVSPIRnLSDGQKCRVCL 527
Cdd:COG1123 75 ELSEAlrgrrigmvFQDPMtqlnpVTVGDQIAEalenlglsRAEARARVlellEAVGLERRLDRYPHQ-LSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 528 AWLAWQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
88-260 |
6.64e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHltreMPPSDKtPLHCV 162
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvDLSH----VPPYQR-PINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 ---------MEVDTERAMLEKEaERLAHEdaeceklmELYERLEELDAdkaemrasrILHGLGFTpamqRKKLKDFSGGW 233
Cdd:PRK11607 97 fqsyalfphMTVEQNIAFGLKQ-DKLPKA--------EIASRVNEMLG---------LVHMQEFA----KRKPHQLSGGQ 154
|
170 180
....*....|....*....|....*..
gi 27881506 234 RMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK11607 155 RQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
86-286 |
8.01e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.09 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GK-----REVPIpeHIDI-------- 144
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdsGRivlngRDLFT--NLPPrerrvgfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 145 ---Y----HLT---------REMPPSdktplhcvmevdteramlEKEAERLAHEdaecekLMELYErLEELdadkaemrA 208
Cdd:COG1118 81 fqhYalfpHMTvaeniafglRVRPPS------------------KAEIRARVEE------LLELVQ-LEGL--------A 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 209 SRILHGLgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHldLDACV------WLEEELKTFKRILVLVS 282
Cdd:COG1118 128 DRYPSQL--------------SGGQRQRVALARALAVEPEVLLLDEPFGA--LDAKVrkelrrWLRRLHDELGGTTVFVT 191
|
....
gi 27881506 283 HSQD 286
Cdd:COG1118 192 HDQE 195
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
385-592 |
8.19e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 67.87 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 385 FPPCGKIPP--PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------- 455
Cdd:COG4987 321 EPAEPAPAPggPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlr 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 456 ---------------KHSHV---------KIGRyhqhlqeqldldlspleymmkcyPEIKEkEEMRKIIGRYGL------ 505
Cdd:COG4987 401 dldeddlrrriavvpQRPHLfdttlrenlRLAR-----------------------PDATD-EELWAALERVGLgdwlaa 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 506 -----------TGkqqvspiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHD 572
Cdd:COG4987 457 lpdgldtwlgeGG-------RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHR 529
|
250 260
....*....|....*....|
gi 27881506 573 FRLIQQvAQEIWVCEKQTIT 592
Cdd:COG4987 530 LAGLER-MDRILVLEDGRIV 548
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
67-284 |
8.54e-12 |
|
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: 67.70 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 67 KAAARAVTGVLAS----HPNSTDV--------HIINLSLTFHGQ-ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-G 132
Cdd:TIGR02857 291 VAAAEALFAVLDAaprpLAGKAPVtaapasslEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 133 KRE----------VPIPeHIDIYHLTREMPPSDKTPlhcvmevdterAMLEKE-AERLahedaeceklmelyeRLEELDA 201
Cdd:TIGR02857 371 FVDptegsiavngVPLA-DADADSWRDQIAWVPQHP-----------FLFAGTiAENI---------------RLARPDA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 202 DKAEMRASRILHGL-GFT---PAMQRKKLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKT 273
Cdd:TIGR02857 424 SDAEIREALERAGLdEFVaalPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
250
....*....|...
gi 27881506 274 FK--RILVLVSHS 284
Cdd:TIGR02857 504 LAqgRTVLLVTHR 516
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
390-548 |
1.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.78 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 390 KIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-----------KHS 458
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenlKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 459 HVKIGRYHQHLQEQL-------DLDLSpLEYmmKCYPeikeKEEMRKIIGRY----GLTGKQQVSPiRNLSDGQKCRVCL 527
Cdd:PRK13632 82 RKKIGIIFQNPDNQFigatvedDIAFG-LEN--KKVP----PKKMKDIIDDLakkvGMEDYLDKEP-QNLSGGQKQRVAI 153
|
170 180
....*....|....*....|.
gi 27881506 528 AWLAWQNPHMLFLDEPTNHLD 548
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLD 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
394-561 |
1.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKHs 458
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklRKH- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 459 hvkIGRYHQHLQEQ-----LDLDLS-PLEYMMKCYPEIKEKeeMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAW 532
Cdd:PRK13648 85 ---IGIVFQNPDNQfvgsiVKYDVAfGLENHAVPYDEMHRR--VSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLA 158
|
170 180
....*....|....*....|....*....
gi 27881506 533 QNPHMLFLDEPTNHLDIETIDALADAINE 561
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRK 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
407-583 |
1.96e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.67 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 407 KDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVKIGRYHQHL-----QEQLDLDLS 478
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLlylghAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 479 PLEYmMKCYPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADA 558
Cdd:cd03231 90 VLEN-LRFWHADHSDEQVEEALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180
....*....|....*....|....*....
gi 27881506 559 INEF--EGGMMLVS--HDFRLIQQVAQEI 583
Cdd:cd03231 168 MAGHcaRGGMVVLTthQDLGLSEAGAREL 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
98-303 |
2.27e-11 |
|
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: 64.44 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 98 QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSDKTPLHCVME-----VDT 167
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqDLYQLDRKQRRAFRRDVQLVFQdspsaVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 168 ERAMLEKEAERLAHedaeceklmelyerLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRP 247
Cdd:TIGR02769 104 RMTVRQIIGEPLRH--------------LTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 248 FMLLLDEPTNHLDL----DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:TIGR02769 170 KLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
86-303 |
2.42e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.26 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMPPSDKTplhcVM 163
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQKPSEKA----IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 EVDTERAMLEKEAERLAHEDAEcEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARAL 243
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVM-ENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 244 FIRPFMLLLDEPTNHLD---LDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:COG4161 157 MMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
395-592 |
2.47e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG--MIRKHSHVK---------IG 463
Cdd:PRK13652 3 LIETRDLCYSYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvLIRGEPITKenirevrkfVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 464 RYHQHLQEQL-------DLDLSPLEYMMKcypEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPH 536
Cdd:PRK13652 82 LVFQNPDDQIfsptveqDIAFGPINLGLD---EETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 537 MLFLDEPTNHLDIETIDALADAINEF--EGGMMLV--SHDFRLIQQVAQEIWVCEKQTIT 592
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIfsTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
67-303 |
2.80e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 66.32 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 67 KAAARAVTGVLASH-----------PNSTDVHII--NLSLTFH-GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIG 132
Cdd:COG4988 305 IAAAEKIFALLDAPepaapagtaplPAAGPPSIEleDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 133 KREVPIPEHIDIyhltremppsDKTPLHcvmEVDTERAMlekeaERLA------HedaecekLME--LYE--RLEELDAD 202
Cdd:COG4988 385 GFLPPYSGSILI----------NGVDLS---DLDPASWR-----RQIAwvpqnpY-------LFAgtIREnlRLGRPDAS 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 203 KAEMRAsrilhglgftpAMQRKKLKDF-------------------SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDA 263
Cdd:COG4988 440 DEELEA-----------ALEAAGLDEFvaalpdgldtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 27881506 264 cvwlEEELKT-----FK-RILVLVSHSQDFLNgVCTNIIHMHNKKL 303
Cdd:COG4988 509 ----EAEILQalrrlAKgRTVILITHRLALLA-QADRILVLDDGRI 549
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
60-283 |
3.07e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 60 LEDFE--MKKAAARAVTGVLASHPNSTDVHIINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI----- 131
Cdd:COG4178 335 LAGFEeaLEAADALPEAASRIETSEDGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwp 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 132 -GKREVPIPEHIDIYHLTRE--MPPsdktplhcvmevDTERAMLEKEAERLAHEDAECEKLME------LYERLEEldad 202
Cdd:COG4178 415 yGSGRIARPAGARVLFLPQRpyLPL------------GTLREALLYPATAEAFSDAELREALEavglghLAERLDE---- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 203 kaEMRASRILhglgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEEL-KTFKR----- 276
Cdd:COG4178 479 --EADWDQVL-----------------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN----EAALyQLLREelpgt 535
|
....*..
gi 27881506 277 ILVLVSH 283
Cdd:COG4178 536 TVISVGH 542
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
419-619 |
3.50e-11 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 64.72 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDG--------MIRKHSHVK--IGRYHQhlQEQLDLDLSPLEYMM 484
Cdd:TIGR01188 11 GVNFKVRegevFGFLGPNGAGKTTTIRMLTTLLRPTSGtarvagydVVREPRKVRrsIGIVPQ--YASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 485 KC-----YPEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 559
Cdd:TIGR01188 89 MMgrlygLPKDEAEERAEELLELFELGEAAD-RPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 560 NEF-EGGM--MLVSHDFRLIQQVAQEIWVCEKqtitkwpGDILAYK--EHLKSKLVDEEPQLTKR 619
Cdd:TIGR01188 168 RALkEEGVtiLLTTHYMEEADKLCDRIAIIDH-------GRIIAEGtpEELKRRLGKDTLESRPR 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
419-591 |
3.70e-11 |
|
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: 62.93 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRYHQHLQ---EQLDL--DLSPLEYM 483
Cdd:cd03262 18 GIDLTVKkgevVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglklTDDKKNINELRQKVGmvfQQFNLfpHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 484 M------KCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALAD 557
Cdd:cd03262 98 TlapikvKGMSKAEAEERALELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881506 558 AINEF--EG-GMMLVSHDFRLIQQVAQEIWVCEKQTI 591
Cdd:cd03262 177 VMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
396-576 |
3.96e-11 |
|
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: 62.81 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKH----SHVK---IGRYHQH 468
Cdd:cd03292 1 IEFINVTKTYPNGTAAL-DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 L----QE-QLDLDLS-------PLEYMMKCYPEIKEKEEMrkIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPH 536
Cdd:cd03292 80 IgvvfQDfRLLPDRNvyenvafALEVTGVPPREIRKRVPA--ALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881506 537 MLFLDEPTNHLDIETIDALADAINEFE--GGMMLVS-HDFRLI 576
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELV 199
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
67-283 |
4.12e-11 |
|
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: 65.94 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 67 KAAARAVTGVL------------ASHPNSTDVHIINLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAig 132
Cdd:COG4987 303 RAAARRLNELLdappavtepaepAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 133 krevpipehidiyhLTREMPPS------DKTPLHCVMEVDTER--AMLEKEAE----------RLAHEDAECEKLME--- 191
Cdd:COG4987 381 --------------LLRFLDPQsgsitlGGVDLRDLDEDDLRRriAVVPQRPHlfdttlrenlRLARPDATDEELWAale 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 192 ------LYERLEE-LDAdkaemrasrILHGLGFTpamqrkklkdFSGGWRMRVALARALFIRPFMLLLDEPTNHLD-LDA 263
Cdd:COG4987 447 rvglgdWLAALPDgLDT---------WLGEGGRR----------LSGGERRRLALARALLRDAPILLLDEPTEGLDaATE 507
|
250 260
....*....|....*....|.
gi 27881506 264 CVWLEEELKTFK-RILVLVSH 283
Cdd:COG4987 508 QALLADLLEALAgRTVLLITH 528
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
419-580 |
4.34e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR------------KHSHVKIGRYHQHL----QeqlDLDLS 478
Cdd:PRK11264 21 GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslSQQKGLIRQLRQHVgfvfQ---NFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 479 P----LEYMMKCyPEIKEKEEM-------RKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHL 547
Cdd:PRK11264 98 PhrtvLENIIEG-PVIVKGEPKeeataraRELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881506 548 DIE-------TIDALAdainEFEGGMMLVSHDFRLIQQVA 580
Cdd:PRK11264 176 DPElvgevlnTIRQLA----QEKRTMVIVTHEMSFARDVA 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
86-283 |
4.57e-11 |
|
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: 63.57 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI---------------GKR--EVPIPE---HIDIY 145
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlfGERrgGEDVWElrkRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 146 --HLTREMPPSDKtplhcVMEV------DTeramlekeaerlahedaeceklMELYERLEELDADKAEmrasRILHGLGF 217
Cdd:COG1119 84 spALQLRFPRDET-----VLDVvlsgffDS----------------------IGLYREPTDEQRERAR----ELLELLGL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 218 TPAMQRKkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLeeeLKTFKRI-------LVLVSH 283
Cdd:COG1119 133 AHLADRP-FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELL---LALLDKLaaegaptLVLVTH 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
414-585 |
4.74e-11 |
|
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: 63.22 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 414 NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------------KHSHVKIGRYHQHLqeQLDLDLSPLE 481
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglpphEIARLGIGRTFQIP--RLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 482 YMM---------------KCYPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPT-- 544
Cdd:cd03219 95 NVMvaaqartgsglllarARREEREARERAEELLERVGLADLADR-PAGELSYGQQRRLEIARALATDPKLLLLDEPAag 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881506 545 -NHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:cd03219 174 lNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
420-588 |
8.77e-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: 61.93 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 420 IDLDT---RVALVGPNGAGKSTLLKLLTGELLPTDGMI----------RKHSHV-----KIGRYHQHLQEQLDLDL-SPL 480
Cdd:cd03297 17 IDFDLneeVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLppqqrKIGLVFQQYALFPHLNVrENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 481 EYMMKCYPEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAIN 560
Cdd:cd03297 97 AFGLKRKRNREDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|..
gi 27881506 561 E----FEGGMMLVSHDFRLIQQVAQEIWVCEK 588
Cdd:cd03297 176 QikknLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
86-303 |
1.54e-10 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 61.75 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTrempPSDKTPLH 160
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgeDISGLS----EAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 161 CVMevdterAMLEKEAerlAHEDAeceklMELYE----RLEELDADKAEMRASRILHGLGFT--PAMQRKKLKDFSGGWR 234
Cdd:cd03261 77 RRM------GMLFQSG---ALFDS-----LTVFEnvafPLREHTRLSEEEIREIVLEKLEAVglRGAEDLYPAELSGGMK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 235 MRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
405-583 |
1.55e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.84 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 405 YTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVKIGRYHQHL-----QEQLDLD 476
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngTPLAEQRDEPHENIlylghLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 477 LSPLE----YMMKCYPEIKEKEEMrkiIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETI 552
Cdd:TIGR01189 88 LSALEnlhfWAAIHGGAQRTIEDA---LAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|...
gi 27881506 553 DALADAINEF--EGGMMLVSHDFRLIQQVAQEI 583
Cdd:TIGR01189 164 ALLAGLLRAHlaRGGIVLLTTHQDLGLVEAREL 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
195-285 |
1.59e-10 |
|
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: 61.48 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 195 RLEELDADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF 274
Cdd:cd03300 98 RLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRL 176
|
90
....*....|....*
gi 27881506 275 KRIL----VLVSHSQ 285
Cdd:cd03300 177 QKELgitfVFVTHDQ 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
396-585 |
1.67e-10 |
|
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: 61.43 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDgpCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLtgellptDGMIRKHSHVKI-GRYHQHLQEQLD 474
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLL-------NRLNDLIPGAPDeGEVLLDGKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 475 LDLSPLEYMMK-------------------CYP----EIKEKEEMRKII----GRYGLTG--KQQVSPiRNLSDGQKCRV 525
Cdd:cd03260 72 LDVDVLELRRRvgmvfqkpnpfpgsiydnvAYGlrlhGIKLKEELDERVeealRKAALWDevKDRLHA-LGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 526 CLAwLAWQN-PHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:cd03260 151 CLA-RALANePEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAF 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
395-607 |
2.71e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------RKHSHV----K 461
Cdd:PRK13639 1 ILETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikyDKKSLLevrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 462 IGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQN 534
Cdd:PRK13639 80 VGIVFQNPDDQLfaptveeDVAFGPLNLGL---SKEEVEKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 535 PHMLFLDEPTNHLD---IETIDALADAINEfEGGMMLVS-HDFRLIQQVAQEIWVCEKQTITK--WPGDILAYKEHLKS 607
Cdd:PRK13639 156 PEIIVLDEPTSGLDpmgASQIMKLLYDLNK-EGITIIIStHDVDLVPVYADKVYVMSDGKIIKegTPKEVFSDIETIRK 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
90-303 |
3.00e-10 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 60.58 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-----IPEHIDIYHLTremppsdktplh 160
Cdd:cd03255 5 NLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtsgevRVDGTDISKLS------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 161 cvmevDTERAmlekeAERLAH-----------------EDAEceklmeLYERLEELDADKAEMRASRILHGLGFTPAMQR 223
Cdd:cd03255 73 -----EKELA-----AFRRRHigfvfqsfnllpdltalENVE------LPLLLAGVPKKERRERAEELLERVGLGDRLNH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 224 K--KLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAC--VW--LEEELKTFKRILVLVSHSQDfLNGVCTNIIH 297
Cdd:cd03255 137 YpsEL---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkeVMelLRELNKEAGTTIVVVTHDPE-LAEYADRIIE 212
|
....*.
gi 27881506 298 MHNKKL 303
Cdd:cd03255 213 LRDGKI 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
396-551 |
3.23e-10 |
|
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: 60.58 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH----VKIGRYHQH--- 468
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlalADPAWLRRQvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 -LQEQLDLDLSPLEYMMKCYP--EIKEKEEMRKIIGRYG-----------LTGKQQVSpirnLSDGQKCRVCLAWLAWQN 534
Cdd:cd03252 81 vLQENVLFNRSIRDNIALADPgmSMERVIEAAKLAGAHDfiselpegydtIVGEQGAG----LSGGQRQRIAIARALIHN 156
|
170
....*....|....*..
gi 27881506 535 PHMLFLDEPTNHLDIET 551
Cdd:cd03252 157 PRILIFDEATSALDYES 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
425-591 |
3.23e-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: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 425 RVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGRY-------------HQHLQEQLDLDLSPleyMMKCY 487
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingVDVTAAPPADRpvsmlfqennlfaHLTVEQNVGLGLSP---GLKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 488 PEikEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGG 565
Cdd:cd03298 103 AE--DRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETK 179
|
170 180
....*....|....*....|....*...
gi 27881506 566 M--MLVSHDFRLIQQVAQEIWVCEKQTI 591
Cdd:cd03298 180 MtvLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
85-325 |
3.72e-10 |
|
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: 62.93 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 85 DVHIINLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP---------IP-EHIDIYHLTREMp 152
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtsgrilidgIDlRQIDPASLRRQI- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 153 psdktplhcvmevdterAMLEKEAErlahedaecekLME--LYE--RLEELDADKAEM-RASRILHGLGFTPAMQRK--- 224
Cdd:COG2274 552 -----------------GVVLQDVF-----------LFSgtIREniTLGDPDATDEEIiEAARLAGLHDFIEALPMGydt 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 225 KLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEE----LKTFK--RILVLVSHSQDFLNgVCTN 294
Cdd:COG2274 604 VVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAET----EAIilenLRRLLkgRTVIIIAHRLSTIR-LADR 678
|
250 260 270
....*....|....*....|....*....|....
