|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
95-609 |
5.19e-172 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 499.59 E-value: 5.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP------IPEHIDIYHLTREMP-PSEKTPLQCV 167
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdsgevsIPKGLRIGYLPQEPPlDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 168 MEVDTERAMLEREAERL----AHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVA 243
Cdd:COG0488 83 LDGDAELRALEAELEELeaklAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 244 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRL 323
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 324 ELEENQMKRFHWEQDQIAHMKNYIARFGhGSAKLARQAQSKEKTLQKMMAsglTERVVSDKTLSFYFPPCGKIPPPVIMV 403
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFR-AKARKAKQAQSRIKALEKLER---EEPPRRDKTVEIRFPPPERLGKKVLEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 404 QNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHlQEQLDLDLS 483
Cdd:COG0488 319 EGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-QEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 484 PLEYMMKCYPEIKEKeEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADA 563
Cdd:COG0488 396 VLDELRDGAPGGTEQ-EVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 23956078 564 INEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEH 609
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
72-612 |
1.59e-155 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 464.72 E-value: 1.59e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 72 KAAARAVTGVLASH------PNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-IP 144
Cdd:PLN03073 153 EAAKAGMPGVYVNHdgngggPAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 145 EHIDIYHLTREMPPSEKTPLQCVMEVDTERA-MLEREAERLAH----------------------EDAECEKLMELYERL 201
Cdd:PLN03073 233 KNCQILHVEQEVVGDDTTALQCVLNTDIERTqLLEEEAQLVAQqrelefetetgkgkgankdgvdKDAVSQRLEEIYKRL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 202 EELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR 281
Cdd:PLN03073 313 ELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 282 ILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHgSAKLARQA 361
Cdd:PLN03073 393 TFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRY-NAKRASLV 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 362 QSKEKTLQKMmasGLTERVVSDKTLSFYFP-PCGKIPPPVIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAG 440
Cdd:PLN03073 472 QSRIKALDRL---GHVDAVVNDPDYKFEFPtPDDRPGPPIISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIG 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 441 KSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEkEEMRKIIGRYGLTGKQQVSPIR 520
Cdd:PLN03073 548 KSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPE-QKLRAHLGSFGVTGNLALQPMY 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 521 NLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWP 600
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFH 706
|
570
....*....|..
gi 23956078 601 GDILAYKEHLKS 612
Cdd:PLN03073 707 GTFHDYKKTLQS 718
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
105-610 |
1.60e-99 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 317.11 E-value: 1.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 105 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKRE-------VPIPEHIDIYHLTREMPPSEKTPLQCVMEVDTERAML 177
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALL-KNEisadggsYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 178 EREAErLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLL 257
Cdd:PRK10636 95 EAQLH-DANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 258 DEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQ 337
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 338 DQIAHMKNYIARFGHGSAKlARQAQSKEKTLQKMmasgltERVV---SDKTLSFYFPPCGKIPPPVIMVQNVSFKYTKDg 414
Cdd:PRK10636 254 ERVAHLQSYIDRFRAKATK-AKQAQSRIKMLERM------ELIApahVDNPFHFSFRAPESLPNPLLKMEKVSAGYGDR- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 415 pCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPE 494
Cdd:PRK10636 326 -IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 495 IKEkEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLV 574
Cdd:PRK10636 405 ELE-QKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVV 483
|
490 500 510
....*....|....*....|....*....|....*.
gi 23956078 575 SHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHL 610
Cdd:PRK10636 484 SHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWL 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
95-616 |
3.38e-71 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 239.02 E-value: 3.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremPPSEK------------- 161
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-------DPNERlgklrqdqfafee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 162 -TPLQCVMEVDTE--RAMLEREAERLAHEDAECE--KLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSG 236
Cdd:PRK15064 79 fTVLDTVIMGHTElwEVKQERDRIYALPEMSEEDgmKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 237 GWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYD 316
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 317 QYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGSAKlARQAQSKEKTLQKMMasgLTE-RVVSDKTLSFYFPPCGK 395
Cdd:PRK15064 239 EYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASK-AKQATSRAKQIDKIK---LEEvKPSSRQNPFIRFEQDKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 396 IPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQ 475
Cdd:PRK15064 315 LHRNALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 476 EQLDLDLSPLEYMMKcYPEIKEKEEM-RKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI 554
Cdd:PRK15064 393 YDFENDLTLFDWMSQ-WRQEGDDEQAvRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 555 ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDilaYKEHLKSKLVD 616
Cdd:PRK15064 472 ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGT---YEEYLRSQGIE 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
102-617 |
1.42e-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: 214.03 E-value: 1.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLL---SAIGKR---EVPIPEHIDIYHLTREmPP--SEKTPLQCVME-VDT 172
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLrimAGVDKDfngEARPQPGIKVGYLPQE-PQldPTKTVRENVEEgVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 ERAMLEREAE---RLAHEDAECEKLMELYERLEE-LDADKA---EMRASRILHGLGFTPAMQrkKLKDFSGGWRMRVALA 245
Cdd:TIGR03719 96 IKDALDRFNEisaKYAEPDADFDKLAAEQAELQEiIDAADAwdlDSQLEIAMDALRCPPWDA--DVTKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 246 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYV---KTR 322
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLeqkQKR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 323 LELEENQ----MKRFHWEQDQIAHmknyiarfghgSAKlARQAQSKEK--TLQKMMASGLTERvvsDKTLSFYFPPCGKI 396
Cdd:TIGR03719 254 LEQEEKEesarQKTLKRELEWVRQ-----------SPK-GRQAKSKARlaRYEELLSQEFQKR---NETAEIYIPPGPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHlQE 476
Cdd:TIGR03719 319 GDKVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS-RD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 477 QLDLDLSPLEYMMKCYPEIK-EKEEM--RKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKlGKREIpsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 554 IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKW-PGDILAYKEHLKSKLVDE 617
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWfEGNFSEYEEDKKRRLGED 540
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
91-592 |
1.88e-56 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 201.72 E-value: 1.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrEVPIPEHIDIYH----LTR--EMPPS--EKT 162
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLLDDGRIIYEqdliVARlqQDPPRnvEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 163 PLQCVMEVDTERAMLEREAERLAHE------DAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAmqrKKLKDFSG 236
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLvetdpsEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 237 GWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYD 316
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 317 QYVKTR---LELEENQMKRFhweQDQIAHMKNYI-----ARF----GHGSA-KLARQAQSKEKTLQ---KMMasglterv 380
Cdd:PRK11147 240 QYLLEKeeaLRVEELQNAEF---DRKLAQEEVWIrqgikARRtrneGRVRAlKALRRERSERREVMgtaKMQ-------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 381 VSDKTLSfyfppcGKIpppVIMVQNVSfkYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR 460
Cdd:PRK11147 309 VEEASRS------GKI---VFEMENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 461 KHSHVKIGRYHQHlQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIG---RYGLTGKQQVSPIRNLSDGQKCRVCLAWLAW 537
Cdd:PRK11147 378 CGTKLEVAYFDQH-RAELDPEKTVMDNLAEGKQEVMVNGRPRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFL 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 538 QNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCE 592
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFE 511
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
120-577 |
1.43e-50 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 183.78 E-value: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 120 GLIGLNGIGKSMLL---SAIGKR---EVPIPEHIDIYHLTREmPP--SEKTPLQCVME-VDTERAMLER--E-AERLAHE 187
Cdd:PRK11819 37 GVLGLNGAGKSTLLrimAGVDKEfegEARPAPGIKVGYLPQE-PQldPEKTVRENVEEgVAEVKAALDRfnEiYAAYAEP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 188 DAECEKLME----LYERLEELDADKAEMRASRILHGLGFTPAMQrkKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNH 263
Cdd:PRK11819 116 DADFDALAAeqgeLQEIIDAADAWDLDSQLEIAMDALRCPPWDA--KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 264 LDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKT---RLELEENQ----MKRFHWE 336
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQkakRLAQEEKQeaarQKALKRE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 337 QDQIAHmknyiarfghgSAKlARQAQSKE--KTLQKMMASGLTERvvsDKTLSFYfppcgkIPPP------VIMVQNVSF 408
Cdd:PRK11819 274 LEWVRQ-----------SPK-ARQAKSKArlARYEELLSEEYQKR---NETNEIF------IPPGprlgdkVIEAENLSK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 409 KYtkDGPCIYNNLEF-----GIdldtrVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHlQEQLDLDLS 483
Cdd:PRK11819 333 SF--GDRLLIDDLSFslppgGI-----VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-RDALDPNKT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 484 PLEymmkcypEIKE--------KEEM--RKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:PRK11819 405 VWE-------EISGgldiikvgNREIpsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
490 500
....*....|....*....|....
gi 23956078 554 IETIDALADAINEFEGGMMLVSHD 577
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 ... |
91-307 |
7.82e-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: 7.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHltremppsektplqcvmev 170
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 dteramlereAERLAHedaeceklmelYERLeeldadkaemrasrilhglgftpamqrkklkdfSGGWRMRVALARALFI 250
Cdd:cd03221 62 ----------TVKIGY-----------FEQL---------------------------------SGGEKMRLALAKLLLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 251 RPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKK 307
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 ... |
401-595 |
8.99e-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: 8.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQhlqeqldl 480
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 481 dlspleymmkcypeikekeemrkiigrygltgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDAL 560
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 23956078 561 ADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQT 595
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
93-324 |
7.36e-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: 103.78 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLtrempPSEKTPLqcvmEVDT 172
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-----DVRKEPR----EARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 ERAMLEreAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRP 252
Cdd:COG4555 75 QIGVLP--DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 253 FMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKLKYY---TGNYDQYVKTRLE 324
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVILHKGKVVAQgslDELREEIGEENLE 229
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
301-371 |
9.01e-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: 98.03 E-value: 9.01e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956078 301 IHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGsAKLARQAQSKEKTLQKM 371
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAK-ASKAKQAQSRIKALEKM 70
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
106-262 |
5.60e-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: 5.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMPPSEKTPLQCVMEVDTERAMLeREAER 183
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgQDLTDDERKSLRKEIGYVFQDPQLFPRL-TVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 184 LAhedaeceklmeLYERLEELDADKAEMRASRILHGLGFTPAMQRK---KLKDFSGGWRMRVALARALFIRPFMLLLDEP 260
Cdd:pfam00005 80 LR-----------LGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 23956078 261 TN 262
Cdd:pfam00005 149 TA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
91-590 |
3.62e-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: 100.36 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKREVPIPEHIDIYHL-----TREMPPSEKTP 163
Cdd:COG1123 5 LEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRISGEVLldgrdLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 164 LQCVMEVDTERAMLereAERLAHEDAECeklmelyerLEELDADKAEM--RASRILHGLGFtPAMQRKKLKDFSGGWRMR 241
Cdd:COG1123 84 RIGMVFQDPMTQLN---PVTVGDQIAEA---------LENLGLSRAEAraRVLELLEAVGL-ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 242 VALARALFIRPFMLLLDEPTNHLD-------LDACVWLEEELKTfkrILVLVSHSQDFLNGVCTNIIHMHNKKLkYYTGN 314
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDvttqaeiLDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVMDDGRI-VEDGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 315 YDQYVKTRLELEEnqmkrfhweqdqiahmknyIARFGHGSAKLARQAQSKEKTLQkmmasgltervVSDktLSFYFPPCG 394
Cdd:COG1123 227 PEEILAAPQALAA-------------------VPRLGAARGRAAPAAAAAEPLLE-----------VRN--LSKRYPVRG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 395 KIPPPVimVQNVSFKytkdgpciynnLEFGidldTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKI 467
Cdd:COG1123 275 KGGVRA--VDDVSLT-----------LRRG----ETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltKLSRRSL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQHLQ-------EQLDldlsP-------LEYMMKCYPEIKEKEEMRKI---IGRYGLTGKQQVSPIRNLSDGQKCRV 530
Cdd:COG1123 338 RELRRRVQmvfqdpySSLN----PrmtvgdiIAEPLRLHGLLSRAERRERVaelLERVGLPPDLADRYPHELSGGQRQRV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 531 CLA-WLAwQNPHMLFLDEPTNHLDIET----IDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:COG1123 414 AIArALA-LEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAV 477
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
93-308 |
3.12e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.19 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGkrevpipeHIDIYH----LTREMPPSEKTPLQCVM 168
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA--------DLDPPTsgeiYLDGKPLSAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 169 EV-----------DTERAMLEReAERLAHEDAECEKLMELYERLeeldadkaemrasrilhglGFTPAMQRKKLKDFSGG 237
Cdd:COG4619 75 QVayvpqepalwgGTVRDNLPF-PFQLRERKFDRERALELLERL-------------------GLPPDILDKPVERLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 238 WRMRVALARALFIRPFMLLLDEPTNHLDLD--ACV--WLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:COG4619 135 ERQRLALIRALLLQPDVLLLDEPTSALDPEntRRVeeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
92-307 |
8.02e-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: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsektplqcvmevd 171
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 172 teramlereaerlahedaeceklmelyerleeLDADKAEMRASRILHGLGFTPamqrkklkDFSGGWRMRVALARALFIR 251
Cdd:cd00267 59 --------------------------------DGKDIAKLPLEELRRRIGYVP--------QLSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 252 PFMLLLDEPTNHLDLDACVWLEEELKTF---KRILVLVSHSQDFLNGVCTNIIHMHNKK 307
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 ... |
95-584 |
1.93e-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: 95.25 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GKREVPIPEHIDIYHLTR-----EMPPSEKTPLQC-- 166
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrGMDQYEPTSGRIIYHVALcekcgYVERPSKVGEPCpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 167 ------VMEVD------TERA--------MLEREAErLAHEDAECEKLMELYERLEeLDADKAEMRASRILHGLGFTPAM 226
Cdd:TIGR03269 85 cggtlePEEVDfwnlsdKLRRrirkriaiMLQRTFA-LYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 227 QRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVW----LEEELKTFKRILVLVSHSQDFLNGVCTNIIH 302
Cdd:TIGR03269 163 THIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 303 MHNKKLKYyTGNYDQYVKTRLELEENqmkrfhWEQDQIAHMKNYIARFghgsaklarqaqskeKTLQKMMASglTERVVs 382
Cdd:TIGR03269 242 LENGEIKE-EGTPDEVVAVFMEGVSE------VEKECEVEVGEPIIKV---------------RNVSKRYIS--VDRGV- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 383 dktlsfyfppcgkipppVIMVQNVSFKytkdgpcIYNNLEFGIdldtrvalVGPNGAGKSTLLKLLTGELLPTDG----- 457
Cdd:TIGR03269 297 -----------------VKAVDNVSLE-------VKEGEIFGI--------VGTSGAGKTTLSKIIAGVLEPTSGevnvr 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 458 -------------MIRKHSHVKIGRYHQ------------HLQEQLDLDLsPLEY-MMKCYPEIK----EKEEMRKIIGR 507
Cdd:TIGR03269 345 vgdewvdmtkpgpDGRGRAKRYIGILHQeydlyphrtvldNLTEAIGLEL-PDELaRMKAVITLKmvgfDEEKAEEILDK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 508 YGLTgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDFRLIQQ 583
Cdd:TIGR03269 424 YPDE----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLD 493
|
.
gi 23956078 584 V 584
Cdd:TIGR03269 494 V 494
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
403-593 |
4.22e-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: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRYH----- 471
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdlTKLSLKELRRKvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 472 QHLQEQL-------DLDLSPLEYMMkcypeikEKEEMRKIIG----RYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNP 540
Cdd:cd03225 82 QNPDDQFfgptveeEVAFGLENLGL-------PEEEIEERVEealeLVGLEGLRDRSP-FTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 541 HMLFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEIWVCEK 593
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLkAEGKtiIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
403-577 |
9.88e-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: 9.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRYHQHLQE 476
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 477 QLDLDLSPLEY-MMKCYPEI--------KEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDE 547
Cdd:cd03235 80 DRDFPISVRDVvLMGLYGHKglfrrlskADKAKVDEALERVGLSELAD-RQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|...
gi 23956078 548 PTNHLDIETIDALADAINEF--EG-GMMLVSHD 577
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrrEGmTILVVTHD 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
91-296 |
1.47e-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: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKRevpipehidiyhltreMPPSEKTplqcvMEV 170
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGL----------------LPPSAGE-----VLW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREAER-----LAHEDAeceklmeLYERL---EELD-------ADKAEMRASRILHGLGFTPAMQRKkLKDFS 235
Cdd:COG4133 62 NGEPIRDAREDYRrrlayLGHADG-------LKPELtvrENLRfwaalygLRADREAIDEALEAVGLAGLADLP-VRQLS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 236 GGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGV 296
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
401-612 |
1.92e-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: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRY--- 470
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditKKNLRELRRKvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 -HQHLQEQL-------DLDLSPLEYMMkcypeikEKEEMRKII----GRYGLTGKQQVSPiRNLSDGQKCRVCLAW-LAw 537
Cdd:COG1122 80 vFQNPDDQLfaptveeDVAFGPENLGL-------PREEIRERVeealELVGLEHLADRPP-HELSGGQKQRVAIAGvLA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 538 QNPHMLFLDEPTNHLDIETIDALADAINEF--EG-GMMLVSHDFRLIQQVAQEIWVCEKQTITKW--PGDILAYKEHLKS 612
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGRIVADgtPREVFSDYELLEE 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
401-577 |
4.64e-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: 86.40 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG--MIRKHS--------HVKIGRY 470
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 HQHlqEQLDLDLSPLEYM-----MKCYPEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFL 545
Cdd:cd03263 81 PQF--DALFDELTVREHLrfyarLKGLPKSEIKEEVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190
....*....|....*....|....*....|....