gi 27881506 295 IIHMHNKKLKyYTGNYDQYVKTR---LELEENQM 325
Cdd:COG2274 679 IIVLDKGRIV-EDGTHEELLARKglyAELVQQQL 711
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
97-263 |
3.78e-10 |
|
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: 60.98 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 97 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHL-TREMPPSDKTPLHCVME--VDTERAMLE 173
Cdd:TIGR03873 13 GRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdLHGLSRRARARRVALVEqdSDTAVPLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 174 KEAERLAHEDaeceklmelYERLEELDADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLD 253
Cdd:TIGR03873 93 RDVVALGRIP---------HRSLWAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLD 162
|
170
....*....|
gi 27881506 254 EPTNHLDLDA 263
Cdd:TIGR03873 163 EPTNHLDVRA 172
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
90-306 |
3.81e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 60.00 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQelLSDTKLELN---SGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsDKTPLhcvmeVD 166
Cdd:cd03297 1 MLCVDIEKR--LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL----------NGTVL-----FD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 167 TERAMLEKEAER---LAHEDAECEKLMELYERLE----ELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVAL 239
Cdd:cd03297 64 SRKKINLPPQQRkigLVFQQYALFPHLNVRENLAfglkRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 240 ARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMHNKKLKYY 306
Cdd:cd03297 143 ARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
86-337 |
3.83e-10 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 60.49 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREV----PIPEHIDI-Y-----HL 147
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlgllpptsGTVRLfgkpPRRARRRIgYvpqraEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 148 TREMPPSdktplhcVMEV-----DTERAMLEkeaeRLAHEDaeCEKLMELyerLEELDADKaemRASRILHGLgftpamq 222
Cdd:COG1121 87 DWDFPIT-------VRDVvlmgrYGRRGLFR----RPSRAD--REAVDEA---LERVGLED---LADRPIGEL------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 223 rkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSHSQDFLNGVCTNIIHMh 299
Cdd:COG1121 141 -------SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDRVLLL- 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 27881506 300 NKKLkYYTGNYDQYVKtrlelEENQMKRFHWEQDQIAH 337
Cdd:COG1121 213 NRGL-VAHGPPEEVLT-----PENLSRAYGGPVALLAH 244
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
230-291 |
4.67e-10 |
|
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: 62.46 E-value: 4.67e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD------LDACVwleEELKTFKRILVLVSHSQDFLNGV 291
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAI---RALKARGATVVVITHRPSLLAAV 533
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
396-611 |
4.71e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGP----CIYNnLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV----------- 460
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferrALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 ----KIGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGLTGK-QQVSPIrNLSDGQKCRVCLA 528
Cdd:PRK13634 82 plrkKVGIVFQFPEHQLfeetvekDICFGPMNFGV---SEEDAKQKAREMIELVGLPEElLARSPF-ELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 529 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM--MLVSHDFRLIQQVAQEIWVCEKQTITKW--PGDILAYK 602
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLttVLVTHSMEDAARYADQIVVMHKGTVFLQgtPREIFADP 237
|
....*....
gi 27881506 603 EHLKSKLVD 611
Cdd:PRK13634 238 DELEAIGLD 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
90-303 |
4.92e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 59.69 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLlsaigkrevpipehidIYHLTREMPPSDKTP----LHCVMEV 165
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTT----------------IKMLTTLLKPTSGRAtvagHDVVREP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERAMLEKEAERLAHEDA-ECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALF 244
Cdd:cd03265 69 REVRRRIGIVFQDLSVDDElTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 245 IRPFMLLLDEPTNHLDLDA--CVW--LEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTraHVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
425-583 |
5.77e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.87 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 425 RVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQE---------QLDLDLSPLE--YMMKCYPEIKE- 492
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRigvvfgqrsQLWWDLPAIDsfRLLKAIYRIPDa 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 493 --KEEMRKIIGRYGLTGKQQVsPIRNLSDGQ--KCRVCLAWLawQNPHMLFLDEPTNHLDIETIDALADAINEF--EGG- 565
Cdd:COG4586 130 eyKKRLDELVELLDLGELLDT-PVRQLSLGQrmRCELAAALL--HRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGt 206
|
170
....*....|....*....
gi 27881506 566 -MMLVSHDFRLIQQVAQEI 583
Cdd:COG4586 207 tILLTSHDMDDIEALCDRV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
395-585 |
7.55e-10 |
|
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: 59.44 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI--------------RKHS 458
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 459 HVKIGRYHQHLQEQLDldlsPLeymMKCYPEIKE---------KEEMRKIIGRYGLTGKQQVSPIRN-----LSDGQKCR 524
Cdd:cd03257 81 RKEIQMVFQDPMSSLN----PR---MTIGEQIAEplrihgklsKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 525 VCLAW-LAwQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:cd03257 154 VAIARaLA-LNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
90-300 |
9.24e-10 |
|
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: 59.37 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHiDIYHL-------- 147
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgflrptsgsvlfdGEDITGLPPH-EIARLgigrtfqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 148 TREMPpsDKTPLHCVM---EVDTERAMLEKEAERlaHEDAECEKLMELYERLEeLdADKAEMRASRILHGlgftpamQRK 224
Cdd:cd03219 84 PRLFP--ELTVLENVMvaaQARTGSGLLLARARR--EEREARERAEELLERVG-L-ADLADRPAGELSYG-------QQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 225 klkdfsggwrmRVALARALFIRPFMLLLDEPT---NHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHN 300
Cdd:cd03219 151 -----------RLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
86-298 |
9.80e-10 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 58.94 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTF--HGQ-----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHL----------T 148
Cdd:TIGR02324 2 LEVEDLSKTFtlHQQggvrlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEgawvdlaqasP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 149 REMPPSDKTP-------LHCVMEVDTERAMLEKEAERLAHEDAECEKLMELYERLEeldadkaemRASRILHglgFTPAM 221
Cdd:TIGR02324 82 REVLEVRRKTigyvsqfLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLN---------IPERLWH---LPPAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 222 qrkklkdFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL---DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHM 298
Cdd:TIGR02324 150 -------FSGGEQQRVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVMDV 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
93-305 |
1.40e-09 |
|
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: 58.27 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 93 LTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHL-TREMPPSDKtPLhcvmevdterAM 171
Cdd:cd03298 6 IRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdVTAAPPADR-PV----------SM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 172 LEKEAERLAHEDAECEKLMELYERLEELDADKAEMRAsrILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLL 251
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEV--ALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 252 LDEPTNHLD-------LDACVWLEEELKTfkrILVLVSHSQDFLNGVCTNIIHMHNKKLKY 305
Cdd:cd03298 152 LDEPFAALDpalraemLDLVLDLHAETKM---TVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
396-588 |
1.45e-09 |
|
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: 58.71 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-KHSHVK---IGRYHQHL- 469
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILlDGVDIRdlnLRWLRSQIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 470 ---QEQLDLDLSPLEYMMKCYPEIKEKEEMR--------KII----GRY----GLTGKQqvspirnLSDGQKCRVCLAWL 530
Cdd:cd03249 81 lvsQEPVLFDGTIAENIRYGKPDATDEEVEEaakkanihDFImslpDGYdtlvGERGSQ-------LSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 531 AWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRL--IQQvAQEIWVCEK 588
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLstIRN-ADLIAVLQN 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
86-306 |
1.51e-09 |
|
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: 58.29 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP------IPEHIDIYHLTREMP----- 152
Cdd:cd03263 1 LQIRNLTKTYKKGTKpaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtsgtayINGYSIRTDRKAARQslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 153 PSDKT--PLHCVMEvdteramlekeaerlahedaecekLMELYERLEELDADKAEMRASRILHGLGFTPamQRKKL-KDF 229
Cdd:cd03263 81 PQFDAlfDELTVRE------------------------HLRFYARLKGLPKSEIKEEVELLLRVLGLTD--KANKRaRTL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTnhLDLDAC----VW--LEEELKtfKRILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:cd03263 135 SGGMKRKLSLAIALIGGPSVLLLDEPT--SGLDPAsrraIWdlILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
...
gi 27881506 304 KYY 306
Cdd:cd03263 211 RCI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
101-286 |
1.59e-09 |
|
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: 58.50 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIyhltREMPPsdktplhcvmevdteramlEKE 175
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkDI----TNLPP-------------------EKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 176 AERLAHEDAECEKLMELYERLE----ELDADKAEM--RASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARALFIRPFM 249
Cdd:cd03299 72 DISYVPQNYALFPHMTVYKNIAyglkKRKVDKKEIerKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27881506 250 LLLDEPTNHLDLDACVWLEEELKTFKR---ILVL-VSHSQD 286
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKefgVTVLhVTHDFE 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
90-284 |
1.96e-09 |
|
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: 58.35 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPE-----------------HIDIYHLTREM- 151
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkdiydlDVDVLELRRRVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 152 ------PPSDKTplhcVME--VDTERAMLEKEAERLAHEDAECEKLMELYERLeeldADKaemrasriLHGLGFtpamqr 223
Cdd:cd03260 85 mvfqkpNPFPGS----IYDnvAYGLRLHGIKLKEELDERVEEALRKAALWDEV----KDR--------LHALGL------ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 224 kklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHS 284
Cdd:cd03260 143 ------SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
90-303 |
1.99e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDktplhcVMEVDTER 169
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD------ERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 AMLEKEAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFM 249
Cdd:PRK09493 80 GMVFQQFYLFPHLTA-LENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 250 LLLDEPTNHLD-------LDACVWLEEELKTfkriLVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:PRK09493 158 MLFDEPTSALDpelrhevLKVMQDLAEEGMT----MVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
90-261 |
2.06e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 58.59 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPS------DKTPLH--C 161
Cdd:COG4559 6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKL----------------LTGELTPSsgevrlNGRPLAawS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 162 VMEVDTERAMLEKEAE--------------RLAH--EDAECEKLMElyERLEELDADkaeMRASRILHGLgftpamqrkk 225
Cdd:COG4559 70 PWELARRRAVLPQHSSlafpftveevvalgRAPHgsSAAQDRQIVR--EALALVGLA---HLAGRSYQTL---------- 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881506 226 lkdfSGGWRMRVALARAL-------FIRPFMLLLDEPTNHLDL 261
Cdd:COG4559 135 ----SGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
395-621 |
2.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGPCIYNNLeFGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR--------------- 455
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRAL-FDIDLEVKkgsyTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 456 KHSHVKIGRYHQHLQEQL-------DLDLSPLEYMMkcypeikEKEEMRKIIGR----YGLTGK-QQVSPIRnLSDGQKC 523
Cdd:PRK13643 80 KPVRKKVGVVFQFPESQLfeetvlkDVAFGPQNFGI-------PKEKAEKIAAEklemVGLADEfWEKSPFE-LSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 524 RVCLAWLAWQNPHMLFLDEPTNHLD----IETIDaLADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKW--PGD 597
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCgtPSD 230
|
250 260
....*....|....*....|....
gi 27881506 598 ILAYKEHLKSklvdEEPQLTKRTH 621
Cdd:PRK13643 231 VFQEVDFLKA----HELGVPKATH 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
396-583 |
2.17e-09 |
|
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: 57.61 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGR----- 464
Cdd:cd03268 1 LKTNDLTKTY-GKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyQKNIEALRRigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 465 ----YHQHLQEQLDLDLSPLEYMmkcypeiKEKEEMRKIIGRYGL--TGKQQVspiRNLSDGQKCRVCLAWLAWQNPHML 538
Cdd:cd03268 79 eapgFYPNLTARENLRLLARLLG-------IRKKRIDEVLDVVGLkdSAKKKV---KGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881506 539 FLDEPTNHLDIETIDALADAI---NEFEGGMMLVSHDFRLIQQVAQEI 583
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELIlslRDQGITVLISSHLLSEIQKVADRI 196
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
396-612 |
2.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCI---YNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------------KH 457
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 458 SHVKIGRYHQHLQEQL-------DLDLSPLEYmmkCYPEIKEKEEMRKIIGRYGLtgKQQV---SPIrNLSDGQKCRVCL 527
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfentvlkDVEFGPKNF---GFSEDEAKEKALKWLKKVGL--SEDLiskSPF-ELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 528 AWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHDFRLIQQVAQEIWVCEKQTITKW--PGDILAYK 602
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHasPKEIFSDK 236
|
250
....*....|
gi 27881506 603 EHLKSKLVDE 612
Cdd:PRK13641 237 EWLKKHYLDE 246
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
88-298 |
2.60e-09 |
|
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: 57.96 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTREMPPSDKTplhcVMEVD 166
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLR----------------CLNGLVEPTSGS----VLIDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 167 TERAMLEKEAER-LAHEDAECEKLMELYERLEELDAdkaemrasrILHG-LGFTP-------------------AMQRKK 225
Cdd:cd03256 63 TDINKLKGKALRqLRRQIGMIFQQFNLIERLSVLEN---------VLSGrLGRRStwrslfglfpkeekqralaALERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 226 LKDF--------SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACvwlEEELKTFKRI------LVLVS-HSQDFLNG 290
Cdd:cd03256 134 LLDKayqradqlSGGQQQRVAIARALMQQPKLILADEPVASLDPASS---RQVMDLLKRInreegiTVIVSlHQVDLARE 210
|
....*...
gi 27881506 291 VCTNIIHM 298
Cdd:cd03256 211 YADRIVGL 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
90-261 |
2.72e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.24 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPS------DKTPLHcvm 163
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRA----------------LSGELSPDsgevrlNGRPLA--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 evDTERAMLekeAERLA--------------HEDAEceklMELYERLEELDADKAEMRAsrilhglgftpAMQRKKLKDF 229
Cdd:PRK13548 68 --DWSPAEL---ARRRAvlpqhsslsfpftvEEVVA----MGRAPHGLSRAEDDALVAA-----------ALAQVDLAHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881506 230 --------SGGWRMRVALARAL------FIRPFMLLLDEPTNHLDL 261
Cdd:PRK13548 128 agrdypqlSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
86-303 |
2.74e-09 |
|
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: 58.12 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--------------------- 144
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpvqernvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 145 YHLTREMPPSDKTPLhcvmevdterAMLEKEAERLAHEDAECEKLMELYE--RLEELdadkaemrASRILHGLgftpamq 222
Cdd:cd03296 83 YALFRHMTVFDNVAF----------GLRVKPRSERPPEAEIRAKVHELLKlvQLDWL--------ADRYPAQL------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 223 rkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHldLDACVwlEEELKTFKRIL--------VLVSHSQDFLNGVCTN 294
Cdd:cd03296 138 -------SGGQRQRVALARALAVEPKVLLLDEPFGA--LDAKV--RKELRRWLRRLhdelhvttVFVTHDQEEALEVADR 206
|
....*....
gi 27881506 295 IIHMHNKKL 303
Cdd:cd03296 207 VVVMNKGRI 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
195-303 |
2.85e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 57.75 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 195 RLEELDADKAEMRASRILHGLGFTPAMQRK--KLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDAcv 265
Cdd:COG1136 112 LLAGVSRKERRERARELLERVGLGDRLDHRpsQL---SGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL-- 186
|
90 100 110
....*....|....*....|....*....|....*...
gi 27881506 266 wLEEELKTFKRILVLVSHSQDFLNgVCTNIIHMHNKKL 303
Cdd:COG1136 187 -LRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
396-576 |
3.29e-09 |
|
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: 57.04 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR----KHSHVKIGRYHQHL-- 469
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgiDISTIPLEDLRSSLti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 470 --QE------QLDLDLSPleymmkcYPEIKEKEEMRKI-IGRYGLtgkqqvspirNLSDGQKCRVCLAWLAWQNPHMLFL 540
Cdd:cd03369 87 ipQDptlfsgTIRSNLDP-------FDEYSDEEIYGALrVSEGGL----------NLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881506 541 DEPTNHLDIETiDALADAI--NEFEGGMML-VSHDFRLI 576
Cdd:cd03369 150 DEATASIDYAT-DALIQKTirEEFTNSTILtIAHRLRTI 187
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
396-588 |
3.36e-09 |
|
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: 57.63 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQH-LQEQL- 473
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-DIREVTLDsLRRAIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 474 --------------------DLDLSPLEYMMKC-----YPEIKE-KEEMRKIIGRYGLtgkqqvspirNLSDGQKCRVCL 527
Cdd:cd03253 79 vvpqdtvlfndtigynirygRPDATDEEVIEAAkaaqiHDKIMRfPDGYDTIVGERGL----------KLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 528 AWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEK 588
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLSTIVN-ADKIIVLKD 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
396-575 |
6.51e-09 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 56.34 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPC--IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRY- 465
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 HQHL----QeQLDL--DLSPLEY----MMKCYPEIKEKEEM-RKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAwQ 533
Cdd:cd03255 81 RRHIgfvfQ-SFNLlpDLTALENvelpLLLAGVPKKERRERaEELLERVGLGDRLNHYP-SELSGGQQQRVAIArALA-N 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881506 534 NPHMLFLDEPTNHLDIET----IDALADaINEFEG-GMMLVSHDFRL 575
Cdd:cd03255 158 DPKIILADEPTGNLDSETgkevMELLRE-LNKEAGtTIVVVTHDPEL 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
86-284 |
6.97e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 57.02 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFH----GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsDKTPlhc 161
Cdd:COG1116 8 LELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV----------DGKP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 162 VMEVDTERAMLekeaerlAHEDAecekLM---------ELYERLEELDADKAEMRASRILHGLGftpamqrkkLKDF--- 229
Cdd:COG1116 75 VTGPGPDRGVV-------FQEPA----LLpwltvldnvALGLELRGVPKAERRERARELLELVG---------LAGFeda 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 230 -----SGGWRMRVALARALFIRPFMLLLDEPTNHLD----LDACVWLEEELKTFKRILVLVSHS 284
Cdd:COG1116 135 yphqlSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHD 198
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
198-260 |
7.58e-09 |
|
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: 58.54 E-value: 7.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 198 ELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG4172 395 GLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
84-292 |
7.72e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.95 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 84 TDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKreVPIPEHIDIYHltREMPPSDKTPlhcvM 163
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFAR--LLTPQSGTVFL--GDKPISMLSS----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 EVDTERAMLEKEaeRLAHEDAECEKLME--------LYERLEELDADKAE--MRASRILHglgftpaMQRKKLKDFSGGW 233
Cdd:PRK11231 73 QLARRLALLPQH--HLTPEGITVRELVAygrspwlsLWGRLSAEDNARVNqaMEQTRINH-------LADRRLTDLSGGQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 234 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSHSqdfLNGVC 292
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRlmrELNTQGKTVVTVLHD---LNQAS 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
230-286 |
7.96e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.80 E-value: 7.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELktfKRIL-------VLVSHSQD 286
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL---RRLQrelgitfIYVTHDQE 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
198-260 |
8.04e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 8.04e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 198 ELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK15134 395 TLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
399-588 |
9.94e-09 |
|
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: 55.94 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 399 QNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-----------RKHSHVKIGRYH 466
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyeHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 467 QH-------LQEQLDLDLSPLEYMmkCYPEIKEKEEMRKIIGRY--------GLTGKQqvspirnLSDGQKCRVCLAWLA 531
Cdd:cd03248 95 QEpvlfarsLQDNIAYGLQSCSFE--CVKEAAQKAHAHSFISELasgydtevGEKGSQ-------LSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 532 WQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLVSHDFRLIQQvAQEIWVCEK 588
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDG 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
396-559 |
1.11e-08 |
|
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: 56.08 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGRYHQH--- 468
Cdd:cd03254 3 IEFENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgIDIRDISRKSLRSMigv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 -LQEQLDLDLSPLEYMMKCYPEIKEKEEMR--KIIGRYGLTGK------QQVSPI-RNLSDGQKCRVCLAWLAWQNPHML 538
Cdd:cd03254 82 vLQDTFLFSGTIMENIRLGRPNATDEEVIEaaKEAGAHDFIMKlpngydTVLGENgGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180
....*....|....*....|.