gi 23956078 546 DEPTNHLDIETIDALADAINEFEGG--MMLVSHD 577
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGrsIILTTHS 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
91-308 |
9.06e-19 |
|
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: 83.99 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPSEKtplqcvmEV 170
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII----------------LGLLKPDSG-------EI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 dteramlereaerlahedaeceklmelyeRLEELDADKAEMRASRIL----HGLGFTPAMQRKKLKDFSGGWRMRVALAR 246
Cdd:cd03230 58 -----------------------------KVLGKDIKKEPEEVKRRIgylpEEPSLYENLTVRENLKLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 247 ALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
420-613 |
1.01e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.01 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 420 NLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQ-------------------HLQEQL-- 478
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydfvaegieEQAEYLkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 479 ------DLDLSPLEYMMKCYPEIKEKEE----------MRKIIGRYGLTGKQQVSpirNLSDGQKCRVCLAWLAWQNPHM 542
Cdd:PRK11147 101 yhdishLVETDPSEKNLNELAKLQEQLDhhnlwqlenrINEVLAQLGLDPDAALS---SLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956078 543 LFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDilaYKEHLKSK 613
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN---YDQYLLEK 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
401-593 |
1.15e-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: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkIGryhqhlqeqlDL 480
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------ID----------GV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 481 DLSPLeymmkcypeikEKEEMRKIIG-------RYGLTgkqqvspIRN--LSDGQKCRVCLAWLAWQNPHMLFLDEPTNH 551
Cdd:cd03228 65 DLRDL-----------DLESLRKNIAyvpqdpfLFSGT-------IREniLSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23956078 552 LDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEK 593
Cdd:cd03228 127 LDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
403-590 |
1.50e-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: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhlqeqldLDL 482
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------------------IDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 483 SPLEYmmkcypeiKEKEEMRKIIGRygltgkqqvspIRNLSDGQKCRVCLAwLAW-QNPHMLFLDEPTNHLDIETIDALA 561
Cdd:cd00267 61 KDIAK--------LPLEELRRRIGY-----------VPQLSGGQRQRVALA-RALlLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|..
gi 23956078 562 DAINEF-EGGMM--LVSHDFRLIQQVAQEIWV 590
Cdd:cd00267 121 ELLRELaEEGRTviIVTHDPELAELAADRVIV 152
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
91-324 |
1.82e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.73 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTREMPPSEKTplqcvMEV 170
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIR----------------MLLGLLRPTSGE-----VRV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREA--ERLA--------HEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMqRKKLKDFSGGWRM 240
Cdd:COG1131 60 LGEDVARDPAEvrRRIGyvpqepalYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 241 RVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKLKyYTGNYDQ 317
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAaegKTVLLSTHYLEEAERLCDRVAIIDKGRIV-ADGTPDE 217
|
....*..
gi 23956078 318 YVKTRLE 324
Cdd:COG1131 218 LKARLLE 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
397-585 |
2.75e-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: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGrY 470
Cdd:COG1121 3 MMPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIG-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 -HQHLQEQLDLDLSPLEY-MMKCYPEI--------KEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLA-WLAwQN 539
Cdd:COG1121 80 vPQRAEVDWDFPITVRDVvLMGRYGRRglfrrpsrADREAVDEALERVGLEDLAD-RPIGELSGGQQQRVLLArALA-QD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23956078 540 PHMLFLDEPTNHLDIETIDALADAINEF--EG-GMMLVSHDFRLIQQVA 585
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYF 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
399-577 |
5.49e-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: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVKIGRYHQHL- 474
Cdd:COG4133 1 MMLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngEPIRDAREDYRRRLa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 475 ----QEQLDLDLSPLEYM---MKCYPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLA--WLAwqNPHMLFL 545
Cdd:COG4133 79 ylghADGLKPELTVRENLrfwAALYGLRADREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALArlLLS--PAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 23956078 546 DEPTNHLDIETIDALADAINEF--EGGM-MLVSHD 577
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHlaRGGAvLLTTHQ 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
91-305 |
8.45e-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: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSEKTPlq 165
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgeDLTDLEDELPPLRRRI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 cvmevdterAMLEREAErlahedaeceklmeLYERLEELDadkaemrasRILHGLgftpamqrkklkdfSGGWRMRVALA 245
Cdd:cd03229 79 ---------GMVFQDFA--------------LFPHLTVLE---------NIALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 246 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKT----FKRILVLVSHSQDFLNGVCTNIIHMHN 305
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
95-307 |
1.19e-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: 81.74 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltREMPPSEKTPLQCVMEV-- 170
Cdd:cd03225 4 NLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----DGKDLTKLSLKELRRKVgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 ---DTERAMLEREAErlahEDAE--CEKLMelyerleeLDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALA 245
Cdd:cd03225 80 vfqNPDDQFFGPTVE----EEVAfgLENLG--------LPEEEIEERVEEALELVGLEGLRDRS-PFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 246 RALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKK 307
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
418-550 |
1.89e-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: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 418 YNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-----------RKHSHVKIGRYHQHLqeQLDLDLSPLE 486
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 487 YM-----MKCYPEIKEKEEMRKIIGRYGLTGKQ---QVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTN 550
Cdd:pfam00005 79 NLrlgllLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
91-308 |
2.88e-17 |
|
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: 81.03 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIyhltremppsEKTPLQCVMEV 170
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI----------DGRDVTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREAERLAHedaeceklMELYE------RLEELDADKAEMRASRILHGLGFTPAMQRK--KLkdfSGGWRMRV 242
Cdd:cd03259 71 RRNIGMVFQDYALFPH--------LTVAEniafglKLRGVPKAEIRARVRELLELVGLEGLLNRYphEL---SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 243 ALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKT----FKRILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
403-590 |
4.56e-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: 78.98 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYtKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGmirkhsHVKIgryhqhlqeqLDLDL 482
Cdd:cd03230 3 VRNLSKRY-GKKTAL-DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG------EIKV----------LGKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 483 spleymmkcypeIKEKEEMRKIIGrY---------GLTGKQQVspirNLSDGQKCRVCLAwlawQ----NPHMLFLDEPT 549
Cdd:cd03230 65 ------------KKEPEEVKRRIG-YlpeepslyeNLTVRENL----KLSGGMKQRLALA----QallhDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23956078 550 NHLDIETIDALADAINEF--EGG-MMLVSHDFRLIQQVAQEIWV 590
Cdd:cd03230 124 SGLDPESRREFWELLRELkkEGKtILLSSHILEEAERLCDRVAI 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
403-590 |
5.93e-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: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigryhqHLQEQLDLDL 482
Cdd:cd03214 2 VENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------------LLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 483 SPLE------YMmkcyPEIKEKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI-- 554
Cdd:cd03214 67 SPKElarkiaYV----PQALELLGLAHLADR----------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIah 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 23956078 555 --ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:cd03214 133 qiELLELLRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
95-308 |
1.21e-16 |
|
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: 78.25 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIY-HLTREMPPSEKTPLQCVMEvdte 173
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDgKDLASLSPKELARKIAYVP---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 174 RAMLEREAERLAHEDaecekLMELyerleeldadkaemrasrilhglgftpamqrkklkdfSGGWRMRVALARALFIRPF 253
Cdd:cd03214 80 QALELLGLAHLADRP-----FNEL-------------------------------------SGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 254 MLLLDEPTNHLDLDACVWLEEELKTFKR----ILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
401-596 |
2.09e-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: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhlqeqLD- 479
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----------------LDg 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 480 LDLSPLeymmkcypeikEKEEMRKIIGryglTGKQQV-----SPIRN-LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:cd03246 64 ADISQW-----------DPNELGDHVG----YLPQDDelfsgSIAENiLSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23956078 554 IETIDALADAINEFEGGM---MLVSHDFRLIQQvAQEIWVCEKQTI 596
Cdd:cd03246 129 VEGERALNQAIAALKAAGatrIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
403-585 |
9.63e-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: 76.14 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVK-----IGRYHQHL 474
Cdd:cd03226 2 IENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKerrksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 475 QEQLDLD--LSPLEYMMKCYPEikEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHL 552
Cdd:cd03226 81 DYQLFTDsvREELLLGLKELDA--GNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 23956078 553 DIETIDALADAINEF--EGGMMLV-SHDFRLIQQVA 585
Cdd:cd03226 158 DYKNMERVGELIRELaaQGKAVIViTHDYEFLAKVC 193
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
401-588 |
1.07e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 76.64 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDgpCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHvkigRYHQH 473
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvaRDPA----EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 L----QE-QLDLDLSP---LEYMMKCY--PEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAwLA-WQNPHM 542
Cdd:COG1131 75 IgyvpQEpALYPDLTVrenLRFFARLYglPRKEARERIDELLELFGLTDAAD-RKVGTLSGGMKQRLGLA-LAlLHDPEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23956078 543 LFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEI 588
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELaAEGKtvLLSTHYLEEAERLCDRV 201
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
105-386 |
1.17e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 80.60 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 105 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTR---------EMPPSEKTPLQcvmevdtera 175
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKlgyfaqhqlEFLRADESPLQ---------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 176 MLEREAERlahedaECEKLMELYerleeldadkaemrasriLHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFML 255
Cdd:PRK10636 397 HLARLAPQ------ELEQKLRDY------------------LGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 256 LLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHW 335
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEA 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 336 EQDQIAH-------MKNYIARFGHGSAKLARQAQSKEKTLQKMMA--SGLTERvVSDKTL 386
Cdd:PRK10636 533 PKENNANsaqarkdQKRREAELRTQTQPLRKEIARLEKEMEKLNAqlAQAEEK-LGDSEL 591
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
89-309 |
1.68e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 89 TDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI----YHLTR----EMPPSE 160
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtINLVRdkdgQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 161 KTPLQCVMevdTERAMLEREAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRM 240
Cdd:PRK10619 84 KNQLRLLR---TRLTMVFQHFNLWSHMTV-LENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 241 RVALARALFIRPFMLLLDEPTNHLD-------LDACVWLEEELKTfkriLVLVSHSQDFLNGVCTNIIHMHNKKLK 309
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDpelvgevLRIMQQLAEEGKT----MVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
400-588 |
1.84e-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: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkHSHVKIGRYHQHLQEQ-- 477
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIL-IDGEDVRKEPREARRQig 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 478 -------LDLDLSPLEYMMKCYP-------EIKEKEEmrKIIGRYGLTGKqQVSPIRNLSDGQKCRVCLAWLAWQNPHML 543
Cdd:COG4555 78 vlpdergLYDRLTVRENIRYFAElyglfdeELKKRIE--ELIELLGLEEF-LDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23956078 544 FLDEPTNHLDIETIDALADAINEF--EGGMMLVS-HDFRLIQQVAQEI 588
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRV 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
95-308 |
2.30e-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: 75.33 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVPIPEHIDIYHLTREMPpsektplqc 166
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlglikpdsGEITFDGKSYQKNIEALRRIG--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 167 vmevdterAMLEREA---ERLAHEDaeceklMELYERLeeldADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVA 243
Cdd:cd03268 76 --------ALIEAPGfypNLTAREN------LRLLARL----LGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 244 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLV-SHSQDFLNGVCTNIIHMHNKKL 308
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
91-310 |
4.81e-15 |
|
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: 74.68 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQ-ELLSDTKLELNSGRRYGLIGLNGIGKSMLLsaigkrevpipehidiYHLTREMPPSEKTPLqcVME 169
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLL----------------RLLNGLLKPTSGEVL--VDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 170 VDTERAMLEREAER--LAHEDAEceklMELYER--LEE---------LDADKAEMRASRILHGLGFTPAMQRK--KLkdf 234
Cdd:COG1122 63 KDITKKNLRELRRKvgLVFQNPD----DQLFAPtvEEDvafgpenlgLPREEIRERVEEALELVGLEHLADRPphEL--- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKKLKY 310
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
400-590 |
8.31e-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: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRY-- 470
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaSLSRRELARRia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 --HQHLqeQLDLDLSPLEY-MMKCYPEIK----EKEEMRKIIGRY----GLTGKQQvSPIRNLSDGQKCRVCLAW-LAwQ 538
Cdd:COG1120 79 yvPQEP--PAPFGLTVRELvALGRYPHLGlfgrPSAEDREAVEEAlertGLEHLAD-RPVDELSGGERQRVLIARaLA-Q 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 539 NPHMLFLDEPTNHLDI----ETIDALADaINEFEG-GMMLVSHDFRLIQQVAQEIWV 590
Cdd:COG1120 155 EPPLLLLDEPTSHLDLahqlEVLELLRR-LARERGrTVVMVLHDLNLAARYADRLVL 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
420-597 |
2.61e-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: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 420 NLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHL---------QEQLDLDLSPLE--YM 488
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLrrigvvfgqKTQLWWDLPVIDsfYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 489 MKCYPEIKEKEEMRKIIGRYGLTGKQQV--SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI---ETIDALADA 563
Cdd:cd03267 119 LAAIYDLPPARFKKRLDELSELLDLEELldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKE 198
|
170 180 190
....*....|....*....|....*....|....*
gi 23956078 564 IN-EFEGGMMLVSHDFRLIQQVAQEIWVCEKQTIT 597
Cdd:cd03267 199 YNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
397-590 |
4.08e-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: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-----------KHSHV 465
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPAL-RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadaDSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 KIGRYHQH-------LQEQLDLDLspleymmkcyPEIKEkEEMRKIIGRYGLTGKQQVSPI----------RNLSDGQKC 528
Cdd:TIGR02857 397 QIAWVPQHpflfagtIAENIRLAR----------PDASD-AEIREALERAGLDEFVAALPQgldtpigeggAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 529 RVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDfRLIQQVAQEIWV 590
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHR-LALAALADRIVV 528
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
400-590 |
5.73e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.46 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-----------KHSHVKIG 468
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 469 RYHQHLQEQL-------DLDLSPLEyMMKCYPEIKEK-EEMRKIIGRYGLTGKqqvsPIRNLSDGQKCRVCLAWLAWQNP 540
Cdd:PRK13647 83 LVFQDPDDQVfsstvwdDVAFGPVN-MGLDKDEVERRvEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23956078 541 HMLFLDEPTNHLD---IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:PRK13647 158 DVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
398-597 |
7.48e-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: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 398 PPVIMVQNVSFKYTKDGPcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR----KHSHVKIGRYHQH 473
Cdd:COG4988 334 PPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 --------------LQEQLDL---DLSPleymmkcypeikekEEMRKIIGRYGLTG-----KQQV-SPI----RNLSDGQ 526
Cdd:COG4988 413 iawvpqnpylfagtIRENLRLgrpDASD--------------EELEAALEAAGLDEfvaalPDGLdTPLgeggRGLSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 527 KCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEKQTIT 597
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 ... |
92-309 |
7.71e-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: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrevpipehidiyhLTREM---------PPSEK 161
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-------------LIKESsgsillngkPIKAK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 162 TPLQC---VMEvDTERAMLEREAERlahedaeceklmELYERLEELDADKAemRASRILHGLGFTPAMQRKKLkDFSGGW 238
Cdd:cd03226 68 ERRKSigyVMQ-DVDYQLFTDSVRE------------ELLLGLKELDAGNE--QAETVLKDLDLYALKERHPL-SLSGGQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 239 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLK 309
Cdd:cd03226 132 KQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGElirELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
93-305 |
9.66e-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: 71.37 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTF----HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKREVPiPEHIDIYHLTREMPPSEKTPLQCVM 168
Cdd:COG1124 4 VRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRAL-AGLER-PWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 169 EV---DTERAMLEREaeRLAHEDAECEKLMELYERLEeldadkaemRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALA 245
Cdd:COG1124 82 QMvfqDPYASLHPRH--TVDRILAEPLRIHGLPDREE---------RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 246 RALFIRPFMLLLDEPTNHLDL--DACVW--LEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHN 305
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVsvQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
95-303 |
1.34e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMPPSEKTPLqcVMEVDT 172
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgdITIDTARSLSQQKGL--IRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 ERAMLEREAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRP 252
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTV-LENIIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 253 FMLLLDEPTNHLD-------LDACVWLEEElktfKRILVLVSHSQDFLNGVCTNIIHM 303
Cdd:PRK11264 164 EVILFDEPTSALDpelvgevLNTIRQLAQE----KRTMVIVTHEMSFARDVADRAIFM 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
91-304 |
1.36e-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: 70.25 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-----IPEHIDIYHltremppsektPLQ 165
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdsgtiIIDGLKLTD-----------DKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 CVMEVDTERAMLEREAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFtPAMQRKKLKDFSGGWRMRVALA 245
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTV-LENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 246 RALFIRPFMLLLDEPTNHLD-------LDACVWLEEELKTfkriLVLVSHSQDFLNGVCTNIIHMH 304
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDpelvgevLDVMKDLAEEGMT----MVVVTHEMGFAREVADRVIFMD 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
95-311 |
1.58e-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: 69.87 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHI----DIYHLTREM 156
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkptsgsirvfGKPLEKERKRIgyvpQRRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 157 PPSektplqcVMEVdterAMLEREAE-----RLAHEDaeCEKLMELYERLeeldadkaemrasrilhGLGftpAMQRKKL 231
Cdd:cd03235 84 PIS-------VRDV----VLMGLYGHkglfrRLSKAD--KAKVDEALERV-----------------GLS---ELADRQI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 232 KDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAC---VWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMhNKKL 308
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQediYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
...