gi 27881506 539 FLDEPTNHLDIETIDALADAI 559
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEAL 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
90-260 |
1.16e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.06 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSM---LLSAIGKREVP--IPEHIDIYHLtremppsdktPLHcvme 164
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGniIIDDEDISLL----------PLH---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 165 vdtERAM-----LEKEA---ERLAHEDaeceKLMELYERLEELDADKAEMRASRILHglGFTPAMQRKKL-KDFSGGWRM 235
Cdd:PRK10895 74 ---ARARrgigyLPQEAsifRRLSVYD----NLMAVLQIRDDLSAEQREDRANELME--EFHIEHLRDSMgQSLSGGERR 144
|
170 180
....*....|....*....|....*
gi 27881506 236 RVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
393-571 |
1.22e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 393 PPVIMVQNVSFkyTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH-------VKIGRY 465
Cdd:PRK13543 9 PPLLAAHALAF--SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 HQHLqEQLDLDLSPLEYM-MKCYPEIKEKEEM-RKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLaWQNPHMLF-LDE 542
Cdd:PRK13543 87 LGHL-PGLKADLSTLENLhFLCGLHGRRAKQMpGSALAIVGLAGYED-TLVRQLSAGQKKRLALARL-WLSPAPLWlLDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 27881506 543 PTNHLDIETIDALADAINEF---EGGMMLVSH 571
Cdd:PRK13543 164 PYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
195-284 |
1.23e-08 |
|
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: 55.56 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 195 RLEELDADKAEMRASRILHGLGftpamqrkkLKDF--------SGGWRMRVALARALFIRPFMLLLDEPTNHLD----LD 262
Cdd:cd03293 99 ELQGVPKAEARERAEELLELVG---------LSGFenayphqlSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQ 169
|
90 100
....*....|....*....|..
gi 27881506 263 ACVWLEEELKTFKRILVLVSHS 284
Cdd:cd03293 170 LQEELLDIWRETGKTVLLVTHD 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
196-303 |
1.34e-08 |
|
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: 55.90 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 196 LEELDADKAEMRASRILH--GLGftpamQR-----KKLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------L 261
Cdd:COG4181 115 LELAGRRDARARARALLErvGLG-----HRldhypAQL---SGGEQQRVALARAFATEPAILFADEPTGNLDaatgeqiI 186
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27881506 262 DACVWLEEELKTfkrILVLVSHSQDfLNGVCTNIIHMHNKKL 303
Cdd:COG4181 187 DLLFELNRERGT---TLVLVTHDPA-LAARCDRVLRLRAGRL 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
396-583 |
1.38e-08 |
|
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: 56.04 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKHSHv 460
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalRQLRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 KIGRYHQHLQ--EQLDL----------DLSPLEYMMKCYPEIkEKEEMRKIIGRYGLTGK--QQVSpirNLSDGQKCRVC 526
Cdd:cd03256 79 QIGMIFQQFNliERLSVlenvlsgrlgRRSTWRSLFGLFPKE-EKQRALAALERVGLLDKayQRAD---QLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 527 LAWLAWQNPHMLFLDEPTNHLDIET----IDALADaINEFEGGMMLVS-HDFRLIQQVAQEI 583
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsrqvMDLLKR-INREEGITVIVSlHQVDLAREYADRI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
427-550 |
1.50e-08 |
|
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: 55.28 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 427 ALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQHLQEQL-----DLDLSP-------LEYM--MKCYPEIKE 492
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ-DVLKQPQKLRRRIgylpqEFGVYPnftvrefLDYIawLKGIPSKEV 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 493 KEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIE 550
Cdd:cd03264 108 KARVDEVLELVNLGDRAK-KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
86-312 |
1.52e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DI---------------- 144
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtDVsrlhardrkvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 145 YHLTREMPPSDKTPLHCVMEVDTER---AMLEKeaerlahedaeceKLMELYE--RLEELdadkaemrASRIlhglgftP 219
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVLPRRERpnaAAIKA-------------KVTQLLEmvQLAHL--------ADRY-------P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 220 AmqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHldLDACV------WLEEELKTFKRILVLVSHSQDFLNGVCT 293
Cdd:PRK10851 135 A-------QLSGGQKQRVALARALAVEPQILLLDEPFGA--LDAQVrkelrrWLRQLHEELKFTSVFVTHDQEEAMEVAD 205
|
250
....*....|....*....
gi 27881506 294 NIIHMHNkklkyytGNYDQ 312
Cdd:PRK10851 206 RVVVMSQ-------GNIEQ 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
106-303 |
1.58e-08 |
|
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: 57.50 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 106 LELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVPI-PEHIDIyhltremppSDKTPLhcvmevDTERA-----M 171
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsGEVNVRVgDEWVDM---------TKPGPD------GRGRAkryigI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 172 LEKEAERLAHEDAecekLMELYERLE-ELDADKAEMRASRILHGLGFTPAMQRKKLKDF----SGGWRMRVALARALFIR 246
Cdd:TIGR03269 370 LHQEYDLYPHRTV----LDNLTEAIGlELPDELARMKAVITLKMVGFDEEKAEEILDKYpdelSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 247 PFMLLLDEPTNHLD-------LDACVWLEEEL-KTFkrilVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:TIGR03269 446 PRIVILDEPTGTMDpitkvdvTHSILKAREEMeQTF----IIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
90-317 |
1.61e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQE----LLSDTKLELNSGRRYGLIGLNGIGKSM-------LLSAIGK---------REV-PIPEHidiyHLT 148
Cdd:PRK09473 17 DLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRiggsatfngREIlNLPEK----ELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 149 R------EMPPSDK-TPLHCVMEVDteramlekeaerlahedaecEKLMELYERLEELDADKAEMRASRILHGLGFTPAM 221
Cdd:PRK09473 93 KlraeqiSMIFQDPmTSLNPYMRVG--------------------EQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 222 QRKKL--KDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDA---CVWLEEELKT-FKRILVLVSHSQDFLNGVCTNI 295
Cdd:PRK09473 153 KRMKMypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKReFNTAIIMITHDLGVVAGICDKV 232
|
250 260
....*....|....*....|..
gi 27881506 296 IHMhnkklkyYTGNYDQYVKTR 317
Cdd:PRK09473 233 LVM-------YAGRTMEYGNAR 247
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
426-589 |
1.74e-08 |
|
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: 55.88 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDGMIR--------KHSHVKI---GRYHQHLQEQLDLDLSPLEYMMkcypEIKEKE 494
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEieldtvsyKPQYIKAdyeGTVRDLLSSITKDFYTHPYFKT----EIAKPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 495 EMRKIIgrygltgKQQVspiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF----EGGMMLVS 570
Cdd:cd03237 104 QIEQIL-------DREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVE 173
|
170
....*....|....*....
gi 27881506 571 HDFRLIQQVAQEIWVCEKQ 589
Cdd:cd03237 174 HDIIMIDYLADRLIVFEGE 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
425-584 |
1.77e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.62 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 425 RVALVGPNGAGKSTLLKLLTgellptdGMIRKHSHVkigryhqHLQEQLDLDLSPLE---------------YMMKCY-- 487
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMA-------GLLPGQGEI-------LLNGRPLSDWSAAElarhraylsqqqsppFAMPVFqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 488 ---------PEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQ-----NPH--MLFLDEPTNHLDIET 551
Cdd:COG4138 90 lalhqpagaSSEAVEQLLAQLAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVAQ 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881506 552 IDALADAINEF--EGGMMLVS-HDFRLIQQVAQEIW 584
Cdd:COG4138 169 QAALDRLLRELcqQGITVVMSsHDLNHTLRHADRVW 204
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
504-621 |
1.92e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 504 GLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEI 583
Cdd:PRK10636 137 GFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27881506 584 WVCEKQTITKWPGDILAYKEHLKSKLVDE----EPQLTKRTH 621
Cdd:PRK10636 217 IHIEQQSLFEYTGNYSSFEVQRATRLAQQqamyESQQERVAH 258
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
419-585 |
2.40e-08 |
|
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: 55.43 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLD----TRVALVGPNGAGKSTLLKLLTGELLPTDGMI--------RKHSH-------------------------VK 461
Cdd:COG0411 22 DVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditGLPPHriarlgiartfqnprlfpeltvlenVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 462 IGRyHQHLQEQLDLDLSPLEYMMKcyPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRV----CLAwlawQNPHM 537
Cdd:COG0411 102 VAA-HARLGRGLLAALLRLPRARR--EEREARERAEELLERVGLADRADE-PAGNLSYGQQRRLeiarALA----TEPKL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881506 538 LFLDEPT---NHLDIETIDALADAINEFEG-GMMLVSHDFRLIQQVAQEIWV 585
Cdd:COG0411 174 LLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
86-303 |
2.54e-08 |
|
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: 54.99 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLsaigKrevpipehidiyHLTREMPPSDKTplhcvMEV 165
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLL----K------------LIIGLLRPDSGE-----ILV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTER--AMLEKEAERLAHE-----------DAeceklMELYE----RLEE---LDADKAEMRASRILH--GLgftPAMQR 223
Cdd:COG1127 65 DGQDitGLSEKELYELRRRigmlfqggalfDS-----LTVFEnvafPLREhtdLSEAEIRELVLEKLElvGL---PGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 224 KKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMH 299
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLA 216
|
....
gi 27881506 300 NKKL 303
Cdd:COG1127 217 DGKI 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
396-583 |
3.46e-08 |
|
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: 53.73 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhlqeqldL 475
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-------------------I 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 476 DLSPLEYMMKCYPEIKEKEEMrkIIGRYGL----TGKQQVSpiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIET 551
Cdd:cd03229 60 DGEDLTDLEDELPPLRRRIGM--VFQDFALfphlTVLENIA--LGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881506 552 ---IDALADAINEFEG-GMMLVSHDFRLIQQVAQEI 583
Cdd:cd03229 136 rreVRALLKSLQAQLGiTVVLVTHDLDEAARLADRV 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
229-302 |
3.49e-08 |
|
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: 53.54 E-value: 3.49e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF--KRILVLVSHSqdfLNGV--CTNIIHMHNKK 302
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALakGKTVIVIAHR---LSTIrdADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
90-285 |
3.53e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.72 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLtrempPSDKTPLHCV-- 162
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqDITHV-----PAENRHVNTVfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 -------MEVdteramLEKEAERLahedaECEKL--MELYERLEEldadkaemrASRILHglgfTPAMQRKKLKDFSGGW 233
Cdd:PRK09452 94 syalfphMTV------FENVAFGL-----RMQKTpaAEITPRVME---------ALRMVQ----LEEFAQRKPHQLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 234 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQ 285
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQ 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
427-583 |
3.58e-08 |
|
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: 54.21 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 427 ALVGPNGAGKSTLLKLLTGELLPTDGMIR-KHSHVKIGRYHQ--HLQEQ--LDLDLSPLEYMM-----KCYPEIKEKEEM 496
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLDIAARNRigYLPEErgLYPKMKVIDQLVylaqlKGLKKEEARRRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 497 RKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHDF 573
Cdd:cd03269 110 DEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQM 188
|
170
....*....|
gi 27881506 574 RLIQQVAQEI 583
Cdd:cd03269 189 ELVEELCDRV 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
86-286 |
5.79e-08 |
|
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: 53.41 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPipEHIDIYHLTREM---PPSDKtplhcv 162
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEP--TSGRIYIGGRDVtdlPPKDR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 mevdtERAMLEKEAERLAHedaeceklMELYE------RLEELDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMR 236
Cdd:cd03301 73 -----DIAMVFQNYALYPH--------MTVYDniafglKLRKVPKDEIDERVREVAELLQIEHLLDRKP-KQLSGGQRQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881506 237 VALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQD 286
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtttIYVTHDQV 192
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
396-618 |
6.29e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIY---NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGM-----------IRKHSHVK 461
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 462 -----IGRYHQHLQEQL-------DLDLSPL---EYMMKCYPEIKEKEEMRKIIGRYGltgkqQVSPIRnLSDGQKCRVC 526
Cdd:PRK13645 87 rlrkeIGLVFQFPEYQLfqetiekDIAFGPVnlgENKQEAYKKVPELLKLVQLPEDYV-----KRSPFE-LSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 527 LAWLAWQNPHMLFLDEPTNHLDIETIDalaDAINEFE-------GGMMLVSHDFRLIQQVAQEIWVC-EKQTITKW-PGD 597
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEE---DFINLFErlnkeykKRIIMVTHNMDQVLRIADEVIVMhEGKVISIGsPFE 237
|
250 260
....*....|....*....|.
gi 27881506 598 ILAYKEhLKSKLVDEEPQLTK 618
Cdd:PRK13645 238 IFSNQE-LLTKIEIDPPKLYQ 257
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
200-286 |
6.33e-08 |
|
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: 55.12 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 200 DADKAEMRAS--RILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL----DACVWLEEELKT 273
Cdd:TIGR02142 102 RARPSERRISfeRVIELLGIGHLLGRLP-GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAE 180
|
90
....*....|...
gi 27881506 274 FKRILVLVSHSQD 286
Cdd:TIGR02142 181 FGIPILYVSHSLQ 193
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
196-303 |
7.92e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.52 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 196 LEELDADKAEM--RASRILH--GLGftpamqrKKLKDF----SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACvwl 267
Cdd:COG2884 104 LRVTGKSRKEIrrRVREVLDlvGLS-------DKAKALphelSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS--- 173
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27881506 268 EEELKTFKRI------LVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:COG2884 174 WEIMELLEEInrrgttVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
412-571 |
8.53e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 412 IYNNLEFGIDLDTRVALVGPNGAGKST--LLKLLTGELLPTDGMIRKhshvkigryhqhLQEQLDLDLSPLEymmkCYPE 489
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTllRLLAGALKGTPVAGCVDV------------PDNQFGREASLID----AIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 490 IKEKEEMRKIIGRYGLTGKQQ-VSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALA----DAINEFEG 564
Cdd:COG2401 109 KGDFKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVArnlqKLARRAGI 188
|
....*..
gi 27881506 565 GMMLVSH 571
Cdd:COG2401 189 TLVVATH 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
419-579 |
9.79e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.53 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLltgellptdgmIRKHSHVKIGRYHQHLQEQLDLDLSPLE------YMMKCYP 488
Cdd:cd03217 18 GVNLTIKkgevHALMGPNGSGKSTLAKT-----------IMGHPKYEVTEGEILFKGEDITDLPPEErarlgiFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 489 E----IKEKEEMRKIigRYGLTGkqqvspirnlsdGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-- 562
Cdd:cd03217 87 PeipgVKNADFLRYV--NEGFSG------------GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLre 152
|
170
....*....|....*...
gi 27881506 563 EG-GMMLVSHDFRLIQQV 579
Cdd:cd03217 153 EGkSVLIITHYQRLLDYI 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
392-607 |
1.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.70 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKYTkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----------RK---HS 458
Cdd:PRK13636 2 EDYILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysRKglmKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 459 HVKIGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGltgkqqVSPIRN-----LSDGQKCRVC 526
Cdd:PRK13636 81 RESVGMVFQDPDNQLfsasvyqDVSFGAVNLKL---PEDEVRKRVDNALKRTG------IEHLKDkpthcLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 527 LAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGM----MLVSHDFRLIQQVAQEIWVCEKQTIT--KWPGDILA 600
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgltiIIATHDIDIVPLYCDNVFVMKEGRVIlqGNPKEVFA 231
|
....*..
gi 27881506 601 YKEHLKS 607
Cdd:PRK13636 232 EKEMLRK 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-581 |
1.12e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-----------KI 462
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQHLQEQL-------DLDLS------PLEYMMkcypeikekEEMRKIIGRYGLTGKQQVSPIRnLSDGQKCRVCLAW 529
Cdd:PRK13635 84 GMVFQNPDNQFvgatvqdDVAFGlenigvPREEMV---------ERVDQALRQVGMEDFLNREPHR-LSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 530 LAWQNPHMLFLDEPTNHLD-------IETIDALADainefEGGMMLVS--HDfrlIQQVAQ 581
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrrevLETVRQLKE-----QKGITVLSitHD---LDEAAQ 206
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
427-585 |
1.24e-07 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 53.28 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 427 ALVGPNGAGKSTLLKLLTGELLPTDG-----------MIRKHSHVKIGRYHQHLQEQLDLD------LSPLEYMMKCYPE 489
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGtvdlagvdlhgLSRRARARRVALVEQDSDTAVPLTvrdvvaLGRIPHRSLWAGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 490 IKEKEEM-RKIIGRYGLTGKQQVSpIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM 566
Cdd:TIGR03873 111 SPHDAAVvDRALARTELSHLADRD-MSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELaaTGVT 189
|
170 180
....*....|....*....|
gi 27881506 567 MLVS-HDFRLIQQVAQEIWV 585
Cdd:TIGR03873 190 VVAAlHDLNLAASYCDHVVV 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
415-571 |
1.38e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 415 NLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHShVKIGR----YHQHL-----QEQLDLDLSPLE---- 481
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-EPIRRqrdeYHQDLlylghQPGIKTELTALEnlrf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 482 --YMMKCYPEikekEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 559
Cdd:PRK13538 98 yqRLHGPGDD----EALWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*
gi 27881506 560 NEF--EGGM-MLVSH 571
Cdd:PRK13538 173 AQHaeQGGMvILTTH 187
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
395-588 |
1.38e-07 |
|
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: 52.97 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKH 457
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 458 SHvKIGRYHQHLQ--------EQLDLdlsPLEYMMKCYPEIKEK-EEMRKIIGrygLTGKQQVSPiRNLSDGQKCRVCLA 528
Cdd:cd03258 81 RR-RIGMIFQHFNllssrtvfENVAL---PLEIAGVPKAEIEERvLELLELVG---LEDKADAYP-AQLSGGQKQRVGIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 529 WLAWQNPHMLFLDEPTNHLDIET---IDALADAIN-EFEGGMMLVSHDFRLIQQVAQEIWVCEK 588
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETtqsILALLRDINrELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
426-584 |
1.40e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTlLKLLTGELLPTDGMIR-------KHSHVKIGRYHQHLQEQ------------LDLDLSPleymmKC 486
Cdd:PRK03695 25 LHLVGPNGAGKST-LLARMAGLLPGSGSIQfagqpleAWSAAELARHRAYLSQQqtppfampvfqyLTLHQPD-----KT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 487 YPEIKEKeEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQ-----NPH--MLFLDEPTNHLDIETIDALADAI 559
Cdd:PRK03695 99 RTEAVAS-ALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180
....*....|....*....|....*...
gi 27881506 560 NEF--EGGMMLVS-HDFRLIQQVAQEIW 584
Cdd:PRK03695 177 SELcqQGIAVVMSsHDLNHTLRHADRVW 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
87-283 |
1.44e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.48 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 87 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-----------GKREVpipEHIDIYHLtremPPSD 155
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspafsasGEVLL---NGRRLTAL----PAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 156 K-------TPL---HcvMEVDTERAM-----LEKEAERLAHEDAeceklmelyerLEELDadkaemrasriLHGLGF-TP 219
Cdd:COG4136 76 RrigilfqDDLlfpH--LSVGENLAFalpptIGRAQRRARVEQA-----------LEEAG-----------LAGFADrDP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 220 AmqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD--LDACV--WLEEELKTFKRILVLVSH 283
Cdd:COG4136 132 A-------TLSGGQRARVALLRALLAEPRALLLDEPFSKLDaaLRAQFreFVFEQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
396-591 |
1.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGP---CIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-----------RKHSHV- 460
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkVKLSDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 -KIGRYHQHLQEQL-------DLDLSPLEYMMKcYPEIKE--KEEMrKIIGRYGLTGKQQvSPIrNLSDGQKCRVCLAWL 530
Cdd:PRK13637 83 kKVGLVFQYPEYQLfeetiekDIAFGPINLGLS-EEEIENrvKRAM-NIVGLDYEDYKDK-SPF-ELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 531 AWQNPHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTI 591
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
99-286 |
1.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.24 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 99 ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDKTplhcVMEVDTERAMLEKEAER 178
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKY----IRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 179 LAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNH 258
Cdd:PRK13646 97 QLFEDT-VEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|..