gi 23956078 309 KYY 311
Cdd:cd03235 210 VAS 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
91-310 |
1.77e-13 |
|
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: 69.91 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRrYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPSEKTplqcvMEV 170
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRIL----------------ATLTPPSSGT-----IRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREAERlAH-----EDAECEKLMELYE------RLEELDADKAEMRASRILHGLGFTPAmQRKKLKDFSGGWR 239
Cdd:cd03264 59 DGQDVLKQPQKLR-RRigylpQEFGVYPNFTVREfldyiaWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 240 MRVALARALFIRPFMLLLDEPTNHLDldacvwlEEELKTFKRIL--------VLVS-HSQDFLNGVCTNIIHMHNKKLKY 310
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLD-------PEERIRFRNLLselgedriVILStHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
433-596 |
2.06e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 433 LVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSpLEYMMKCYPEIKeKEEMRKIIGRYGlTG 512
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLT-VNRFLRLRPGTK-KEDILPALKRVQ-AG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 513 KQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAIN----EFEGGMMLVSHDFRLIQQVAQEI 588
Cdd:PRK09544 112 HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDqlrrELDCAVLMVSHDLHLVMAKTDEV 191
|
....*...
gi 23956078 589 wVCEKQTI 596
Cdd:PRK09544 192 -LCLNHHI 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
95-266 |
2.50e-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: 70.07 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTRE--------MPPSEK 161
Cdd:COG1120 6 NLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrDLASLSRRelarriayVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 162 TPLQC-VMEVdterAMLEReaerLAHedaeceklMELYERLEELDADKAE--MRASRILHglgftpaMQRKKLKDFSGGW 238
Cdd:COG1120 86 APFGLtVREL----VALGR----YPH--------LGLFGRPSAEDREAVEeaLERTGLEH-------LADRPVDELSGGE 142
|
170 180
....*....|....*....|....*...
gi 23956078 239 RMRVALARALFIRPFMLLLDEPTNHLDL 266
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
92-303 |
2.59e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.77 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTF-----HGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREmppsektpl 164
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGW--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 qcvmeVD----TERAMLE-REAE------------RLAHEDAECEKLMELyerleELDADKAEMRASRILHGLGFtpamq 227
Cdd:COG4778 77 -----VDlaqaSPREILAlRRRTigyvsqflrvipRVSALDVVAEPLLER-----GVDREEARARARELLARLNL----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 228 RKKLKD-----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDL---DACVWLEEELKTFKRILVLVSHSQDFLNGVCTN 299
Cdd:COG4778 142 PERLWDlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
....
gi 23956078 300 IIHM 303
Cdd:COG4778 222 VVDV 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
102-289 |
2.71e-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: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GKREVPIPEH-IDIYHLTrEMPPSEKTPLQCVMEvdtERAML-- 177
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLDPLQGEVtLDGVPVS-SLDQDEVRRRVSVCA---QDAHLfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 178 --EREAERLAHEDAECEKLMELYER--LEELdadkaemrASRILHGLGfTPAMQRKKLkdFSGGWRMRVALARALFIRPF 253
Cdd:TIGR02868 423 ttVRENLRLARPDATDEELWAALERvgLADW--------LRALPDGLD-TVLGEGGAR--LSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 23956078 254 MLLLDEPTNHLDLDACVWLEEEL--KTFKRILVLVSHS 289
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLlaALSGRTVVLITHH 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
403-590 |
4.17e-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: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkIGRY------HQHLQE 476
Cdd:COG2274 476 LENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL------IDGIdlrqidPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 477 QL-----DLDL---SPLEYMMKCYPEIkEKEEMRKIIGRYGLTG---------KQQVSPI-RNLSDGQKCRVCLA--WLa 536
Cdd:COG2274 550 QIgvvlqDVFLfsgTIRENITLGDPDA-TDEEIIEAARLAGLHDfiealpmgyDTVVGEGgSNLSGGQRQRLAIAraLL- 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 537 wQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWV 590
Cdd:COG2274 628 -RNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRL-ADRIIV 681
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
100-305 |
5.26e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 100 FHG-QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMPPSEKTPLQCVMEVdterAM 176
Cdd:PRK11124 11 FYGaHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSDKAIRELRRNV----GM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 177 LEREAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARALFIRPFMLL 256
Cdd:PRK11124 87 VFQQYNLWPHLTV-QQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23956078 257 LDEPTNHLDLD---ACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHN 305
Cdd:PRK11124 165 FDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
103-308 |
6.55e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 69.06 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 103 QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSEKTPLQCVMEvDTERAML 177
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqDLYQLDRKQRRAFRRDVQLVFQ-DSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 178 EREAERlahedaecEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLL 257
Cdd:TIGR02769 103 PRMTVR--------QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 258 DEPTNHLDL----DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:TIGR02769 175 DEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
398-576 |
9.68e-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: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 398 PPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGM----------------IRK 461
Cdd:COG1119 1 DPLLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 462 HshvkIGRYHQHLQEQLDLDLSPLE------Y-MMKCYPEIKEKEEMR--KIIGRYGLTGKQQvSPIRNLSDGQKCRVCL 532
Cdd:COG1119 79 R----IGLVSPALQLRFPRDETVLDvvlsgfFdSIGLYREPTDEQRERarELLELLGLAHLAD-RPFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 533 --AWLAwqNPHMLFLDEPTNHLD-------IETIDALADainefEGG--MMLVSH 576
Cdd:COG1119 154 arALVK--DPELLILDEPTAGLDlgarellLALLDKLAA-----EGAptLVLVTH 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
116-310 |
1.23e-12 |
|
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: 67.39 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 116 GRRYGLIGLNGIGKS----MLLSAI----GKREVpipEHIDIYHLTREMppsektpLQCVMEVDTERAMLEREAERlahe 187
Cdd:cd03266 31 GEVTGLLGPNGAGKTttlrMLAGLLepdaGFATV---DGFDVVKEPAEA-------RRRLGFVSDSTGLYDRLTAR---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 188 daeceKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLD 267
Cdd:cd03266 97 -----ENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRR-VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23956078 268 ACVWLEEELKTFKRI---LVLVSHSQDFLNGVCTNIIHMHNKKLKY 310
Cdd:cd03266 171 ATRALREFIRQLRALgkcILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
433-592 |
1.30e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 433 LVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGrYHQhlQE-QLDLDLSPLEYMMKCYPEIKEK------------- 498
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVG-YLP--QEpQLDPEKTVRENVEEGVAEVKAAldrfneiyaayae 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 499 --EEMRKIIGRYG-LTGK----------QQV-------------SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHL 552
Cdd:PRK11819 115 pdADFDALAAEQGeLQEIidaadawdldSQLeiamdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23956078 553 DIETIDALADAINEFEGGMMLVSHDFRLIQQVAQeiWVCE 592
Cdd:PRK11819 195 DAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
93-308 |
1.72e-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: 67.15 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVpipEHIDIYHLTREMPPSE 160
Cdd:cd03257 4 VKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsGSIIF---DGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 161 KTPLQCV-----------MEVdteramleREAerlahedaecekLMELYERLEELDADKA-EMRASRILHGLGFTPAMQR 228
Cdd:cd03257 81 RKEIQMVfqdpmsslnprMTI--------GEQ------------IAEPLRIHGKLSKKEArKEAVLLLLVGVGLPEEVLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 229 KKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLD--ACVwleeeLKTFKRI-------LVLVSHSQDFLNGVCTN 299
Cdd:cd03257 141 RYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSvqAQI-----LDLLKKLqeelgltLLFITHDLGVVAKIADR 215
|
....*....