gi 27881506 259 LDLDACVWLEEELKTFK----RILVLVSHSQD 286
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtdenKTIILVSHDMN 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
90-298 |
1.84e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI--DIYHLTRemppsdktplHCVMEVDT 167
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwlDGEHIQH----------YASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 168 ERAMLEKEA---------ERLAHEDAECEKLMELYeRLEELDADKAEMRASRILHglgftpaMQRKKLKDFSGGWRMRVA 238
Cdd:PRK10253 82 RIGLLAQNAttpgditvqELVARGRYPHQPLFTRW-RKEDEEAVTKAMQATGITH-------LADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR----ILVLVSHSqdfLNGVCTNIIHM 298
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQACRYASHL 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
419-549 |
1.94e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.47 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDG----------------------MIRKHSH----------VKI 462
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGevrlngrpladwspaelarrraVLPQHSSlsfpftveevVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHqHLQEQLDLDLSPLEYMMKCypeikekeemrkiigryGLTGKQQvSPIRNLSDGQKCRVCLA------WLAWQNPH 536
Cdd:PRK13548 100 GRAP-HGLSRAEDDALVAAALAQV-----------------DLAHLAG-RDYPQLSGGEQQRVQLArvlaqlWEPDGPPR 160
|
170
....*....|...
gi 27881506 537 MLFLDEPTNHLDI 549
Cdd:PRK13548 161 WLLLDEPTSALDL 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
412-598 |
2.19e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.06 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 412 IYNNLEFGIDLD----TRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGR-------------YHQHLQ 470
Cdd:COG3840 10 RYGDFPLRFDLTiaagERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngQDLTALPPAErpvsmlfqennlfPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 471 EQLDLDLSPleymmKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAWQNPHMLfLDEPTNHLDI 549
Cdd:COG3840 90 QNIGLGLRP-----GLKLTAEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALArCLVRKRPILL-LDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881506 550 ----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQE-IWVCEKQTItkWPGDI 598
Cdd:COG3840 163 alrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRvLLVADGRIA--ADGPT 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
88-303 |
2.24e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 51.76 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIY---HLTREMPPsdktplhcvme 164
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILfkgEDITDLPP----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 165 vdTERAmlekeaerlahedaeceklmelyerleeldadkaemrasrilhGLGFTPAMQRK------KLKD--------FS 230
Cdd:cd03217 72 --EERA-------------------------------------------RLGIFLAFQYPpeipgvKNADflryvnegFS 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 231 GGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRI---LVLVSHSQDFLNGVCTNIIH-MHNKKL 303
Cdd:cd03217 107 GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEgksVLIITHYQRLLDYIKPDRVHvLYDGRI 183
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
87-297 |
2.35e-07 |
|
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: 52.26 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 87 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIY---HLTREMPPSDK------- 156
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILfkgQDLLELEPDERaraglfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 157 ---TPLHC--VMEVDTERAMLEkeaerlAHEDAECEKLMELYERLEELDadkaEMRASrilhgLGFTPAMQRKKLKD-FS 230
Cdd:TIGR01978 82 afqYPEEIpgVSNLEFLRSALN------ARRSARGEEPLDLLDFEKLLK----EKLAL-----LDMDEEFLNRSVNEgFS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 231 GGWRMRVALARALFIRPFMLLLDEPTNHLDLDA------CVwleEELKTFKRILVLVSHSQDFLNGVCTNIIH 297
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLDIDAlkivaeGI---NRLREPDRSFLIITHYQRLLNYIKPDYVH 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
395-591 |
2.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.68 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----------RKHSHVK--I 462
Cdd:PRK13644 1 MIRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfSKLQGIRklV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQHLQEQL-------DLDLSPLEYmmkCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNP 535
Cdd:PRK13644 80 GIVFQNPETQFvgrtveeDLAFGPENL---CLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 536 HMLFLDEPTNHLDIETIDALADAINEF-EGGMMLV--SHDFRLIqQVAQEIWVCEKQTI 591
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVyiTHNLEEL-HDADRIIVMDRGKI 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
386-548 |
2.53e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.91 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 386 PPCGKIPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------- 455
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpara 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 456 KHSHVKIGRYHQHlqEQLDLDLSPLE----YMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLA 531
Cdd:PRK13536 110 RLARARIGVVPQF--DNLDLEFTVREnllvFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170
....*....|....*..
gi 27881506 532 WQNPHMLFLDEPTNHLD 548
Cdd:PRK13536 188 INDPQLLILDEPTTGLD 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
396-572 |
2.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIY---NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI------------------ 454
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkalDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 455 ------------RKHSHVK-----IGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGLTGKQ- 509
Cdd:PRK13651 83 vleklviqktrfKKIKKIKeirrrVGVVFQFAEYQLfeqtiekDIIFGPVSMGV---SKEEAKKRAAKYIELVGLDESYl 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 510 QVSPIrNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD----IETIDALaDAINEFEGGMMLVSHD 572
Cdd:PRK13651 160 QRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIF-DNLNKQGKTIILVTHD 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
86-302 |
2.91e-07 |
|
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: 51.51 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVP-IPEHIDIYHLTREMPpsdk 156
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdsGEVLFDgKPLDIAARNRIGYLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 157 tplhcvmevdTERAMLEKEAERlahedaecEKLMELyERLEELDADKAEMRASRILHGLGFTPaMQRKKLKDFSGGWRMR 236
Cdd:cd03269 77 ----------EERGLYPKMKVI--------DQLVYL-AQLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 237 VALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKK 302
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
201-286 |
4.58e-07 |
|
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: 52.41 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 201 ADKAEMRAS--RILHGLGFTPAMQRK--KLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDacvWLE- 268
Cdd:COG4148 105 APRAERRISfdEVVELLGIGHLLDRRpaTL---SGGERQRVAIGRALLSSPRLLLMDEPLAALDlarkaeiLP---YLEr 178
|
90 100
....*....|....*....|.
gi 27881506 269 --EELktfkRILVL-VSHSQD 286
Cdd:COG4148 179 lrDEL----DIPILyVSHSLD 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
398-572 |
4.59e-07 |
|
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: 50.98 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYTKDGpcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGR--------- 464
Cdd:cd03259 3 LKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPERrnigmvfqd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 465 Y----HQHLQEQLDLDLSpleymMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAwQNPHMLF 539
Cdd:cd03259 81 YalfpHLTVAENIAFGLK-----LRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALArALA-REPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881506 540 LDEPTNHLD----IETIDALADAINEFEGGMMLVSHD 572
Cdd:cd03259 154 LDEPLSALDaklrEELREELKELQRELGITTIYVTHD 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
396-572 |
4.75e-07 |
|
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: 50.93 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtKDGPCIYNNLEfGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRY 465
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALE-DISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 HQH--------LQEQLDLdlsPLEymMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAwQNPH 536
Cdd:cd03293 79 FQQdallpwltVLDNVAL---GLE--LQGVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALArALA-VDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881506 537 MLFLDEPTNHLDIET----IDALADAINEFEGGMMLVSHD 572
Cdd:cd03293 152 VLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
396-585 |
4.96e-07 |
|
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: 50.96 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtkDGPCIYNnlefGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQHLQE 471
Cdd:cd03261 1 IELRGLTKSF--GGRTVLK----GVDLDVRrgeiLAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-DISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 472 QLDL-------------DLS-------PL-EYMMKCYPEIKEKEEMRkiIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-W 529
Cdd:cd03261 74 RLRRrmgmlfqsgalfdSLTvfenvafPLrEHTRLSEEEIREIVLEK--LEAVGLRGAEDLYP-AELSGGMKKRVALArA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 530 LAwQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM--MLVSHDFRLIQQVAQEIWV 585
Cdd:cd03261 151 LA-LDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLtsIMVTHDLDTAFAIADRIAV 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
394-572 |
5.16e-07 |
|
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: 52.75 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGmirkhsHVKIGRYHQHLQEQL 473
Cdd:TIGR02868 333 PTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG------EVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 474 DL--------------DLSPLEYMMKCYPEIKEkEEMRKIIGRYGLTgkqqvSPIRNLSD---------------GQKCR 524
Cdd:TIGR02868 406 EVrrrvsvcaqdahlfDTTVRENLRLARPDATD-EELWAALERVGLA-----DWLRALPDgldtvlgeggarlsgGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881506 525 VCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHD 572
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
100-260 |
5.24e-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: 51.12 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 100 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKRevpIPEHIDIYH--LTREMPPSDKTPLHCVMEVDTERAMLE--KE 175
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGqiLFNGQPRKPDQFQKCVAYVRQDDILLPglTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 176 AERLAHedaeCEKLmelyeRLEEL--DADKAEMRASRILHGLGFTPAmQRKKLKDFSGGWRMRVALARALFIRPFMLLLD 253
Cdd:cd03234 99 RETLTY----TAIL-----RLPRKssDAIRKKRVEDVLLRDLALTRI-GGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
....*..
gi 27881506 254 EPTNHLD 260
Cdd:cd03234 169 EPTSGLD 175
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
101-306 |
5.58e-07 |
|
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: 50.99 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrevpipehidIYHLTREmppsdktplhcvmEVDTER---AMLEkeae 177
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG----------IYPPDSG-------------TVTVRGrvsSLLG---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 178 rLAHE-DAECEKLMELYERLEELDADKAEMRAsRILHGLGFT--PAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDE 254
Cdd:cd03220 91 -LGGGfNPELTGRENIYLNGRLLGLSRKEIDE-KIDEIIEFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 255 PTNHLDL---DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYY 306
Cdd:cd03220 169 VLAVGDAafqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
101-271 |
5.81e-07 |
|
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: 50.93 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPipEHIDIYHLTREM--PPSDKTPL---HCVMEVDTERAMLEKE 175
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP--TSGGVILEGKQItePGPDRMVVfqnYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 176 AERLAHEDAECEKLMELYERLEeldadkaemrasriLHGLGftpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEP 255
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIA--------------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170
....*....|....*.
gi 27881506 256 TNHLDLDACVWLEEEL 271
Cdd:TIGR01184 142 FGALDALTRGNLQEEL 157
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
87-284 |
5.89e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.91 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 87 HIINLSLTFHGQELLSDtkLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLtremPPSDKtPLhc 161
Cdd:COG3840 3 RLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqDLTAL----PPAER-PV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 162 vmevdterAMLEKEAERLAHedaeceklMELYE----------RLEELDADKAEMRASRI-LHGLGftpamQRK--KLkd 228
Cdd:COG3840 74 --------SMLFQENNLFPH--------LTVAQniglglrpglKLTAEQRAQVEQALERVgLAGLL-----DRLpgQL-- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 229 fSGGWRMRVALARALfIR--PfMLLLDEPTNHLD-------LDacvWLEEELKTFKRILVLVSHS 284
Cdd:COG3840 131 -SGGQRQRVALARCL-VRkrP-ILLLDEPFSALDpalrqemLD---LVDELCRERGLTVLMVTHD 189
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
426-585 |
6.24e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDlDLSPLEYMMKC--YPEIKEKEEMRKIIgRY 503
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLT-GIENIEFKMLCmgFKRKEIKAMTPKII-EF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 504 GLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHDFRLIQQVA 580
Cdd:PRK13546 131 SELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQFC 210
|
....*.
gi 27881506 581 QEI-WV 585
Cdd:PRK13546 211 TKIaWI 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
393-575 |
6.37e-07 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 50.81 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 393 PPVIMVQNVSFKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------- 454
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 455 --RKHshvKIG----RYH--QHL--QEQLDLdlsPLEYMMKCYPEIKEKeeMRKIIGRYGLTGKQQVSPiRNLSDGQKCR 524
Cdd:COG1136 82 rlRRR---HIGfvfqFFNllPELtaLENVAL---PLLLAGVSRKERRER--ARELLERVGLGDRLDHRP-SQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 525 VCLA-WLAwQNPHMLFLDEPTNHLDIET----IDALADAINEFEGGMMLVSHDFRL 575
Cdd:COG1136 153 VAIArALV-NRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
90-260 |
6.43e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIdiyhltrempPSDKTPLHCVMEvDTer 169
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------LAGTAPLAEARE-DT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 amlekeaeRLAHEDAEC---EKLMELY----------ERLEELDADKAEMRASRilhglgfTPAMqrkklkdFSGGWRMR 236
Cdd:PRK11247 84 --------RLMFQDARLlpwKKVIDNVglglkgqwrdAALQALAAVGLADRANE-------WPAA-------LSGGQKQR 141
|
170 180
....*....|....*....|....
gi 27881506 237 VALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALD 165
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
419-585 |
6.87e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 50.88 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR----------------------KHSH----------VKI 462
Cdd:COG4559 19 DVSLTLRpgelTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspwelarrravlpQHSSlafpftveevVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQHLQEQLDLDLsPLEYMMKCypeikekeemrkiigryGLTGKQQvspiRN---LSDGQKCRVCLAW-LA--WQNPH 536
Cdd:COG4559 99 GRAPHGSSAAQDRQI-VREALALV-----------------GLAHLAG----RSyqtLSGGEQQRVQLARvLAqlWEPVD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 537 M----LFLDEPTNHLDI-------ETIDALADAinefEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:COG4559 157 GgprwLFLDEPTSALDLahqhavlRLARQLARR----GGGVVAVLHDLNLAAQYADRILL 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
88-262 |
7.08e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.77 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsDKTPLHCV--MEV 165
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV----------AGDDVEALsaRAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 166 DTERAMLEKEAErLAHE-DAECEKLMELYERLEELD-ADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARAL 243
Cdd:PRK09536 76 SRRVASVPQDTS-LSFEfDVRQVVEMGRTPHRSRFDtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170
....*....|....*....
gi 27881506 244 FIRPFMLLLDEPTNHLDLD 262
Cdd:PRK09536 155 AQATPVLLLDEPTASLDIN 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
86-303 |
8.37e-07 |
|
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: 50.27 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-----IPEHIDIYHLT-REMPP-- 153
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtsgsvLVDGTDLTLLSgKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 154 -------------SDKTPLHCVMevdterAMLEkeaerLAHEDAEceklmELYERLEELD-----ADKAEMRASRIlhgl 215
Cdd:cd03258 82 rrigmifqhfnllSSRTVFENVA------LPLE-----IAGVPKA-----EIEERVLELLelvglEDKADAYPAQL---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 216 gftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACvwlEEELKTFKRI-------LVLVSHSQDFL 288
Cdd:cd03258 142 --------------SGGQKQRVGIARALANNPKVLLCDEATSALDPETT---QSILALLRDInrelgltIVLITHEMEVV 204
|
250
....*....|....*
gi 27881506 289 NGVCTNIIHMHNKKL 303
Cdd:cd03258 205 KRICDRVAVMEKGEV 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
403-603 |
1.13e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 403 FKYtKDGPCIYN-NLEFGIDLDTrvALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-------------KIGRYHQH 468
Cdd:PRK13638 9 FRY-QDEPVLKGlNLDFSLSPVT--GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 LQEQL---DLDlSPLEYMMKCYpEIKEKEEMRKIIGRYGLTGKQQV--SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEP 543
Cdd:PRK13638 86 PEQQIfytDID-SDIAFSLRNL-GVPEAEITRRVDEALTLVDAQHFrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 544 TNHLD-------IETIDALADAINEfeggMMLVSHDFRLIQQVAQEIWV-CEKQTITKW-PGDILAYKE 603
Cdd:PRK13638 164 TAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVlRQGQILTHGaPGEVFACTE 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
420-589 |
1.14e-06 |
|
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: 49.53 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 420 IDLDTRVAL-VGPNGAGKST-----------LLKLLTGELLPTDGMIRKHShvKIGRYHQHLQEQLDLD------LSPLE 481
Cdd:cd03240 18 IEFFSPLTLiVGQNGAGKTTiiealkyaltgELPPNSKGGAHDPKLIREGE--VRAQVKLAFENANGKKytitrsLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 482 YMMKCYpeikeKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAW-LAWQ-----NPHMLFLDEPTNHLDIETID-A 554
Cdd:cd03240 96 NVIFCH-----QGESNWPLLD----------MRGRCSGGEKVLASLIIrLALAetfgsNCGILALDEPTTNLDEENIEeS 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881506 555 LADAINEFEGG----MMLVSHDFRLIqQVAQEIWVCEKQ 589
Cdd:cd03240 161 LAEIIEERKSQknfqLIVITHDEELV-DAADHIYRVEKD 198
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
86-260 |
1.17e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.99 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-------------GKREVPIPEHiDIYHLTREM- 151
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlleepdsgtitvDGEDLTDSKK-DINKLRRKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 152 ---------PpsDKTPLHCVME----VdteRAMLEKEAERLAhedaeceklMELYERLEeLdADKAEMRASRIlhglgft 218
Cdd:COG1126 81 mvfqqfnlfP--HLTVLENVTLapikV---KKMSKAEAEERA---------MELLERVG-L-ADKADAYPAQL------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881506 219 pamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG1126 138 -----------SGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
83-283 |
1.21e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 83 STDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDKTPLHCV 162
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 MEVDTERAMLEKEAERLAhedaeceKLMELYERLEeldadkaemrASRILHGlgftpAMQRkklkdFSGGWRMRVALARA 242
Cdd:PRK09544 82 LPLTVNRFLRLRPGTKKE-------DILPALKRVQ----------AGHLIDA-----PMQK-----LSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881506 243 LFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSH 283
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSH 179
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
396-572 |
1.35e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.08 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTkDGPCIYN-NLEF---GIdldtrVALVGPNGAGKSTLLKLLTGELLPTDGMI----------------- 454
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDvSLTIpkgGI-----TALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvattpsrelak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 455 -----RKHSHVKI----------GRY-----------HQHLQEQLD-LDLSPLEymmkcypeikekeemrkiiGRYgltg 507
Cdd:COG4604 76 rlailRQENHINSrltvrelvafGRFpyskgrltaedREIIDEAIAyLDLEDLA-------------------DRY---- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 508 kqqvspIRNLSDGQKCRVCLAW-LAwQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHD 572
Cdd:COG4604 133 ------LDELSGGQRQRAFIAMvLA-QDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
228-302 |
1.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.43 E-value: 1.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 228 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLD---LDACVWLEEEL-KTFKRILVLVSHSQDFLNGVCTNIIHMHNKK 302
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
396-549 |
1.42e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.01 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGpcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGM-------IRKHSHVKIGRYHQH 468
Cdd:PRK11231 3 LRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 LQEQLdldLSPleymmkcypeikEKEEMRKII-----------GRYGLTGKQQVS--------------PIRNLSDGQKC 523
Cdd:PRK11231 81 LPQHH---LTP------------EGITVRELVaygrspwlslwGRLSAEDNARVNqameqtrinhladrRLTDLSGGQRQ 145
|
170 180
....*....|....*....|....*.
gi 27881506 524 RVCLAWLAWQNPHMLFLDEPTNHLDI 549
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
416-583 |
1.49e-06 |
|
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: 49.67 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 416 LEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigryhqhLQEQLDLDLSPLEYM---------MKC 486
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------------TVDGFDVVKEPAEARrrlgfvsdsTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 487 YPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSD-----------------GQKCRVCLAWLAWQNPHMLFLDEPTNHLDI 549
Cdd:cd03266 90 YDRLTARENLEYFAGLYGLKGDELTARLEELADrlgmeelldrrvggfstGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881506 550 ETIDALADAINEF--EGGMMLVS-HDFRLIQQVAQEI 583
Cdd:cd03266 170 MATRALREFIRQLraLGKCILFStHIMQEVERLCDRV 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
201-285 |
1.55e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 201 ADKAEMR-----ASRILHgLGftpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL---- 271
Cdd:PRK11000 105 AKKEEINqrvnqVAEVLQ-LA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIsrlh 180
|
90
....*....|....
gi 27881506 272 KTFKRILVLVSHSQ 285
Cdd:PRK11000 181 KRLGRTMIYVTHDQ 194
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
196-286 |
1.77e-06 |
|
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: 49.61 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 196 LEELDADKAEMRASRILHGLGFTPAMQRKKLKD-FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF 274
Cdd:cd03295 102 LLKWPKEKIRERADELLALVGLDPAEFADRYPHeLSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRL 181
|
90
....*....|....*.
gi 27881506 275 KRIL----VLVSHSQD 286
Cdd:cd03295 182 QQELgktiVFVTHDID 197
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
98-261 |
1.86e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 98 QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREM--------------PPSDKTP 158
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgePLAKLNRAQrkafrrdiqmvfqdSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 159 LHCVmevdteRAMLekeAERLAHedaeceklmelyerLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVA 238
Cdd:PRK10419 105 RKTV------REII---REPLRH--------------LLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180
....*....|....*....|...