gi 23956078 300 IIHMHNKKL 308
Cdd:cd03257 216 VAVMYAGKI 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
95-308 |
2.46e-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: 66.46 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIyhltREMPPSE-KTPLQC 166
Cdd:cd03245 7 NVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtDI----RQLDPADlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 167 VMEVDTERAMLEREAERLAHEDAECEKLMELYER--LEELDADkaemrasrilHGLGFtpAMQ-RKKLKDFSGGWRMRVA 243
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELagVTDFVNK----------HPNGL--DLQiGERGRGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 244 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK--RILVLVSHSQDFLNgVCTNIIHMHNKKL 308
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
424-577 |
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 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYM-MKCYPEI--- 495
Cdd:NF040873 10 GVDLTIPagslTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVaMGRWARRglw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 496 -KEKEEMRKIIG----RYGLTGkQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEG- 569
Cdd:NF040873 90 rRLTRDDRAAVDdaleRVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
|
170
....*....|
gi 23956078 570 --GMMLVSHD 577
Cdd:NF040873 169 gaTVVVVTHD 178
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
221-332 |
2.73e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 221 GFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNI 300
Cdd:PRK11819 433 NFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI 512
|
90 100 110
....*....|....*....|....*....|...
gi 23956078 301 IHMH-NKKLKYYTGNYDQYvktrlelEENQMKR 332
Cdd:PRK11819 513 LAFEgDSQVEWFEGNFQEY-------EEDKKRR 538
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
234-288 |
3.44e-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: 3.44e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSH 288
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAH 154
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
400-593 |
3.91e-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: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------KHSHV----- 465
Cdd:COG2884 1 MIRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 KIGRYHQ--HLqeqLDlDLS-------PLEYMMKCYPEIKEKeeMRKIIGRYGLTGKQQVSPIrNLSDGQKCRVCLAwla 536
Cdd:COG2884 80 RIGVVFQdfRL---LP-DRTvyenvalPLRVTGKSRKEIRRR--VREVLDLVGLSDKAKALPH-ELSGGEQQRVAIAral 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 537 wqNPHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLV-SHDFRLIQQVAQEIWVCEK 593
Cdd:COG2884 153 vnRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLELED 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
371-593 |
5.17e-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: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 371 MMASGLTERVVS--DKTLSFyfPPCGKIPPP----VIMVQNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKST 443
Cdd:TIGR00958 445 MQAVGASEKVFEylDRKPNI--PLTGTLAPLnlegLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 444 LLKLLTGELLPTDGM-------IRKHSHVkigRYHQHL----QEQL------------DLDLSPLEYMMK------CYPE 494
Cdd:TIGR00958 523 VAALLQNLYQPTGGQvlldgvpLVQYDHH---YLHRQValvgQEPVlfsgsvreniayGLTDTPDEEIMAaakaanAHDF 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 495 IKEKEEmrKIIGRYGLTGKQqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLV 574
Cdd:TIGR00958 600 IMEFPN--GYDTEVGEKGSQ-------LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLI 670
|
250
....*....|....*....
gi 23956078 575 SHDFRLIQQvAQEIWVCEK 593
Cdd:TIGR00958 671 AHRLSTVER-ADQILVLKK 688
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
91-308 |
6.13e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.80 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREMPPSEKTPLQCVM 168
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 169 EVdterAMLEREAERLAHEDAEcEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARAL 248
Cdd:COG4161 83 KV----GMVFQQYNLWPHLTVM-ENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 249 FIRPFMLLLDEPTNHLD---LDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:COG4161 157 MMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
401-584 |
6.38e-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: 65.30 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKHshv 465
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpadlRRN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 kIGRYHQH-------LQEQLDLDlspleymmkcYPEIKEKEEMR--KIIGRYGLTGKQ------QVSPI-RNLSDGQKCR 529
Cdd:cd03245 80 -IGYVPQDvtlfygtLRDNITLG----------APLADDERILRaaELAGVTDFVNKHpngldlQIGERgRGLSGGQRQA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 530 VCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQV 584
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLV 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
401-596 |
6.86e-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: 65.71 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH----VKIGRYHQHL-- 474
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdYTLASLRRQIgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 475 --QEQLDLDLSPLEYMMKCYPEIKEKEEMR-------------------KIIGRYGLtgkqqvspirNLSDGQKCRVCLA 533
Cdd:cd03251 81 vsQDVFLFNDTVAENIAYGRPGATREEVEEaaraanahefimelpegydTVIGERGV----------KLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 534 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEKQTI 596
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
399-590 |
7.30e-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: 68.01 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTgellptdGMIRKHSHVKiGRYHQHLQEQL 478
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM-------GLLPHGGRIS-GEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 479 DLDLS---------PLEYM-----MKCYPEIKE--------KEEMRKII----GRYGLTGKQQVSPIRnLSDGQKCRVCL 532
Cdd:COG1123 75 ELSEAlrgrrigmvFQDPMtqlnpVTVGDQIAEalenlglsRAEARARVlellEAVGLERRLDRYPHQ-LSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 533 AWLAWQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
65-288 |
7.62e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 65 LEDFE--MKKAAARAVTGVLASHPNSTDVHIINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI----- 136
Cdd:COG4178 335 LAGFEeaLEAADALPEAASRIETSEDGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwp 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 137 -GKREVPIPEHIDIYHLTRE--MPPsektplqcvmevDTERAMLEREAERLAHEDAECEKLME------LYERLEEldad 207
Cdd:COG4178 415 yGSGRIARPAGARVLFLPQRpyLPL------------GTLREALLYPATAEAFSDAELREALEavglghLAERLDE---- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 208 kaEMRASRILhglgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEEL-KTFKR----- 281
Cdd:COG4178 479 --EADWDQVL-----------------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN----EAALyQLLREelpgt 535
|
....*..
gi 23956078 282 ILVLVSH 288
Cdd:COG4178 536 TVISVGH 542
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
390-597 |
8.38e-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: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 390 FPPCGKIPP--PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------- 460
Cdd:COG4987 321 EPAEPAPAPggPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlr 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 461 ---------------KHSHV---------KIGRyhqhlqeqldldlspleymmkcyPEIKEkEEMRKIIGRYGL------ 510
Cdd:COG4987 401 dldeddlrrriavvpQRPHLfdttlrenlRLAR-----------------------PDATD-EELWAALERVGLgdwlaa 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 511 -----------TGkqqvspiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHD 577
Cdd:COG4987 457 lpdgldtwlgeGG-------RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHR 529
|
250 260
....*....|....*....|
gi 23956078 578 FRLIQQvAQEIWVCEKQTIT 597
Cdd:COG4987 530 LAGLER-MDRILVLEDGRIV 548
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
91-291 |
9.20e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 66.71 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GK-----REVPIpeHIDI-------- 149
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdsGRivlngRDLFT--NLPPrerrvgfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 150 ---Y----HLT---------REMPPSEktplqcvmevdteramleREAERLAHEdaecekLMELYErLEELdadkaemrA 213
Cdd:COG1118 81 fqhYalfpHMTvaeniafglRVRPPSK------------------AEIRARVEE------LLELVQ-LEGL--------A 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 214 SRILHGLgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHldLDACV------WLEEELKTFKRILVLVS 287
Cdd:COG1118 128 DRYPSQL--------------SGGQRQRVALARALAVEPEVLLLDEPFGA--LDAKVrkelrrWLRRLHDELGGTTVFVT 191
|
....
gi 23956078 288 HSQD 291
Cdd:COG1118 192 HDQE 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
395-553 |
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 23956078 395 KIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-----------KHS 463
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenlKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 HVKIGRYHQHLQEQL-------DLDLSpLEYmmKCYPeikeKEEMRKIIGRY----GLTGKQQVSPiRNLSDGQKCRVCL 532
Cdd:PRK13632 82 RKKIGIIFQNPDNQFigatvedDIAFG-LEN--KKVP----PKKMKDIIDDLakkvGMEDYLDKEP-QNLSGGQKQRVAI 153
|
170 180
....*....|....*....|.
gi 23956078 533 AWLAWQNPHMLFLDEPTNHLD 553
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLD 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
93-265 |
1.11e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHltreMPPSEKtPLQcv 167
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvDLSH----VPPYQR-PIN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 168 mevdteraMLEREAERLAHEDAECEKLMEL-YERL--EELDADKAEMRAsrILHGLGFTpamqRKKLKDFSGGWRMRVAL 244
Cdd:PRK11607 95 --------MMFQSYALFPHMTVEQNIAFGLkQDKLpkAEIASRVNEMLG--LVHMQEFA----KRKPHQLSGGQRQRVAL 160
|
170 180
....*....|....*....|.
gi 23956078 245 ARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALD 181
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
72-289 |
1.15e-11 |
|
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: 67.31 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 72 KAAARAVTGVLAS----HPNSTDV--------HIINLSLTFHGQ-ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigk 138
Cdd:TIGR02857 291 VAAAEALFAVLDAaprpLAGKAPVtaapasslEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNL--- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 139 revpipehidiyhLTREMPPSEKTPLqcVMEVDTERAMLEREAERLAH--------EDAECEKLmelyeRLEELDADKAE 210
Cdd:TIGR02857 368 -------------LLGFVDPTEGSIA--VNGVPLADADADSWRDQIAWvpqhpflfAGTIAENI-----RLARPDASDAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 211 MRASRILHGL-GFT---PAMQRKKLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK-- 280
Cdd:TIGR02857 428 IREALERAGLdEFVaalPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAqg 507
|
....*....
gi 23956078 281 RILVLVSHS 289
Cdd:TIGR02857 508 RTVLLVTHR 516
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
399-566 |
1.56e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKHs 463
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklRKH- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 hvkIGRYHQHLQEQ-----LDLDLS-PLEYMMKCYPEIKEKeeMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAW 537
Cdd:PRK13648 85 ---IGIVFQNPDNQfvgsiVKYDVAfGLENHAVPYDEMHRR--VSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLA 158
|
170 180
....*....|....*....|....*....
gi 23956078 538 QNPHMLFLDEPTNHLDIETIDALADAINE 566
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRK 187
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
102-268 |
1.79e-11 |
|
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: 64.84 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHL-TREMPPSEKTPLQCVME--VDTERAMLE 178
Cdd:TIGR03873 13 GRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdLHGLSRRARARRVALVEqdSDTAVPLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 179 REAERLAHEDaeceklmelYERLEELDADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLD 258
Cdd:TIGR03873 93 RDVVALGRIP---------HRSLWAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLD 162
|
170
....*....|
gi 23956078 259 EPTNHLDLDA 268
Cdd:TIGR03873 163 EPTNHLDVRA 172
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
72-308 |
2.17e-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: 66.71 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 72 KAAARAVTGVLASH-----------PNSTDVHII--NLSLTFH-GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIG 137
Cdd:COG4988 305 IAAAEKIFALLDAPepaapagtaplPAAGPPSIEleDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 138 KREVP------IpEHIDIYHLTREmppsekTPLQCVMEV--------DTERAMLereaeRLAHEDAeceklmelyerlee 203
Cdd:COG4988 385 GFLPPysgsilI-NGVDLSDLDPA------SWRRQIAWVpqnpylfaGTIRENL-----RLGRPDA-------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 204 ldaDKAEMRAsrilhglgftpAMQRKKLKDF-------------------SGGWRMRVALARALFIRPFMLLLDEPTNHL 264
Cdd:COG4988 439 ---SDEELEA-----------ALEAAGLDEFvaalpdgldtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 23956078 265 DLDAcvwlEEELKT-----FK-RILVLVSHSQDFLNgVCTNIIHMHNKKL 308
Cdd:COG4988 505 DAET----EAEILQalrrlAKgRTVILITHRLALLA-QADRILVLDDGRI 549
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
91-288 |
2.40e-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: 64.34 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI---------------GKR--EVPIPE---HIDIY 150
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlfGERrgGEDVWElrkRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 151 --HLTREMPPSEKtplqcVMEV------DTeramlereaerlahedaeceklMELYERLEELDADKAEmrasRILHGLGF 222
Cdd:COG1119 84 spALQLRFPRDET-----VLDVvlsgffDS----------------------IGLYREPTDEQRERAR----ELLELLGL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 223 TPAMQRKkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLeeeLKTFKRI-------LVLVSH 288
Cdd:COG1119 133 AHLADRP-FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELL---LALLDKLaaegaptLVLVTH 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
412-588 |
2.58e-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: 63.28 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 412 KDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVKIGRYHQHL-----QEQLDLDLS 483
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLlylghAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 484 PLEYmMKCYPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADA 563
Cdd:cd03231 90 VLEN-LRFWHADHSDEQVEEALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180
....*....|....*....|....*....
gi 23956078 564 INEF--EGGMMLVS--HDFRLIQQVAQEI 588
Cdd:cd03231 168 MAGHcaRGGMVVLTthQDLGLSEAGAREL 196
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
95-315 |
2.71e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLS-AIGKREvpiPEHIDIYHLTRemppsektplqcvMEV--- 170
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ---ADSGRIHCGTK-------------LEVayf 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREA---ERLAhedaeceklmelyerleelDADKAEMRASRILHGLG------FTPAMQRKKLKDFSGGWRMR 241
Cdd:PRK11147 388 DQHRAELDPEKtvmDNLA-------------------EGKQEVMVNGRPRHVLGylqdflFHPKRAMTPVKALSGGERNR 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 242 VALARaLFIRPFMLL-LDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFL-NGVCTNIIHMHNKKLKYYTGNY 315
Cdd:PRK11147 449 LLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGGY 523
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
400-597 |
2.87e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.44 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG--MIRKHSHVK---------IG 468
Cdd:PRK13652 3 LIETRDLCYSYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvLIRGEPITKenirevrkfVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 469 RYHQHLQEQL-------DLDLSPLEYMMKcypEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPH 541
Cdd:PRK13652 82 LVFQNPDDQIfsptveqDIAFGPINLGLD---EETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 542 MLFLDEPTNHLDIETIDALADAINEF--EGGMMLV--SHDFRLIQQVAQEIWVCEKQTIT 597
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIfsTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
401-581 |
4.04e-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: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKH----SHVK---IGRYHQH 473
Cdd:cd03292 1 IEFINVTKTYPNGTAAL-DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 L----QE-QLDLDLS-------PLEYMMKCYPEIKEKEEMrkIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPH 541
Cdd:cd03292 80 IgvvfQDfRLLPDRNvyenvafALEVTGVPPREIRKRVPA--ALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23956078 542 MLFLDEPTNHLDIETIDALADAINEFE--GGMMLVS-HDFRLI 581
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELV 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
424-596 |
4.22e-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: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRYHQHLQ---EQLDL--DLSPLEYM 488
Cdd:cd03262 18 GIDLTVKkgevVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglklTDDKKNINELRQKVGmvfQQFNLfpHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 489 M------KCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALAD 562
Cdd:cd03262 98 TlapikvKGMSKAEAEERALELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 23956078 563 AINEF--EG-GMMLVSHDFRLIQQVAQEIWVCEKQTI 596
Cdd:cd03262 177 VMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
424-624 |
5.24e-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: 63.95 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDG--------MIRKHSHVK--IGRYHQhlQEQLDLDLSPLEYMM 489
Cdd:TIGR01188 11 GVNFKVRegevFGFLGPNGAGKTTTIRMLTTLLRPTSGtarvagydVVREPRKVRrsIGIVPQ--YASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 490 KC-----YPEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 564
Cdd:TIGR01188 89 MMgrlygLPKDEAEERAEELLELFELGEAAD-RPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 565 NEF-EGGM--MLVSHDFRLIQQVAQEIWVCEKqtitkwpGDILAYK--EHLKSKLVDEEPQLTKR 624
Cdd:TIGR01188 168 RALkEEGVtiLLTTHYMEEADKLCDRIAIIDH-------GRIIAEGtpEELKRRLGKDTLESRPR 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
419-590 |
5.41e-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: 62.84 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 419 NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------------KHSHVKIGRYHQHLqeQLDLDLSPLE 486
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglpphEIARLGIGRTFQIP--RLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 487 YMM---------------KCYPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPT-- 549
Cdd:cd03219 95 NVMvaaqartgsglllarARREEREARERAEELLERVGLADLADR-PAGELSYGQQRRLEIARALATDPKLLLLDEPAag 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23956078 550 -NHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:cd03219 174 lNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
91-308 |
5.55e-11 |
|
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: 62.90 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTrempPSEKTPLQ 165
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgeDISGLS----EAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 CVMevdterAMLEREAerlAHEDAeceklMELYE----RLEELDADKAEMRASRILHGLGFT--PAMQRKKLKDFSGGWR 239
Cdd:cd03261 77 RRM------GMLFQSG---ALFDS-----LTVFEnvafPLREHTRLSEEEIREIVLEKLEAVglRGAEDLYPAELSGGMK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 240 MRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
424-585 |
6.67e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR------------KHSHVKIGRYHQHL----QeqlDLDLS 483
Cdd:PRK11264 21 GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslSQQKGLIRQLRQHVgfvfQ---NFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 484 P----LEYMMKCyPEIKEKEEM-------RKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHL 552
Cdd:PRK11264 98 PhrtvLENIIEG-PVIVKGEPKeeataraRELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23956078 553 DIE-------TIDALAdainEFEGGMMLVSHDFRLIQQVA 585
Cdd:PRK11264 176 DPElvgevlnTIRQLA----QEKRTMVIVTHEMSFARDVA 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
95-308 |
7.33e-11 |
|
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: 62.12 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-----IPEHIDIYHLTremppsektplq 165
Cdd:cd03255 5 NLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtsgevRVDGTDISKLS------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 cvmevDTERAMLERE------------AERLAHEDAEceklmeLYERLEELDADKAEMRASRILHGLGFTPAMQRK--KL 231
Cdd:cd03255 73 -----EKELAAFRRRhigfvfqsfnllPDLTALENVE------LPLLLAGVPKKERRERAEELLERVGLGDRLNHYpsEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 232 kdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAC--VW--LEEELKTFKRILVLVSHSQDfLNGVCTNIIHMHNKK 307
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkeVMelLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGK 217
|
.