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDL 261
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDL 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
223-284 |
2.03e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 2.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 223 RKKLKDF----SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHS 284
Cdd:PRK14267 140 KDRLNDYpsnlSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHS 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
90-255 |
2.04e-06 |
|
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: 49.08 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-----IPEHIDIYHLtremppsdktPLHcvme 164
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdsgkiLLDGQDITKL----------PMH---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 165 vdtERA-----MLEKEA---ERLAHED---AECEKLMELY-ERLEELDADKAEMRASRILHGLGFTpamqrkklkdFSGG 232
Cdd:cd03218 71 ---KRArlgigYLPQEAsifRKLTVEEnilAVLEIRGLSKkEREEKLEELLEEFHITHLRKSKASS----------LSGG 137
|
170 180
....*....|....*....|...
gi 27881506 233 WRMRVALARALFIRPFMLLLDEP 255
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEP 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
389-548 |
2.19e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.80 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 389 GKIPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR----------KHS 458
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 459 HVKIGRYHQHlqEQLDLDLSPLEYMMkcypeikekeemrkIIGRY-GLTGKQ-----------------QVSPIRNLSDG 520
Cdd:PRK13537 79 RQRVGVVPQF--DNLDPDFTVRENLL--------------VFGRYfGLSAAAaralvppllefaklenkADAKVGELSGG 142
|
170 180
....*....|....*....|....*...
gi 27881506 521 QKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
396-548 |
2.19e-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: 51.06 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLpTDGMI---------------RKHSHV 460
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIqidgvswnsvtlqtwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 ---KIGRYHQHLQEQLDldlsPLEYMmkcypeikEKEEMRKIIGRYGLTGKQQVSPIR----------NLSDGQKCRVCL 527
Cdd:TIGR01271 1297 ipqKVFIFSGTFRKNLD----PYEQW--------SDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyVLSNGHKQLMCL 1364
|
170 180
....*....|....*....|.
gi 27881506 528 AWLAWQNPHMLFLDEPTNHLD 548
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLD 1385
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
517-585 |
2.25e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 2.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 517 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
95-283 |
2.29e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 48.38 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 95 FHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI---------------GKREVPIPEHIdiyHLTREMPpsdKTPL 159
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagvlrptsgtvrragGARVAYVPQRS---EVPDSLP---LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 160 HCV-MEVDTERAMLEkeaeRLAHEDaeceklmelyerleeldadkaEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVA 238
Cdd:NF040873 76 DLVaMGRWARRGLWR----RLTRDD---------------------RAAVDDALERVGLA-DLAGRQLGELSGGQRQRAL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881506 239 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF---KRILVLVSH 283
Cdd:NF040873 130 LAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
89-325 |
2.45e-06 |
|
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: 48.94 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 89 INLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSDKTPLHCV 162
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqDVSDLRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 163 MEvDT---------ERAMLEKEAERLAHEDAEcEKLMELYERLEeLDADKAEMrasrilhglgftpAMQrkklkdFSGGW 233
Cdd:cd03292 84 FQ-DFrllpdrnvyENVAFALEVTGVPPREIR-KRVPAALELVG-LSHKHRAL-------------PAE------LSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 234 RMRVALARALFIRPFMLLLDEPTNHLDLDacvwleeelkTFKRILVLVSHSQDflNGVcTNIIHMHNKKLkyytgnYDQY 313
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPD----------TTWEIMNLLKKINK--AGT-TVVVATHAKEL------VDTT 202
|
250
....*....|..
gi 27881506 314 VKTRLELEENQM 325
Cdd:cd03292 203 RHRVIALERGKL 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-594 |
2.47e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 408 DGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-----------------KIGRYHQHLQ 470
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidaiklrkEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 471 EQLDLDL-SPLEYMMKCYpEIKEKEEMRKI-------IGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDE 542
Cdd:PRK14246 101 PFPHLSIyDNIAYPLKSH-GIKEKREIKKIveeclrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881506 543 PTNHLDIETIDALADAINEF--EGGMMLVSHDFRLIQQVAQEIWVCEKQTITKW 594
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
396-571 |
2.49e-06 |
|
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: 47.92 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFkYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTL--------LKLLTGELLPTDG---MIRKHSHVKIGR 464
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLfralaglwPWGSGRIGMPEGEdllFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 465 yhqhLQEQLdldlspleymmkCYPEIKEkeemrkiigrygltgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPT 544
Cdd:cd03223 80 ----LREQL------------IYPWDDV------------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180
....*....|....*....|....*..
gi 27881506 545 NHLDIETIDALADAINEFEGGMMLVSH 571
Cdd:cd03223 120 SALDEESEDRLYQLLKELGITVISVGH 146
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
230-304 |
2.83e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDL----DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLK 304
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
229-283 |
3.33e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 3.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLD--ACVW-----LEEELKTfkrILVLVSH 283
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSvqAQVLnlmmdLQQELGL---SYVFISH 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
101-286 |
3.92e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.96 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLT-------REMPPSDKTpLHCVMEVDTERAMLE 173
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqKEIKPVRKK-VGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 174 KEAERLAHEDaecEKLMELYERLEELDADKAEMrasrilhgLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLD 253
Cdd:PRK13643 101 TVLKDVAFGP---QNFGIPKEKAEKIAAEKLEM--------VGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881506 254 EPTNHLDLDACVwleEELKTFKRI------LVLVSHSQD 286
Cdd:PRK13643 170 EPTAGLDPKARI---EMMQLFESIhqsgqtVVLVTHLMD 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
514-557 |
4.03e-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: 4.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 27881506 514 IRNLSDGQKCRVCLAW-LAWqNPHMLFLDEPTNHLD-------IETIDALAD 557
Cdd:cd03213 109 LRGLSGGERKRVSIALeLVS-NPSLLFLDEPTSGLDsssalqvMSLLRRLAD 159
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
225-260 |
4.27e-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: 47.55 E-value: 4.27e-06
10 20 30
....*....|....*....|....*....|....*.
gi 27881506 225 KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:cd03213 108 KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
340-438 |
4.82e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.39 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 340 NYIARFGHGSAKLARQAQSkektLQKMMASglTERVVS--DKTLSFYFPPCGKIPPPV---IMVQNVSFKYTKDGPcIYN 414
Cdd:COG1132 285 LYLLRLFGPLRQLANVLNQ----LQRALAS--AERIFEllDEPPEIPDPPGAVPLPPVrgeIEFENVSFSYPGDRP-VLK 357
|
90 100
....*....|....*....|....
gi 27881506 415 NLEFGIDLDTRVALVGPNGAGKST 438
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKST 381
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
202-304 |
4.89e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 202 DKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwLEEELKTFKRI---- 277
Cdd:PRK13634 119 EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG---RKEMMEMFYKLhkek 195
|
90 100 110
....*....|....*....|....*....|
gi 27881506 278 ---LVLVSHSQDFLNGVCTNIIHMHNKKLK 304
Cdd:PRK13634 196 gltTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
101-306 |
4.96e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.15 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrevpipehidIYHLTREmppsdktplhcvmEVDTE---RAMLEkeae 177
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG----------ILEPTSG-------------RVEVNgrvSALLE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 178 rLA---HedaeceklMELYERleeldaDKAEMRAsRILhglGFTPAMQRKKLK---DFSG--------------GWRMRV 237
Cdd:COG1134 95 -LGagfH--------PELTGR------ENIYLNG-RLL---GLSRKEIDEKFDeivEFAElgdfidqpvktyssGMRARL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 238 ALARALFIRPFMLLLDEptnhldldacvWL-----------EEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:COG1134 156 AFAVATAVDPDILLVDE-----------VLavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
...
gi 27881506 304 KYY 306
Cdd:COG1134 225 VMD 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
427-583 |
5.27e-06 |
|
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: 47.75 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 427 ALVGPNGAGKSTLLKLLTGELLPTDG--MIRKHSHVK--------IGRYHQHLqeQLDLDLSPLEYM-----MKCYPEIK 491
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPTSGraTVAGHDVVReprevrrrIGIVFQDL--SVDDELTGWENLyiharLYGVPGAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 492 EKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM--M 567
Cdd:cd03265 108 RRERIDELLDFVGLLEAAD-RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeEFGMtiL 186
|
170
....*....|....*.
gi 27881506 568 LVSHDFRLIQQVAQEI 583
Cdd:cd03265 187 LTTHYMEEAEQLCDRV 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
90-260 |
5.39e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKReVPiPEHIDIyHLtremppsDKTPlhcVMEVDTER 169
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF-VP-YQHGSI-TL-------DGKP---VEGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 AMLEKEAERLAHEDAECEKLMELyeRLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRPFM 249
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGL--QLAGVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIARALAANPQL 149
|
170
....*....|.
gi 27881506 250 LLLDEPTNHLD 260
Cdd:PRK11248 150 LLLDEPFGALD 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
394-583 |
5.54e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYtKDGPC---IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG------------------ 452
Cdd:PRK11629 4 ILLQCDNLCKRY-QEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 453 MIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAW 532
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 533 QNPHMLFLDEPTNHLDIETIDALADAINEFE----GGMMLVSHDFRLIQQVAQEI 583
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQL 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
414-590 |
5.55e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 414 NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTD---------------------GMIRKHSHVKIGR-------- 464
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGgtillrgqhieglpghqiarmGVVRTFQHVRLFRemtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 465 ---YHQHLQEQLdldLSPLeYMMKCYPEiKEKEEMRKI---IGRYGLTgkqQVS--PIRNLSDGQKCRVCLAWLAWQNPH 536
Cdd:PRK11300 102 lvaQHQQLKTGL---FSGL-LKTPAFRR-AESEALDRAatwLERVGLL---EHAnrQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 537 MLFLDEPTNHLD-IETID--ALADAI-NEFEGGMMLVSHDFRLIQQVAQEIWVCEKQT 590
Cdd:PRK11300 174 ILMLDEPAAGLNpKETKEldELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
195-260 |
5.94e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.32 E-value: 5.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 195 RLEELDADKAEMRASRILHGLGFTPAmQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG4525 102 RLRGVPKAERRARAEELLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
86-283 |
6.10e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPE---------------HIDIYHLTRE 150
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEarvsgevyldgqdifKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 151 MPPSDKTPLHCVMEVDTERAMLEKEAERLAHEDAEC-EKLMELYERLEELDADKAEMRAsrilhglgftPAMQrkklkdF 229
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELqERVRWALEKAQLWDEVKDRLDA----------PAGK------L 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSH 283
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
90-264 |
7.97e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.18 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GkrevpipehidiyhLTRemppsdktPLHCVMEVDTE 168
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIaG--------------LLP--------PAAGTIKLDGG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 169 RAMLEKEAER---LAHEDAeCEKLMELYERLE---------ELDADKAemrASRI-LHGLGFTPAmqrkklKDFSGGWRM 235
Cdd:PRK13539 65 DIDDPDVAEAchyLGHRNA-MKPALTVAENLEfwaaflggeELDIAAA---LEAVgLAPLAHLPF------GYLSAGQKR 134
|
170 180 190
....*....|....*....|....*....|
gi 27881506 236 RVALARAL-FIRPfMLLLDEPTNHLDLDAC 264
Cdd:PRK13539 135 RVALARLLvSNRP-IWILDEPTAALDAAAV 163
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
419-592 |
8.06e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.39 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDG-MIRKHSHVKIGRYHQHL--QE------QLDL--DLSPLEYM 483
Cdd:PRK09493 19 NIDLNIDqgevVVIIGPSGSGKSTLLRCINKLEEITSGdLIVDGLKVNDPKVDERLirQEagmvfqQFYLfpHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 484 MkcYPEIK----EKEEMRKI----IGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIE----- 550
Cdd:PRK09493 99 M--FGPLRvrgaSKEEAEKQarelLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhev 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881506 551 --TIDALADainefEG-GMMLVSHDFRLIQQVAQEIWVCEKQTIT 592
Cdd:PRK09493 176 lkVMQDLAE-----EGmTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
396-592 |
8.60e-06 |
|
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: 46.54 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLltgellptdgmirkhshvkIGRYHQHLQEQLDL 475
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQL-------------------LTGDLKPQQGEITL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 476 DLSPLEymmkcypeiKEKEEMRKIIGRYgltgKQQV----SPIRN-----LSDGQKCRVCLAWLAWQNPHMLFLDEPTNH 546
Cdd:cd03247 62 DGVPVS---------DLEKALSSLISVL----NQRPylfdTTLRNnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881506 547 LDIETIDALADAINEF--EGGMMLVSHDFRLIQQVaQEIWVCEKQTIT 592
Cdd:cd03247 129 LDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
218-322 |
8.97e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 218 TPAMQrkklkdFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHSQDFLNGVCTNI 295
Cdd:PRK14246 149 SPASQ------LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
90 100
....*....|....*....|....*..
gi 27881506 296 IHMHNKKLKYYTGNYDQYVKTRLELEE 322
Cdd:PRK14246 223 AFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
396-600 |
9.45e-06 |
|
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: 47.30 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----------------RKHSH 459
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpvelrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 460 V--KIGRY-HQHLQEQLDLDLSPLEymmkcYPEIKEKEEMRKIIGRYGLTGKQ--QVSPiRNLSDGQKCRVCLAWLAWQN 534
Cdd:cd03295 80 ViqQIGLFpHMTVEENIALVPKLLK-----WPKEKIRERADELLALVGLDPAEfaDRYP-HELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 535 PHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHD----FRLiqqvAQEIWVCEKQTITKW--PGDILA 600
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDideaFRL----ADRIAIMKNGEIVQVgtPDEILR 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
230-260 |
9.85e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 9.85e-06
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
48-283 |
1.08e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.90 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 48 RETTEVDLLTKELEDFEMKKAAARAVTGVLASHPNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKS-- 125
Cdd:PRK13536 4 RAVAEEAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSti 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 126 --MLLSAIGKRE-------VPIPEHIdiyHLTRE----MPPSDKTPLHCVMEvdtERAMLEKEAERLAHEDAEC--EKLM 190
Cdd:PRK13536 84 arMILGMTSPDAgkitvlgVPVPARA---RLARArigvVPQFDNLDLEFTVR---ENLLVFGRYFGMSTREIEAviPSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 191 ElYERLEeldaDKAEMRASrilhglgftpamqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEE 270
Cdd:PRK13536 158 E-FARLE----SKADARVS------------------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER 214
|
250
....*....|....*..
gi 27881506 271 LKTF----KRILvLVSH 283
Cdd:PRK13536 215 LRSLlargKTIL-LTTH 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
395-613 |
1.08e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.49 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLP---------TDGMIRKHSHV----- 460
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGITLTAKTVwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 KIGRYHQHLQEQL-------DLDLSpLEYmmKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQ 533
Cdd:PRK13640 85 KVGIVFQNPDNQFvgatvgdDVAFG-LEN--RAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 534 NPHMLFLDEPTNHLDIE------------------TIDALADAINEFEGG-MMLVSHDFRLIQQvAQEIWVCEKQTITKW 594
Cdd:PRK13640 161 EPKIIILDESTSMLDPAgkeqilklirklkkknnlTVISITHDIDEANMAdQVLVLDDGKLLAQ-GSPVEIFSKVEMLKE 239
|
250
....*....|....*....
gi 27881506 595 PGDILAYKEHLKSKLVDEE 613
Cdd:PRK13640 240 IGLDIPFVYKLKNKLKEKG 258
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
202-261 |
1.13e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.12 E-value: 1.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 202 DKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL 261
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
393-583 |
1.20e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 393 PPVIMVQNVSFKYtkdGPCIYNNlefGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR--------KHSHV 460
Cdd:COG3845 3 PPALELRGITKRF---GGVVAND---DVSLTVRpgeiHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvriRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 ----KIGRYHQHLQ--------EQLDLDLSPLEYM---MKcypeiKEKEEMRKIIGRYGLtgkqQVSP---IRNLSDGQK 522
Cdd:COG3845 77 aialGIGMVHQHFMlvpnltvaENIVLGLEPTKGGrldRK-----AARARIRELSERYGL----DVDPdakVEDLSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 523 CRV----CLawlaWQNPHMLFLDEPTNHLDIETIDALADAINEF--EG-GMMLVSHDFRLIQQVAQEI 583
Cdd:COG3845 148 QRVeilkAL----YRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKLREVMAIADRV 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
90-300 |
1.21e-05 |
|
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: 47.34 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHiDIYHL-------- 147
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItgfyrptsgrilfdGRDITGLPPH-RIARLgiartfqn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 148 TREMPpsDKTPLHCVM-----------EVDTERAMLEKEAERLAHEDAeceklMELyerLEELD-ADKAEMRASRILHGl 215
Cdd:COG0411 88 PRLFP--ELTVLENVLvaaharlgrglLAALLRLPRARREEREARERA-----EEL---LERVGlADRADEPAGNLSYG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 216 gftpamQRKklkdfsggwrmRVALARALFIRPFMLLLDEPT---NHLDLDACVWLEEELKTFKRI-LVLVSHSQDFLNGV 291
Cdd:COG0411 157 ------QQR-----------RLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGItILLIEHDMDLVMGL 219
|
....*....
gi 27881506 292 CTNIIHMHN 300
Cdd:COG0411 220 ADRIVVLDF 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
396-618 |
1.28e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.43 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLeFGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR---------------K 456
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRAL-FDVNLTIEdgsyTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 457 HSHVKIGRYHQHLQEQL-------DLDLSPLEYmmkcypEIKEKEEMRKIIGRYGLTGKQQVSPIRN---LSDGQKCRVC 526
Cdd:PRK13649 82 QIRKKVGLVFQFPESQLfeetvlkDVAFGPQNF------GVSQEEAEALAREKLALVGISESLFEKNpfeLSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 527 LAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEIWVCEKQTITK--WPGDILAY 601
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMtiVLVTHLMDDVANYADFVYVLEKGKLVLsgKPKDIFQD 235
|
250
....*....|....*..
gi 27881506 602 KEHLKSKLVDeEPQLTK 618
Cdd:PRK13649 236 VDFLEEKQLG-VPKITK 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
90-260 |
1.37e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIdIYHlTREMPPSDktpLHCVMEvdTER 169
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYR-MRDGQLRD---LYALSE--AER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 AMLEKEAERLAHEDAE-------------CEKLMEL----YERLEELDAD---KAEMRASRIlhglgftpamqrkklkD- 228
Cdd:PRK11701 84 RRLLRTEWGFVHQHPRdglrmqvsaggniGERLMAVgarhYGDIRATAGDwleRVEIDAARI----------------Dd 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881506 229 ----FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK11701 148 lpttFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
116-289 |
1.38e-05 |
|
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: 46.45 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 116 LIGLNGIGKSMLLSAIgkrevpipehidIYHLTREMPPSDKTPLHC--VMEVDTERAMLEKEAERLAHEDAECEKLMELY 193
Cdd:cd03240 27 IVGQNGAGKTTIIEAL------------KYALTGELPPNSKGGAHDpkLIREGEVRAQVKLAFENANGKKYTITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 194 E-----RLEELDADKAEMRASrilhglgftpamqrkklkdFSGGWRM------RVALARALFIRPFMLLLDEPTNHLDLD 262
Cdd:cd03240 95 EnvifcHQGESNWPLLDMRGR-------------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180 190
....*....|....*....|....*....|..
gi 27881506 263 ACVW-----LEEELKTFKRILVLVSHSQDFLN 289
Cdd:cd03240 156 NIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
90-284 |
1.42e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.08 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPE-----------HiDIYHltremPPSDktp 158
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEvtitgsivyngH-NIYS-----PRTD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 159 lhcVMEVDTERAMLEKEAERLAhedaeceklMELYE------RLEELDaDKAEMRAS--RILHGlgftpAMQRKKLKD-- 228
Cdd:PRK14239 81 ---TVDLRKEIGMVFQQPNPFP---------MSIYEnvvyglRLKGIK-DKQVLDEAveKSLKG-----ASIWDEVKDrl 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881506 229 ------FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHS 284
Cdd:PRK14239 143 hdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRS 206
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
396-562 |
1.48e-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: 46.33 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHShVKIGRYHQH-LQEQLD 474
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG-VDISKIGLHdLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 475 L--------------DLSPLEYmmkcYPEikekEEMRKIIGRYGLTGKQQVSPIR----------NLSDGQKCRVCLAWL 530
Cdd:cd03244 82 IipqdpvlfsgtirsNLDPFGE----YSD----EELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARA 153
|
170 180 190
....*....|....*....|....*....|..
gi 27881506 531 AWQNPHMLFLDEPTNHLDIETIDALADAINEF 562
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
399-561 |
1.84e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.65 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 399 QNVSFKYTKDGPCIYNnLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPT------DGM-IRKhshVKIGRYHQHL-- 469
Cdd:PRK13657 338 DDVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQsgriliDGTdIRT---VTRASLRRNIav 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 470 --QEQLDLDLSPLEYMMKCYPEIKEkEEMRK--------------------IIGRYGltgkqqvspiRNLSDGQKCRVCL 527
Cdd:PRK13657 414 vfQDAGLFNRSIEDNIRVGRPDATD-EEMRAaaeraqahdfierkpdgydtVVGERG----------RQLSGGERQRLAI 482
|
170 180 190
....*....|....*....|....*....|....
gi 27881506 528 AWLAWQNPHMLFLDEPTNHLDIETIDALADAINE 561
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
80-286 |
1.90e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.51 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 80 HPNSTDVHIINLSLTFHGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPS--- 154
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQL----------------LTRAWDPQqge 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 155 ---DKTPLHCVMEvDTERAMLE-------------KEAERLAHEDAECEKLMELYER--LEELDADKAEMRA-----SRI 211
Cdd:PRK11160 397 illNGQPIADYSE-AALRQAISvvsqrvhlfsatlRDNLLLAAPNASDEALIEVLQQvgLEKLLEDDKGLNAwlgegGRQ 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 212 LhglgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDacvwleeelkTFKRIL-VLVSHSQD 286
Cdd:PRK11160 476 L-----------------SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE----------TERQILeLLAEHAQN 524
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
84-319 |
1.91e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.54 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 84 TDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTrEMPPSDKTPlHCVM 163
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR----------------HLS-GLITGDKSA-GSHI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 164 EV---DTERA-MLEKEAERLAHEDAECEKLMELYERLEELD--------------------ADKAEMRASRILHGLGFTP 219
Cdd:PRK09984 65 ELlgrTVQREgRLARDIRKSRANTGYIFQQFNLVNRLSVLEnvligalgstpfwrtcfswfTREQKQRALQALTRVGMVH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 220 -AMQRkkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVS-HSQDFLNGVCTN 294
Cdd:PRK09984 145 fAHQR--VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgITVVVTlHQVDYALRYCER 222
|
250 260
....*....|....*....|....*
gi 27881506 295 IIHMHNKKLkYYTGNYDQYVKTRLE 319
Cdd:PRK09984 223 IVALRQGHV-FYDGSSQQFDNERFD 246
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
392-578 |
2.15e-05 |
|
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: 46.27 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKY-TKDGP-CIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV--------- 460
Cdd:COG4181 5 SAPIIELRGLTKTVgTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 ------KIGRYHQhlQEQLDLDLSPLEYMMkcYP-EIKE----KEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAW 529
Cdd:COG4181 85 arlrarHVGFVFQ--SFQLLPTLTALENVM--LPlELAGrrdaRARARALLERVGLGHRLDHYP-AQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881506 530 LAWQNPHMLFLDEPTNHLDIETIDALAD---AINEfEGG--MMLVSHDFRLIQQ 578
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDllfELNR-ERGttLVLVTHDPALAAR 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
229-305 |
2.17e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 45.22 E-value: 2.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLngvctniiHMHNKKLKY 305
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLW--------KFHDRVLDL 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
202-285 |
2.40e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.99 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 202 DKAEM--RASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEP-TNhldLDAC--VWLEEELKTFKR 276
Cdd:COG3839 106 PKAEIdrRVREAAELLGLEDLLDRKP-KQLSGGQRQRVALGRALVREPKVFLLDEPlSN---LDAKlrVEMRAEIKRLHR 181
|
90
....*....|...
gi 27881506 277 IL----VLVSHSQ 285
Cdd:COG3839 182 RLgtttIYVTHDQ 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
86-284 |
2.53e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKR-----EVPIP------------EHIDIYHLT 148
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEgrveffnqniyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 149 REM----PPSDKTPLHCVMEVdteramlekeaerlahedAECEKLMELYERLEELDADKAEMRAS----RILHGLgftpa 220
Cdd:PRK14258 88 RQVsmvhPKPNLFPMSVYDNV------------------AYGVKIVGWRPKLEIDDIVESALKDAdlwdEIKHKI----- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 221 mqRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK----RILVLVSHS 284
Cdd:PRK14258 145 --HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
515-585 |
2.57e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 47.10 E-value: 2.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 515 RNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETI----DALADAINEFEGGMMLVSHDFRLIQQVAQE-IWV 585
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKaIWL 242
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
97-260 |
2.84e-05 |
|
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: 45.94 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 97 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEH--IDIYHLTREMPPSDKTPLHCVMEVDT--ERAML 172
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlVDGHDLALADPAWLRRQVGVVLQENVlfNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 173 EKEAerLAHEDAECEKLMELyERLEELDADKAEMRasrilhgLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLL 252
Cdd:cd03252 94 DNIA--LADPGMSMERVIEA-AKLAGAHDFISELP-------EGYD-TIVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
....*...
gi 27881506 253 DEPTNHLD 260
Cdd:cd03252 163 DEATSALD 170
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
90-286 |
2.96e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQELLSDtkLELNSGRRYGLIGLNGIGKSMLLSAIGKreVPIPEHIDIY-----HltREMPPSdKTPLhcvme 164
Cdd:PRK10771 6 DITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAG--FLTPASGSLTlngqdH--TTTPPS-RRPV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 165 vdterAMLEKEAERLAHEDAECEKLMELYERLEELDADKAEMRAsrILHGLGFTPAMQRKKlKDFSGGWRMRVALARALF 244
Cdd:PRK10771 74 -----SMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHA--IARQMGIEDLLARLP-GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881506 245 IRPFMLLLDEPTNHLD---------LDACVWLEEELKtfkriLVLVSHSQD 286
Cdd:PRK10771 146 REQPILLLDEPFSALDpalrqemltLVSQVCQERQLT-----LLMVSHSLE 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
517-575 |
3.05e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.54 E-value: 3.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 517 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDFRL 575
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQL 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
189-260 |
3.09e-05 |
|
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: 46.20 E-value: 3.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 189 LMELYERLEELDADKAEMRASRILHGLGFTPAMQRkkLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG0444 109 IAEPLRIHGGLSKAEARERAIELLERVGLPDPERR--LDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
88-260 |
3.13e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSML-LSAIgkREVPIPEHI----DIYHLTREMPPSDKTP 158
Cdd:PRK15134 8 IENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTaLSIL--RLLPSPPVVypsgDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 159 LHCVMevDTERAMLEKEAERLAHEDAECEKlmELYERLE-----ELDADKAEMraSRILHGLGFTPAMQRkkLKDF---- 229
Cdd:PRK15134 86 LRGVR--GNKIAMIFQEPMVSLNPLHTLEK--QLYEVLSlhrgmRREAARGEI--LNCLDRVGIRQAAKR--LTDYphql 157
|
170 180 190
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
396-591 |
3.28e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.78 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKdgpciyNNLEFGIDL-----DTRVaLVGPNGAGKSTLLKLLTGELLPTDGMI---------RKHSHVK 461
Cdd:PRK11124 3 IQLNGINCFYGA------HQALFDITLdcpqgETLV-LLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 462 IGR------------YH--QHLQEQLDLdlspLEYMMKCYPEIKE--KEEMRKIIGRYGLTGKQQVSPIrNLSDGQKCRV 525
Cdd:PRK11124 76 AIRelrrnvgmvfqqYNlwPHLTVQQNL----IEAPCRVLGLSKDqaLARAEKLLERLRLKPYADRFPL-HLSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 526 CLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEIWVCEKQTI 591
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaETGItqVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
426-585 |
3.55e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDGMIrkHSHVKIGRYHQHLQEqlDLDLSPLEYMMKCYPEI----KEKEEmrkIIG 501
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISP--DYDGTVEEFLRSANTDDfgssYYKTE---IIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 502 RYGLTgKQQVSPIRNLSDGQKCRV----CLAwlawQNPHMLFLDEPTNHLDIETIDALADAINEF----EGGMMLVSHDF 573
Cdd:COG1245 442 PLGLE-KLLDKNVKDLSGGELQRVaiaaCLS----RDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDI 516
|
170
....*....|..
gi 27881506 574 RLIQQVAQEIWV 585
Cdd:COG1245 517 YLIDYISDRLMV 528
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
413-571 |
3.65e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.34 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 413 YNNLEFGIDLDT----RVALVGPNGAGKSTLLKLLTGELLPTDGMIR----KHSHVKIGRY-------------HQHLQE 471
Cdd:PRK10771 11 YHHLPMRFDLTVergeRVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqDHTTTPPSRRpvsmlfqennlfsHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 472 QLDLDLSPleyMMKCYPEikEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAWQNPhMLFLDEPTNHLD-- 548
Cdd:PRK10771 91 NIGLGLNP---GLKLNAA--QREKLHAIARQMGIEDLLARLP-GQLSGGQRQRVALArCLVREQP-ILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*
gi 27881506 549 --IETIDALADAINEFEGGMMLVSH 571
Cdd:PRK10771 164 lrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
223-283 |
3.72e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 3.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 223 RKKLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSH 283
Cdd:PRK14243 142 KDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTH 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
390-578 |
3.91e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.74 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 390 KIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKhSHVKIGRYHQ-- 467
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIADYSEaa 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 468 ------------H-----LQEQLDLDLspleymmkcyPEIKEkEEMRKIIGRYGLtGK--QQVSPI--------RNLSDG 520
Cdd:PRK11160 412 lrqaisvvsqrvHlfsatLRDNLLLAA----------PNASD-EALIEVLQQVGL-EKllEDDKGLnawlgeggRQLSGG 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 521 QKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQ 578
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNktVLMITHRLTGLEQ 539
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
409-570 |
3.93e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 409 GPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhLQEQLDLDLSPLEYM----- 483
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-------------LDGGDIDDPDVAEAChylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 484 ---MKcyPEIKEKEEM---RKIIG-----------RYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNH 546
Cdd:PRK13539 81 rnaMK--PALTVAENLefwAAFLGgeeldiaaaleAVGLAPLAHL-PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 27881506 547 LDIETIDALADAINEF--EGGMMLVS 570
Cdd:PRK13539 158 LDAAAVALFAELIRAHlaQGGIVIAA 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
425-579 |
4.11e-05 |
|
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: 45.22 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 425 RVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVK--IGryhqhLQEQLDLDLSPLEY-MMKC------YPEIKEKEE 495
Cdd:cd03220 50 RIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSslLG-----LGGGFNPELTGRENiYLNGrllglsRKEIDEKID 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 496 mrKIIGRYGLtGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGGMM--LVSHD 572
Cdd:cd03220 125 --EIIEFSEL-GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlKQGKTviLVSHD 201
|
....*..
gi 27881506 573 FRLIQQV 579
Cdd:cd03220 202 PSSIKRL 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
205-283 |
4.18e-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: 45.71 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 205 EMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL----KTFKRILVL 280
Cdd:cd03294 138 EERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELlrlqAELQKTIVF 216
|
...
gi 27881506 281 VSH 283
Cdd:cd03294 217 ITH 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
195-260 |
4.90e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 4.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 195 RLEELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
99-305 |
5.41e-05 |
|
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: 45.02 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 99 ELLSDTKLELNSGRRYGLIGLNGIGKSM---LLSAI-----GKREVP--IPEHIDIYHLTR-------------EMPPSD 155
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLlqptsGEVRVAglVPWKRRKKFLRRigvvfgqktqlwwDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 156 KTPLHcvmevdteRAMLEKEAERLAHEDAECEKLMELyerleeldadkaemraSRILHglgfTPAMQrkklkdFSGGWRM 235
Cdd:cd03267 115 SFYLL--------AAIYDLPPARFKKRLDELSELLDL----------------EELLD----TPVRQ------LSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 236 RVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEELKTFKRILV--------LVSHSQDFLNGVCTNIIHMHNKKLKY 305
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVA----QENIRNFLKEYNrergttvlLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
90-260 |
5.86e-05 |
|
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: 44.23 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 90 NLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPSDKTplhcvmevdt 167
Cdd:cd03247 5 NVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL----------------TGDLKPQQGE---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 168 eraMLEKEAERLAHEDAECEKLMELYERleeldadkAEMRASRILHGLGftpamqrkklKDFSGGWRMRVALARALFIRP 247
Cdd:cd03247 59 ---ITLDGVPVSDLEKALSSLISVLNQR--------PYLFDTTLRNNLG----------RRFSGGERQRLALARILLQDA 117
|
170
....*....|...
gi 27881506 248 FMLLLDEPTNHLD 260
Cdd:cd03247 118 PIVLLDEPTVGLD 130
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
229-260 |
6.35e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.49 E-value: 6.35e-05
10 20 30
....*....|....*....|....*....|..
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
419-585 |
6.45e-05 |
|
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: 43.57 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHshvkiGRYHQHlqeqldldLSPleymmkcypeikeKE 494
Cdd:cd03216 18 GVSLSVRrgevHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GKEVSF--------ASP-------------RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 495 EMRKIIGR-YGLTG--KQQVSPIRNLSdgqkcrvclawlawQNPHMLFLDEPTNHLDIETIDALADAINEF--EG-GMML 568
Cdd:cd03216 72 ARRAGIAMvYQLSVgeRQMVEIARALA--------------RNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIF 137
|
170
....*....|....*..
gi 27881506 569 VSHDFRLIQQVAQEIWV 585
Cdd:cd03216 138 ISHRLDEVFEIADRVTV 154
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
79-261 |
6.88e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.78 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 79 SHPNSTDVHII--NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-------------- 142
Cdd:PRK10575 3 EYTNHSDTTFAlrNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsska 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 143 ---DIYHLTREMPPSDKTplhCVME-VDTERAMLEKEAERLAHEDaeceklmelYERLEEldadkaemrasrILHGLGFT 218
Cdd:PRK10575 83 farKVAYLPQQLPAAEGM---TVRElVAIGRYPWHGALGRFGAAD---------REKVEE------------AISLVGLK 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881506 219 PAMQRkkLKD-FSGGWRMRVALARALFIRPFMLLLDEPTNHLDL 261
Cdd:PRK10575 139 PLAHR--LVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
230-283 |
7.06e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.87 E-value: 7.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLdACVWLEEELKTFK-RILVLVSH 283
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDA-ECEQLLQESRSRAsRTVLLIAH 672
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
516-585 |
7.27e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.63 E-value: 7.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 516 NLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADA-----INEFEGGMMLVSHDfrlIQQVAQEIWV 585
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHK---LQYLPHADWI 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
101-303 |
7.70e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.82 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMppSDKTplhcVMEVDTERAMLEKEAER 178
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagYHITPET--GNKN----LKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 179 LAHEDAECEKLMELYERLEELDaDKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNH 258
Cdd:PRK13641 97 QLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881506 259 LDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKKL 303
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
419-549 |
7.92e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 45.22 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRyhqhlqeqlDLDLSPLEYMMKCY 487
Cdd:PRK09536 21 GVDLSVRegslVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddveALSARAASR---------RVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 488 PEIKEKEEM-----RKIIGRYGLTGKQQVS--------------PIRNLSDGQKCRVCLA-WLAWQNPhMLFLDEPTNHL 547
Cdd:PRK09536 92 FDVRQVVEMgrtphRSRFDTWTETDRAAVEramertgvaqfadrPVTSLSGGERQRVLLArALAQATP-VLLLDEPTASL 170
|
..
gi 27881506 548 DI 549
Cdd:PRK09536 171 DI 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
170-304 |
7.96e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.38 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 170 AMLEKEAERLAHEDA-ECEKLMELYERLEELDADkaemrasrilhglgftpamqrkklkdFSGGWRMRVALARALFIRPF 248
Cdd:PRK10584 113 ALLRGESSRQSRNGAkALLEQLGLGKRLDHLPAQ--------------------------LSGGEQQRVALARAFNGRPD 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 249 MLLLDEPTNHLD-------LDACVWLEEELKTfkrILVLVSHSQDfLNGVCTNIIHMHNKKLK 304
Cdd:PRK10584 167 VLFADEPTGNLDrqtgdkiADLLFSLNREHGT---TLILVTHDLQ-LAARCDRRLRLVNGQLQ 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
394-570 |
8.09e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.87 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshVKIGRYHQHLQEQL 473
Cdd:PRK15056 5 AGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS----ILGQPTRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 474 DLDLSPLEYMMKCYPEIKEKEEMrkiIGRYGLTG---------KQQVSP--------------IRNLSDGQKCRVCLAWL 530
Cdd:PRK15056 80 VAYVPQSEEVDWSFPVLVEDVVM---MGRYGHMGwlrrakkrdRQIVTAalarvdmvefrhrqIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881506 531 AWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLVS 570
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELrdEGKTMLVS 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
192-298 |
8.12e-05 |
|
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: 46.16 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 192 LYERLEELDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL 271
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
90 100 110
....*....|....*....|....*....|
gi 27881506 272 KTF---KRILVLVSHSQDFLNGVCTNIIHM 298
Cdd:TIGR01257 2114 VSIireGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
228-288 |
8.89e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.24 E-value: 8.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 228 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEE-----LKTFKRILVLVSHSQDFL 288
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
100-283 |
9.07e-05 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 44.38 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 100 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehIDIYHLTREMPPSDKTPL----HC-----VMEVDTERA 170
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALL----------ENFYQPQGGQVLLDGKPIsqyeHKylhskVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 171 MLEKE-AERLAH--EDAECEKLMELyerleeldADKAemrasrilHGLGFTPAMQR-------KKLKDFSGGWRMRVALA 240
Cdd:cd03248 99 LFARSlQDNIAYglQSCSFECVKEA--------AQKA--------HAHSFISELASgydtevgEKGSQLSGGQKQRVAIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881506 241 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF--KRILVLVSH 283
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
420-573 |
9.25e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 420 IDLDTRVAL-VGPNGAGKST---------LLKLLTGELLPTDGMIRKHSHVKI--------GRYH--------------- 466
Cdd:COG0419 19 IDFDDGLNLiVGPNGAGKSTileairyalYGKARSRSKLRSDLINVGSEEASVelefehggKRYRierrqgefaefleak 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 467 -QHLQEQLD--LDLSPLEYMMKCYPEIKEKEEmRKIIGRYGLTGKQQV--------SPIRNLSDGQKCRVCLAWLAwqnp 535
Cdd:COG0419 99 pSERKEALKrlLGLEIYEELKERLKELEEALE-SALEELAELQKLKQEilaqlsglDPIETLSGGERLRLALADLL---- 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881506 536 hMLFLDepTNHLDIETIDALADAINEfeggMMLVSHDF 573
Cdd:COG0419 174 -SLILD--FGSLDEERLERLLDALEE----LAIITHVI 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
390-438 |
9.49e-05 |
|
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: 45.58 E-value: 9.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 27881506 390 KIPPPVIMVQNVSFKYTKDGPcIYNNLEFGIDLDTRVALVGPNGAGKST 438
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
489-572 |
9.97e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 489 EIKEKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI-ETIDAlADAINEFEGG-- 565
Cdd:PRK13409 195 EVVERLGLENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrQRLNV-ARLIRELAEGky 263
|
....*..
gi 27881506 566 MMLVSHD 572
Cdd:PRK13409 264 VLVVEHD 270
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
392-572 |
1.10e-04 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 44.31 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKY-TKDGPciYNNLEfGIDLDTR----VALVGPNGAGKSTllklltgeLLPTDGMIrkhshvkigRYH 466
Cdd:COG1116 4 AAPALELRGVSKRFpTGGGG--VTALD-DVSLTVAagefVALVGPSGCGKSTllrliaglEKPTSGEV---------LVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 467 QHLQEQLDLDLS--------------------PLEymMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVC 526
Cdd:COG1116 72 GKPVTGPGPDRGvvfqepallpwltvldnvalGLE--LRGVPKAERRERARELLELVGLAGFEDAYP-HQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881506 527 LA-WLAwQNPHMLFLDEPTNHLDIETIDALAD---AINEFEG-GMMLVSHD 572
Cdd:COG1116 149 IArALA-NDPEVLLMDEPFGALDALTRERLQDellRLWQETGkTVLFVTHD 198
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
396-555 |
1.13e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLpTDGMIrkhshvkigryhqhlqeQLD- 474
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDI-----------------QIDg 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 475 --LDLSPLEYMMKCYPEIKEK--------------------EEMRKIIGRYGLTGKQQVSPIR----------NLSDGQK 522
Cdd:cd03289 65 vsWNSVPLQKWRKAFGVIPQKvfifsgtfrknldpygkwsdEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcVLSHGHK 144
|
170 180 190
....*....|....*....|....*....|...
gi 27881506 523 CRVCLAWLAWQNPHMLFLDEPTNHLDIETIDAL 555
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVI 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
98-289 |
1.16e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 98 QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltrEMPPSdktplhcvmEVDTERAMLEkeae 177
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----DVPDN---------QFGREASLID---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 178 RLAHEDaeceklmelyerleeldaDKAEmrASRILHGLGF-TPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPT 256
Cdd:COG2401 105 AIGRKG------------------DFKD--AVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881506 257 NHLD-LDACVW---LEEELKTFKRILVLVSHSQDFLN 289
Cdd:COG2401 165 SHLDrQTAKRVarnLQKLARRAGITLVVATHHYDVID 201
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
419-576 |
1.17e-04 |
|
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: 44.17 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTR----VALVGPNGAGKSTLLklltgellptdGMIRKHSHVKIGRYHQHLQEQLDLDLSPLE------YMMKCYP 488
Cdd:TIGR01978 18 GVNLTVKkgeiHAIMGPNGSGKSTLS-----------KTIAGHPSYEVTSGTILFKGQDLLELEPDEraraglFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 489 E----IKEKEEMRKIIGryGLTGKQQVSPI------------------------RNL----SDGQKCRVCLAWLAWQNPH 536
Cdd:TIGR01978 87 EeipgVSNLEFLRSALN--ARRSARGEEPLdlldfekllkeklalldmdeeflnRSVnegfSGGEKKRNEILQMALLEPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881506 537 MLFLDEPTNHLDIETIDALADAINEF---EGGMMLVSHDFRLI 576
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLL 207
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
403-571 |
1.43e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 403 FKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQL----DLD 476
Cdd:PRK13545 28 FFRSKDGEYHYalNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtgieNIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 477 LSPLeyMMKCYPEiKEKEEMRKIIgRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALA 556
Cdd:PRK13545 108 LKGL--MMGLTKE-KIKEIIPEII-EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170
....*....|....*...
gi 27881506 557 DAINEF-EGG--MMLVSH 571
Cdd:PRK13545 184 DKMNEFkEQGktIFFISH 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
175-585 |
1.45e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 175 EAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDE 254
Cdd:PRK10261 129 ESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQL--------------SGGMRQRVMIAMALSCRPAVLIADE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 255 PTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMHNKKlKYYTGNYDQ--------YVKTRLElee 322
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEMsmgvIFITHDMGVVAEIADRVLVMYQGE-AVETGSVEQifhapqhpYTRALLA--- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 323 nqmkrfhwEQDQIAHMK--NYIARFGHGSakLARQAQSKEKTLQKMMASGltERVVSDKTLSFYFPPCG----KIPPPVI 396
Cdd:PRK10261 271 --------AVPQLGAMKglDYPRRFPLIS--LEHPAKQEPPIEQDTVVDG--EPILQVRNLVTRFPLRSgllnRVTREVH 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 397 MVQNVSFkytkdgpciynNLEFGIDLdtrvALVGPNGAGKSTLLKLLTGELLPTDGMIRKHShvkigryhQHLQEQLDLD 476
Cdd:PRK10261 339 AVEKVSF-----------DLWPGETL----SLVGESGSGKSTTGRALLRLVESQGGEIIFNG--------QRIDTLSPGK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 477 LSPLEYMMKC-----YPEIKEK-------------------EEMRK----IIGRYGLTGKQQVSPIRNLSDGQKCRVCLA 528
Cdd:PRK10261 396 LQALRRDIQFifqdpYASLDPRqtvgdsimeplrvhgllpgKAAAArvawLLERVGLLPEHAWRYPHEFSGGQRQRICIA 475
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 529 WLAWQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:PRK10261 476 RALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
227-283 |
1.48e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881506 227 KDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK----RILVLVSH 283
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAH 1417
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
426-589 |
1.49e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigryhqhlqeqlDLDLSPLEYMmkcypeikekeemrkiigrygl 505
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------EWDGITPVYK---------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 506 tgKQQVSpirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF----EGGMMLVSHDFRLIQQVAQ 581
Cdd:cd03222 67 --PQYID----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSD 140
|
....*...
gi 27881506 582 EIWVCEKQ 589
Cdd:cd03222 141 RIHVFEGE 148
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
229-283 |
1.53e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.77 E-value: 1.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDAcvwLEEELKtfKRILVLVSH 283
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMK--GRTTIVIAH 533
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
426-583 |
1.53e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.80 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDG----------MIR-KHSHVKIGRYHQ--HLQEQLDL---------DLSPLEYM 483
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtinLVRdKDGQLKVADKNQlrLLRTRLTMvfqhfnlwsHMTVLENV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 484 MKCYPEI------KEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALAD 557
Cdd:PRK10619 114 MEAPIQVlglskqEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR 193
|
170 180
....*....|....*....|....*....
gi 27881506 558 AINEF--EGG-MMLVSHDFRLIQQVAQEI 583
Cdd:PRK10619 194 IMQQLaeEGKtMVVVTHEMGFARHVSSHV 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
426-585 |
1.53e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDGMIrkHSHVKIGRYHQHLQEqlDLDLSPLEYMMKCYPEIKE---KEEmrkIIGR 502
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKP--DYDGTVEDLLRSITDDLGSsyyKSE---IIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 503 YGLTgKQQVSPIRNLSDGQKCRV----CLAwlawQNPHMLFLDEPTNHLDIETIDALADAIN----EFEGGMMLVSHDFR 574
Cdd:PRK13409 441 LQLE-RLLDKNVKDLSGGELQRVaiaaCLS----RDADLYLLDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHDIY 515
|
170
....*....|.
gi 27881506 575 LIQQVAQEIWV 585
Cdd:PRK13409 516 MIDYISDRLMV 526
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
225-283 |
1.59e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 44.03 E-value: 1.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 225 KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF----KRILvLVSH 283
Cdd:PRK13537 135 KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlargKTIL-LTTH 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
396-579 |
1.64e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.94 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGmirkHSHVK--IGRYHQH----- 468
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG----HVHMKgsVAYVPQQawiqn 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 --LQEQLDL--DLSPLEY---MMKC--YPEIkekeEM-----RKIIGRYGLtgkqqvspirNLSDGQKCRVCLAWLAWQN 534
Cdd:TIGR00957 713 dsLRENILFgkALNEKYYqqvLEACalLPDL----EIlpsgdRTEIGEKGV----------NLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881506 535 PHMLFLDEPTNHLDIETIDALADAINEFEGGM-----MLVSHDFRLIQQV 579
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQV 828
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
230-260 |
1.84e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 43.30 E-value: 1.84e-04
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
427-556 |
1.92e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.62 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 427 ALVGPNGAGKSTLLKLLTGELLPTDGMI-------RKHSHVKIGRYHQHLQEQLdldlSPLEYM-------MKCYPeike 492
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqplESWSSKAFARKVAYLPQQL----PAAEGMtvrelvaIGRYP---- 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 493 keeMRKIIGRYGLTGKQQV---------SPIRN-----LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI-ETIDALA 556
Cdd:PRK10575 113 ---WHGALGRFGAADREKVeeaislvglKPLAHrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLA 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
426-572 |
2.26e-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: 43.12 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPT----------DGMIRKHSHVKIGRYHQHLQE-QLD-------LDLSPLEYMMKCY 487
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwDEILDEFRGSELQNYFTKLLEgDVKvivkpqyVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 488 PEIKEKEE---MRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIE---TIDALADAINE 561
Cdd:cd03236 109 ELLKKKDErgkLDELVDQLELRHVLD-RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAE 187
|
170
....*....|.
gi 27881506 562 FEGGMMLVSHD 572
Cdd:cd03236 188 DDNYVLVVEHD 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
230-256 |
2.33e-04 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 42.81 E-value: 2.33e-04
10 20
....*....|....*....|....*..
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPT 256
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
218-299 |
2.44e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 218 TPAMQrKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTN 294
Cdd:PRK10762 386 TPSME-QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDR 464
|
....*
gi 27881506 295 IIHMH 299
Cdd:PRK10762 465 ILVMH 469
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
116-283 |
2.56e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 116 LIGLNGIGKSMLLSAI-----GKREVPIPEHIDIYHltremPPSDKTPLHCVMEVDTERAMLEK---EAERLAHEDAE-- 185
Cdd:COG0419 28 IVGPNGAGKSTILEAIryalyGKARSRSKLRSDLIN-----VGSEEASVELEFEHGGKRYRIERrqgEFAEFLEAKPSer 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 186 ---------CEKLMELYERLEELDAD----KAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALfirpfMLLL 252
Cdd:COG0419 103 kealkrllgLEIYEELKERLKELEEAlesaLEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL-----SLIL 177
|
170 180 190
....*....|....*....|....*....|....
gi 27881506 253 DepTNHLDldacvwlEEELKTFKRIL---VLVSH 283
Cdd:COG0419 178 D--FGSLD-------EERLERLLDALeelAIITH 202
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
88-289 |
2.69e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.13 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 88 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GkrevpipehIDIYHLTR-----------EMPPsd 155
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmG---------HPKYEVTSgsilldgedilELSP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 156 ktplhcvmevdTERA-----------------------MLEKEAERLAHEDAEcEKLMELYERLEELDADKaEMrASRIL 212
Cdd:COG0396 72 -----------DERAragiflafqypveipgvsvsnflRTALNARRGEELSAR-EFLKLLKEKMKELGLDE-DF-LDRYV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 213 HGlgftpamqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwLE------EELKTFKRILVLVSHSQD 286
Cdd:COG0396 138 NE-------------GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA---LRivaegvNKLRSPDRGILIITHYQR 201
|
...
gi 27881506 287 FLN 289
Cdd:COG0396 202 ILD 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
396-591 |
2.74e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.23 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIY---NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------------KH 457
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 458 SHVKIGRYHQHLQEQL-------DLDLSPLEYMMkcypEIKE-KEEMRKIIGRYGLTGK-QQVSPIRnLSDGQKCRVCLA 528
Cdd:PRK13646 83 VRKRIGMVFQFPESQLfedtverEIIFGPKNFKM----NLDEvKNYAHRLLMDLGFSRDvMSQSPFQ-MSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 529 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEFE----GGMMLVSHDFRLIQQVAQEIWVCEKQTI 591
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
97-298 |
2.97e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 43.30 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 97 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTREMPPSDKTPLHCVMEVDTERA--MLEK 174
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQ----------------NLNGILKPSSGRILFDGKPIDYSRKglMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 175 EAERLAHEDAECEKL-MELYERLE------ELDADKAEMRASRILHGLGFTPaMQRKKLKDFSGGWRMRVALARALFIRP 247
Cdd:PRK13636 82 ESVGMVFQDPDNQLFsASVYQDVSfgavnlKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 248 FMLLLDEPTNHLD----LDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHM 298
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
196-255 |
3.14e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.71 E-value: 3.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 196 LE--ELDADKAEMRASRILHGLGFT-----PAMQrkklkdFSGGWRMRVALARALFIRPFMLLLDEP 255
Cdd:COG1137 103 LElrKLSKKEREERLEELLEEFGIThlrksKAYS------LSGGERRRVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
202-286 |
3.33e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.81 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 202 DKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEELKT-FKRI--- 277
Cdd:PRK13649 119 EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG----RKELMTlFKKLhqs 194
|
90
....*....|..
gi 27881506 278 ---LVLVSHSQD 286
Cdd:PRK13649 195 gmtIVLVTHLMD 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
209-260 |
3.44e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 3.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 27881506 209 SRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK13409 435 SEIIKPLQLERLLDKN-VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
396-559 |
3.83e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.55 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKYTKDGPCIYNnlefgIDLD--TR--VALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSH----- 459
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQN-----INLSvpSRgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsSLSHsvlrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 460 -------------------VKIGRYHQHLQEQLDLDLSPLEYMMKCYPEikekeemrkiiGRYGLTGKQQvspiRNLSDG 520
Cdd:PRK10790 416 gvamvqqdpvvladtflanVTLGRDISEEQVWQALETVQLAELARSLPD-----------GLYTPLGEQG----NNLSVG 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881506 521 QKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 559
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL 519
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
228-300 |
3.87e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 3.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 228 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF----KRILVLVSHSQDFLNGVCTNIIHMHN 300
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
230-260 |
4.24e-04 |
|
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: 42.22 E-value: 4.24e-04
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
221-298 |
4.36e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.01 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 221 MQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVL-VSHSQDFLNGvCTNII 296
Cdd:PRK10247 130 ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEiihRYVREQNIAVLwVTHDKDEINH-ADKVI 208
|
..
gi 27881506 297 HM 298
Cdd:PRK10247 209 TL 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
204-326 |
4.60e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.77 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 204 AEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDldaCVWLEEELKTFKRI------ 277
Cdd:PRK13651 141 AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD---PQGVKEILEIFDNLnkqgkt 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 27881506 278 LVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLeLEENQMK 326
Cdd:PRK13651 218 IILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKF-LIENNME 265
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
426-548 |
4.76e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.11 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPtdGMIRKHSHV----KIGRYHQHLQ----EQLDL---DLSPLEYMM--------KC 486
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLlngmPIDAKEMRAIsayvQQDDLfipTLTVREHLMfqahlrmpRR 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 487 YPEIKEKEEMRKIIGRYGL-----TGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:TIGR00955 132 VTKKEKRERVDEVLQALGLrkcanTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
491-558 |
4.76e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 491 KEKEEMRKIIGRYGL--TGKQQvsPIRNLSDG--QKcrVCLA-WLAwQNPHMLFLDEPTNHLDI-------ETIDALADA 558
Cdd:COG1129 369 RERALAEEYIKRLRIktPSPEQ--PVGNLSGGnqQK--VVLAkWLA-TDPKVLILDEPTRGIDVgakaeiyRLIRELAAE 443
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
396-591 |
5.09e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKY-TKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYH-QHLQEQL 473
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH-DLRDYTlASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 474 DLdLSPLEYMMK-------CYP--------EIKEKEEMR--------------KIIGRYGLtgkqqvspirNLSDGQKCR 524
Cdd:PRK11176 420 AL-VSQNVHLFNdtianniAYArteqysreQIEEAARMAyamdfinkmdngldTVIGENGV----------LLSGGQRQR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 525 VCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEKQTI 591
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
198-260 |
5.32e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.39 E-value: 5.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 198 ELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK15079 131 KLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
395-571 |
5.35e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDG----PCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-------RKHSHV--- 460
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtSDEENLwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 461 --KIGRYHQHLQEQL-------DLDLSPlEYMMKCYPEIKEK-EEMRKIIGRYgltgKQQVSPIRNLSDGQKCRVCLAWL 530
Cdd:PRK13633 84 rnKAGMVFQNPDNQIvativeeDVAFGP-ENLGIPPEEIRERvDESLKKVGMY----EYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881506 531 AWQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSH 571
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
228-303 |
5.56e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.30 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 228 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEEL--------KTFKRILVLVSHSQDFLNGVCTNIIHMH 299
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG----EEDFinlferlnKEYKKRIIMVTHNMDQVLRIADEVIVMH 225
|
....
gi 27881506 300 NKKL 303
Cdd:PRK13645 226 EGKV 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
97-260 |
5.70e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.78 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 97 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHL-TREMPPSDKT------PLHCVME 164
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLkNREVPFLRRQigmifqDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 165 vdteRAMLEKEAERLAHEDAECEKLMElyerleeldadkaemRASRILHGLGFTpamqrKKLKDF----SGGWRMRVALA 240
Cdd:PRK10908 94 ----RTVYDNVAIPLIIAGASGDDIRR---------------RVSAALDKVGLL-----DKAKNFpiqlSGGEQQRVGIA 149
|
170 180
....*....|....*....|
gi 27881506 241 RALFIRPFMLLLDEPTNHLD 260
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLD 169
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
230-260 |
6.34e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.37 E-value: 6.34e-04
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
396-591 |
7.66e-04 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 41.56 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSfKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVK-----IGRYH 466
Cdd:cd03296 3 IEVRNVS-KRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPvqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 467 QH--------LQEQLDLDLSpLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHML 538
Cdd:cd03296 81 QHyalfrhmtVFDNVAFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 539 FLDEPTNHLDIETIDALADAINEFEGGM----MLVSHDFRLIQQVAQEIWVCEKQTI 591
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-573 |
7.87e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYTkdGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMiRKHSHVKIG-----RYHQH 468
Cdd:PRK14271 20 PAMAAVNLTLGFA--GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGgrsifNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 LQEQLDLDL---SPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQV-----------------SPIRnLSDGQKCRVCLA 528
Cdd:PRK14271 97 LEFRRRVGMlfqRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQArltevglwdavkdrlsdSPFR-LSGGQQQLLCLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881506 529 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGM--MLVSHDF 573
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLtvIIVTHNL 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
86-131 |
7.91e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 7.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 27881506 86 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI 131
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI 47
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
230-283 |
7.97e-04 |
|
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: 40.49 E-value: 7.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSH 283
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
209-260 |
8.36e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 8.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 27881506 209 SRILHGLGFTPAMQrKKLKDFSGGWRMRVALARALfIRPF-MLLLDEPTNHLD 260
Cdd:COG1245 437 TEIIKPLGLEKLLD-KNVKDLSGGELQRVAIAACL-SRDAdLYLLDEPSAHLD 487
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
419-578 |
8.43e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.40 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 419 GIDLDTRVA----LVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQH----LQEQLDLDLSPLEYMMK----- 485
Cdd:PRK10908 20 GVTFHMRPGemafLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH-DITRLKNRevpfLRRQIGMIFQDHHLLMDrtvyd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 486 --CYPEI---KEKEEMRKIIG----RYGLTGKQQVSPIRnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDietiDALA 556
Cdd:PRK10908 99 nvAIPLIiagASGDDIRRRVSaaldKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALS 173
|
170 180
....*....|....*....|....*....
gi 27881506 557 DAI-------NEFEGGMMLVSHDFRLIQQ 578
Cdd:PRK10908 174 EGIlrlfeefNRVGVTVLMATHDIGLISR 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
420-593 |
8.44e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 420 IDLDTRV----ALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVK--------IGRYHQHL--------QEQLDL 475
Cdd:PRK09700 24 VNLTVYPgeihALLGENGAGKSTLMKVLSGIHEPTKGTItinnINYNKLDhklaaqlgIGIIYQELsvideltvLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 476 DLSPLEYMMKC----YPEIKEKEEMrkIIGRYGLtgkqQVSP---IRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:PRK09700 104 GRHLTKKVCGVniidWREMRVRAAM--MLLRVGL----KVDLdekVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881506 549 IETIDALADAINEFEG---GMMLVSHDFRLIQQvaqeiwVCEKQTITK 593
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKegtAIVYISHKLAEIRR------ICDRYTVMK 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
230-300 |
1.02e-03 |
|
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: 40.92 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE-----ELKtFKRILVLVSHSQDFLNgVCTNIIHMHN 300
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLL-NNKTRILVTHQLQLLP-HADQIVVLDN 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
395-572 |
1.13e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 41.26 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGP-CIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-----------KI 462
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQHLQEQL-------DLDLSpLEYMMKCYPEIKEK-EEMRKIIGRYGLTGKQqvsPIRnLSDGQKCRVCLAWLAWQN 534
Cdd:PRK13650 84 GMVFQNPDNQFvgatvedDVAFG-LENKGIPHEEMKERvNEALELVGMQDFKERE---PAR-LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881506 535 PHMLFLDEPTNHLD-------IETIDALADainefEGGMMLVS--HD 572
Cdd:PRK13650 159 PKIIILDEATSMLDpegrlelIKTIKGIRD-----DYQMTVISitHD 200
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
398-543 |
1.15e-03 |
|
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: 40.99 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 398 VQNVSFKYTKDgpCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkHSHVKIGRYHQHLQEQLDL-- 475
Cdd:cd03218 3 AENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL-LDGQDITKLPMHKRARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 476 ---------DLS-------PLEYMMKCYPEIKEKEEmrkiigryGLTGKQQVSPIRN-----LSDGQKCRVCLAWLAWQN 534
Cdd:cd03218 80 lpqeasifrKLTveenilaVLEIRGLSKKEREEKLE--------ELLEEFHITHLRKskassLSGGERRRVEIARALATN 151
|
....*....
gi 27881506 535 PHMLFLDEP 543
Cdd:cd03218 152 PKFLLLDEP 160
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
226-274 |
1.16e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 1.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 27881506 226 LKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF 274
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
101-348 |
1.18e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSdktplhcvmevdterAMLEKEAERLa 180
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS---------------SGLNGQLTGI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 181 hEDAECEKLME--LYERLEELDADKAEM-RASRILHglgftpamqrKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTN 257
Cdd:PRK13545 104 -ENIELKGLMMglTKEKIKEIIPEIIEFaDIGKFIY----------QPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 258 HLD---LDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYY------TGNYDQYVKTRLELEENQMKRF 328
Cdd:PRK13545 173 VGDqtfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDEFLKKYNQMSVEERKDF 252
|
250 260
....*....|....*....|
gi 27881506 329 HWEQdqiahmknyIARFGHG 348
Cdd:PRK13545 253 REEQ---------ISQFQHG 263
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
395-573 |
1.21e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.23 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 395 VIMVQNVSFKYTKDGPC-IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH-----------VKI 462
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGK----QQVSPIRnLSDGQKCRVCLAWLAWQNPHML 538
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRPEII 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881506 539 FLDEPTNHLD----IETIDALADAINEFEGGMMLVSHDF 573
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDL 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
199-260 |
1.28e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.94 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 199 LDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK13652 109 LDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
230-260 |
1.36e-03 |
|
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: 40.68 E-value: 1.36e-03
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
230-256 |
1.67e-03 |
|
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: 40.35 E-value: 1.67e-03
10 20
....*....|....*....|....*..
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPT 256
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
489-572 |
1.74e-03 |
|
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: 41.31 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 489 EIKEKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGG-- 565
Cdd:COG1245 195 ELAEKLGLENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaEEGky 264
|
....*..
gi 27881506 566 MMLVSHD 572
Cdd:COG1245 265 VLVVEHD 271
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
178-260 |
1.91e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 41.37 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 178 RLAHEDAECEKLMELYERleeldADKAEMrASRILHGLGFTPAMQRKKLkdfSGGWRMRVALARALFIRPFMLLLDEPTN 257
Cdd:PRK11174 444 LLGNPDASDEQLQQALEN-----AWVSEF-LPLLPQGLDTPIGDQAAGL---SVGQAQRLALARALLQPCQLLLLDEPTA 514
|
...
gi 27881506 258 HLD 260
Cdd:PRK11174 515 SLD 517
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
512-571 |
2.25e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 512 SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGM--MLVSH 571
Cdd:PRK14247 142 APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMtiVLVTH 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
225-284 |
2.47e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.02 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881506 225 KLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTfKRILVLVSHS 284
Cdd:COG1117 147 RLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEElilELKK-DYTIVIVTHN 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
202-285 |
2.49e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.60 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 202 DKAEMRAsRILHG---LGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL 278
Cdd:PRK11650 107 PKAEIEE-RVAEAariLELEPLLDRKP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRL 184
|
90
....*....|.
gi 27881506 279 ----VLVSHSQ 285
Cdd:PRK11650 185 kttsLYVTHDQ 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
394-615 |
2.50e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 394 PVIMVQNVSFKYTKDGP--CIYNNLEFGIDLDTRVALVGPNGAGKS-TLLKLLTGELLP----TDGMIRKHS-------- 458
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGesllhase 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 459 ----HVKIGRYHQHLQEQLdLDLSPLEYMMKCYPEIKEKEE-MRKIIGRYGLTGKQQVSPIRN-----------LSDGQK 522
Cdd:PRK15134 84 qtlrGVRGNKIAMIFQEPM-VSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQaakrltdyphqLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 523 CRVCLAWLAWQNPHMLFLDEPTNHLDIeTIDA-----LADAINEFEGGMMLVSHDFRLIQQVAQEIWV-----CEKQTIT 592
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDV-SVQAqilqlLRELQQELNMGLLFITHNLSIVRKLADRVAVmqngrCVEQNRA 241
|
250 260
....*....|....*....|....
gi 27881506 593 KwpgDILAYKEH-LKSKLVDEEPQ 615
Cdd:PRK15134 242 A---TLFSAPTHpYTQKLLNSEPS 262
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
200-260 |
2.73e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.71 E-value: 2.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881506 200 DADKAEMR-ASRILHGLGFtpaMQRKKLK----------DFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK13657 435 DATDEEMRaAAERAQAHDF---IERKPDGydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
220-260 |
2.80e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 40.00 E-value: 2.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 27881506 220 AMQRKKLKDF--------SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK13635 124 ALRQVGMEDFlnrephrlSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
101-438 |
2.86e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 101 LSDTK------LELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVPIpEHI------DIYHLTREMPPSDKTPLH 160
Cdd:PRK10938 13 LSDTKtlqlpsLTLNAGDSWAFVGANGSGKSALARALagelpllsGERQSQF-SHItrlsfeQLQKLVSDEWQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 161 CVMEVDTERAMLEKEAERLaHEDAECEKLMELyerleeldadkaemrasrilhgLGFTPAMQRKkLKDFSGGWRMRVALA 240
Cdd:PRK10938 92 SPGEDDTGRTTAEIIQDEV-KDPARCEQLAQQ----------------------FGITALLDRR-FKYLSTGETRKTLLC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 241 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVshsqdfLNgvctniihmhnkklkyytgnydqyvktr 317
Cdd:PRK10938 148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLV------LN---------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 318 leleenqmkRFhweqDQIAHMKNYIARFGhgSAKLARQAqSKEKTLQKMMASGL--TERVVsDKTLSFYFPPCGK--IPP 393
Cdd:PRK10938 194 ---------RF----DEIPDFVQFAGVLA--DCTLAETG-EREEILQQALVAQLahSEQLE-GVQLPEPDEPSARhaLPA 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 27881506 394 --PVIMVQNVSFKYTkDGPcIYNNLEFGIDLDTRVALVGPNGAGKST 438
Cdd:PRK10938 257 nePRIVLNNGVVSYN-DRP-ILHNLSWQVNPGEHWQIVGPNGAGKST 301
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
386-572 |
2.93e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.20 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 386 PPCGKIPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigry 465
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 466 hqhlqeQLD-LDLS-------PLEYMMKCYP-----------------------EIKEK-EEMRKIIGRYGLTGKQQvsp 513
Cdd:PRK11607 77 ------MLDgVDLShvppyqrPINMMFQSYAlfphmtveqniafglkqdklpkaEIASRvNEMLGLVHMQEFAKRKP--- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 514 iRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDAL----ADAINEFEGGMMLVSHD 572
Cdd:PRK11607 148 -HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERVGVTCVMVTHD 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
412-551 |
3.14e-03 |
|
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: 40.66 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 412 IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrKHSHvKIGRYHQ-------HLQEQLDLDLSPLEY-- 482
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-KHSG-RISFSPQtswimpgTIKDNIIFGLSYDEYry 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 483 ---MMKCYPE---IKEKEEMRKIIGRYGLTgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIET 551
Cdd:TIGR01271 519 tsvIKACQLEediALFPEKDKTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
229-283 |
3.15e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 3.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK----RILVLVSH 283
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenRITIIIAH 638
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
418-438 |
3.17e-03 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 39.34 E-value: 3.17e-03
10 20
....*....|....*....|....*
gi 27881506 418 FGIDLDTR----VALVGPNGAGKST 438
Cdd:cd03224 17 FGVSLTVPegeiVALLGRNGAGKTT 41
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
90-132 |
3.18e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 39.68 E-value: 3.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 27881506 90 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIG 132
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS 48
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
229-284 |
3.21e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.69 E-value: 3.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 229 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF--KRILVLVSHS 284
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
462-572 |
3.45e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 462 IGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQqvsPIRNLSDGQKcRV-CLAWLAWQNPH---M 537
Cdd:pfam13304 185 LQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGEL---PAFELSDGTK-RLlALLAALLSALPkggL 260
|
90 100 110
....*....|....*....|....*....|....*...
gi 27881506 538 LFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHD 572
Cdd:pfam13304 261 LLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHS 298
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
196-260 |
3.72e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.71 E-value: 3.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 196 LEELDADKAEMRaSRILHGLGFTpAMQRKKLKD---FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK13650 107 LENKGIPHEEMK-ERVNEALELV-GMQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
396-585 |
3.93e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 396 IMVQNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG-MIRKHSH-----------VKI 462
Cdd:PTZ00265 383 IQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHnlkdinlkwwrSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 463 GRYHQ------------------------HLQEQLD------------------------------LDLSPLEYMMKCYP 488
Cdd:PTZ00265 463 GVVSQdpllfsnsiknnikyslyslkdleALSNYYNedgndsqenknkrnscrakcagdlndmsntTDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 489 EIKEKE----EMRKIIGRY--GLTGKQQV---SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 559
Cdd:PTZ00265 543 TIKDSEvvdvSKKVLIHDFvsALPDKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|
gi 27881506 560 NEFEGG----MMLVSHDFRLIqQVAQEIWV 585
Cdd:PTZ00265 623 NNLKGNenriTIIIAHRLSTI-RYANTIFV 651
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
517-585 |
3.93e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 3.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881506 517 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
517-585 |
3.95e-03 |
|
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: 40.05 E-value: 3.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 517 LSDGQKCRVCLAW-LAwQNPHMLFLDEPTNHLDIeTIDA-----LADAINEFEGGMMLVSHDFRLIQQVAQEIWV 585
Cdd:COG4172 157 LSGGQRQRVMIAMaLA-NEPDLLIADEPTTALDV-TVQAqildlLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
226-260 |
4.24e-03 |
|
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: 40.19 E-value: 4.24e-03
10 20 30
....*....|....*....|....*....|....*
gi 27881506 226 LKdFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:COG5265 493 LK-LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
412-551 |
4.58e-03 |
|
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: 39.45 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 412 IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrKHSHvKIGRYHQ-------HLQEQLDLDLSPLEYMM 484
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-KHSG-RISFSSQfswimpgTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881506 485 K-----CYPE---IKEKEEMRKIIGRYGLTgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIET 551
Cdd:cd03291 130 KsvvkaCQLEediTKFPEKDNTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
202-256 |
4.61e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 4.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 202 DKAEMR--ASRILHGLGFT--PamqRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPT 256
Cdd:COG1129 113 DWRAMRrrARELLARLGLDidP---DTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
392-572 |
4.62e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 39.70 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTllklltgeLLPTDGMI----RKHSHVKIGRYH- 466
Cdd:COG3842 2 AMPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmiagfETPDSGRIlldgRDVTGLPPEKRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 467 ----QhlqeqlDLDLSPleYM-----------MKCYP--EIKEK-EEMRKIIgryGLTGKQQVSPiRNLSDGQKCRVCLA 528
Cdd:COG3842 80 gmvfQ------DYALFP--HLtvaenvafglrMRGVPkaEIRARvAELLELV---GLEGLADRYP-HQLSGGQQQRVALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881506 529 -WLAwQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSHD 572
Cdd:COG3842 148 rALA-PEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
517-548 |
5.50e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.99 E-value: 5.50e-03
10 20 30
....*....|....*....|....*....|..
gi 27881506 517 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
418-438 |
5.61e-03 |
|
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: 38.81 E-value: 5.61e-03
10 20
....*....|....*....|....*
gi 27881506 418 FGIDLDTR----VALVGPNGAGKST 438
Cdd:COG0410 20 HGVSLEVEegeiVALLGRNGAGKTT 44
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
203-288 |
5.63e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 39.93 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 203 KAEMRASRILHGLGFTPAMQRKKLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDACVWLEEEL 271
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVL 810
|
90
....*....|....*..
gi 27881506 272 KTFKRIlvLVSHSQDFL 288
Cdd:TIGR00957 811 KNKTRI--LVTHGISYL 825
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
392-583 |
5.68e-03 |
|
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: 38.81 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 392 PPPVIMVQNVSFKYtkDGPCIYNnlefGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMI------------- 454
Cdd:COG1127 2 SEPMIEVRNLTKSF--GDRVVLD----GVSLDVPrgeiLAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 455 -----RKhshvKIGRYHQH----------------LQEQLDLDlspleymmkcypeikeKEEMRKI----IGRYGLTGKQ 509
Cdd:COG1127 76 elyelRR----RIGMLFQGgalfdsltvfenvafpLREHTDLS----------------EAEIRELvlekLELVGLPGAA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 510 QVSPiRNLSDGQKCRVCLA-WLAwQNPHMLFLDEPTNHLDIETIDALADAINE----FEGGMMLVSHDFRLIQQVAQEI 583
Cdd:COG1127 136 DKMP-SELSGGMRKRVALArALA-LDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRV 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
400-583 |
5.73e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 39.30 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 400 NVSFKYTKdgpcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKH----SHV-----KIGRYHQH-- 468
Cdd:PRK10851 9 KKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvSRLhardrKVGFVFQHya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 469 ------LQEQLDLDLSPLEYMMKCYPEIKEKEEMRkiigrygLTGKQQVSPIRN-----LSDGQKCRVCLAWLAWQNPHM 537
Cdd:PRK10851 85 lfrhmtVFDNIAFGLTVLPRRERPNAAAIKAKVTQ-------LLEMVQLAHLADrypaqLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881506 538 LFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDfrliQQVAQEI 583
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHD----QEEAMEV 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
514-548 |
5.77e-03 |
|
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: 38.79 E-value: 5.77e-03
10 20 30
....*....|....*....|....*....|....*
gi 27881506 514 IRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 548
Cdd:cd03234 141 VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
230-260 |
5.84e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.40 E-value: 5.84e-03
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
426-583 |
6.30e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 39.71 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 426 VALVGPNGAGKSTLLKLLTGELLPTDG-------------------MIRKHSHVKIGRYH--QHLQEQLDLDLsPLEYMM 484
Cdd:PRK10535 37 VAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqdvatldadalaqLRREHFGFIFQRYHllSHLTAAQNVEV-PAVYAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881506 485 KcyPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI---ETIDALADAINE 561
Cdd:PRK10535 116 L--ERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLRD 192
|
170 180
....*....|....*....|..
gi 27881506 562 FEGGMMLVSHDFRLIQQvAQEI 583
Cdd:PRK10535 193 RGHTVIIVTHDPQVAAQ-AERV 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
203-260 |
6.47e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.06 E-value: 6.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881506 203 KAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:PRK13631 151 EAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
230-260 |
8.09e-03 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 39.31 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|.
gi 27881506 230 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
207-260 |
9.46e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 38.87 E-value: 9.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881506 207 RASRILHGLGFTPAMQRK-----KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 260
Cdd:TIGR00955 140 RVDEVLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
220-263 |
9.51e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.04 E-value: 9.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 27881506 220 AMQRKKLKDF---------SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDA 263
Cdd:TIGR02633 386 AIQRLKVKTAspflpigrlSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
|
| |