gi 23956078 308 L 308
Cdd:cd03255 218 I 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
425-593 |
9.03e-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: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 425 IDLDT---RVALVGPNGAGKSTLLKLLTGELLPTDGMI----------RKHSHV-----KIGRYHQHLQEQLDLDL-SPL 485
Cdd:cd03297 17 IDFDLneeVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLppqqrKIGLVFQQYALFPHLNVrENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 486 EYMMKCYPEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAIN 565
Cdd:cd03297 97 AFGLKRKRNREDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|..
gi 23956078 566 E----FEGGMMLVSHDFRLIQQVAQEIWVCEK 593
Cdd:cd03297 176 QikknLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
72-288 |
1.16e-10 |
|
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: 64.40 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 72 KAAARAVTGVL------------ASHPNSTDVHIINLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAig 137
Cdd:COG4987 303 RAAARRLNELLdappavtepaepAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 138 krevpipehidiyhLTREMPPSE------KTPLQCVMEVDTER--AMLEREAE----------RLAHEDAECEKLME--- 196
Cdd:COG4987 381 --------------LLRFLDPQSgsitlgGVDLRDLDEDDLRRriAVVPQRPHlfdttlrenlRLARPDATDEELWAale 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 197 ------LYERLEE-LDAdkaemrasrILHGLGFTpamqrkklkdFSGGWRMRVALARALFIRPFMLLLDEPTNHLD-LDA 268
Cdd:COG4987 447 rvglgdWLAALPDgLDT---------WLGEGGRR----------LSGGERRRLALARALLRDAPILLLDEPTEGLDaATE 507
|
250 260
....*....|....*....|.
gi 23956078 269 CVWLEEELKTFK-RILVLVSH 288
Cdd:COG4987 508 QALLADLLEALAgRTVLLITH 528
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
95-305 |
1.37e-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: 61.68 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHiDIYHL-------- 152
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgflrptsgsvlfdGEDITGLPPH-EIARLgigrtfqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 153 TREMPpsEKTPLQCVM---EVDTERAMLEREAERlaHEDAECEKLMELYERLEeLdADKAEMRASRILHGlgftpamQRK 229
Cdd:cd03219 84 PRLFP--ELTVLENVMvaaQARTGSGLLLARARR--EEREARERAEELLERVG-L-ADLADRPAGELSYG-------QQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 230 klkdfsggwrmRVALARALFIRPFMLLLDEPT---NHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHN 305
Cdd:cd03219 151 -----------RLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
90-330 |
1.80e-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: 64.08 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 90 DVHIINLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP---------IP-EHIDIYHLTRemp 157
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtsgrilidgIDlRQIDPASLRR--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 158 psektplQCVMeVDTERAMLE---REAERLAHEDAEceklmelyerLEELdadkaeMRASRILHGLGFTPAMQRK---KL 231
Cdd:COG2274 550 -------QIGV-VLQDVFLFSgtiRENITLGDPDAT----------DEEI------IEAARLAGLHDFIEALPMGydtVV 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 232 KD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEE----LKTFK--RILVLVSHSQDFLNgVCTNII 301
Cdd:COG2274 606 GEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAET----EAIilenLRRLLkgRTVIIIAHRLSTIR-LADRII 680
|
250 260 270
....*....|....*....|....*....|..
gi 23956078 302 HMHNKKLKyYTGNYDQYVKTR---LELEENQM 330
Cdd:COG2274 681 VLDKGRIV-EDGTHEELLARKglyAELVQQQL 711
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
410-588 |
1.82e-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: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 410 YTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---KHSHVKIGRYHQHL-----QEQLDLD 481
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngTPLAEQRDEPHENIlylghLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 482 LSPLE----YMMKCYPEIKEKEEMrkiIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETI 557
Cdd:TIGR01189 88 LSALEnlhfWAAIHGGAQRTIEDA---LAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|...
gi 23956078 558 DALADAINEF--EGGMMLVSHDFRLIQQVAQEI 588
Cdd:TIGR01189 164 ALLAGLLRAHlaRGGIVLLTTHQDLGLVEAREL 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
200-290 |
1.83e-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: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 200 RLEELDADKAEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF 279
Cdd:cd03300 98 RLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRL 176
|
90
....*....|....*
gi 23956078 280 KRIL----VLVSHSQ 290
Cdd:cd03300 177 QKELgitfVFVTHDQ 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
401-590 |
1.96e-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: 61.04 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDgpCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLtgellptDGMIRKHSHVKI-GRYHQHLQEQLD 479
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLL-------NRLNDLIPGAPDeGEVLLDGKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 480 LDLSPLEYMMK-------------------CYP----EIKEKEEMRKII----GRYGLTG--KQQVSPiRNLSDGQKCRV 530
Cdd:cd03260 72 LDVDVLELRRRvgmvfqkpnpfpgsiydnvAYGlrlhGIKLKEELDERVeealRKAALWDevKDRLHA-LGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 531 CLAwLAWQN-PHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:cd03260 151 CLA-RALANePEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAF 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
91-342 |
2.06e-10 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 61.26 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREV----PIPEHIDI-Y-----HL 152
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlgllpptsGTVRLfgkpPRRARRRIgYvpqraEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 153 TREMPPSektplqcVMEVdterAMLEREAE-----RLAHEDaeCEKLMELyerLEELDADKaemRASRILHGLgftpamq 227
Cdd:COG1121 87 DWDFPIT-------VRDV----VLMGRYGRrglfrRPSRAD--REAVDEA---LERVGLED---LADRPIGEL------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 228 rkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSHSQDFLNGVCTNIIHMh 304
Cdd:COG1121 141 -------SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDRVLLL- 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 23956078 305 NKKLkYYTGNYDQYVKtrlelEENQMKRFHWEQDQIAH 342
Cdd:COG1121 213 NRGL-VAHGPPEEVLT-----PENLSRAYGGPVALLAH 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
400-612 |
2.97e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------RKHSHV----K 466
Cdd:PRK13639 1 ILETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikyDKKSLLevrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 467 IGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQN 539
Cdd:PRK13639 80 VGIVFQNPDDQLfaptveeDVAFGPLNLGL---SKEEVEKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 540 PHMLFLDEPTNHLD---IETIDALADAINEfEGGMMLVS-HDFRLIQQVAQEIWVCEKQTITK--WPGDILAYKEHLKS 612
Cdd:PRK13639 156 PEIIVLDEPTSGLDpmgASQIMKLLYDLNK-EGITIIIStHDVDLVPVYADKVYVMSDGKIIKegTPKEVFSDIETIRK 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
401-556 |
3.20e-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: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH----VKIGRYHQH--- 473
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlalADPAWLRRQvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 -LQEQLDLDLSPLEYMMKCYP--EIKEKEEMRKIIGRYG-----------LTGKQQVSpirnLSDGQKCRVCLAWLAWQN 539
Cdd:cd03252 81 vLQENVLFNRSIRDNIALADPgmSMERVIEAAKLAGAHDfiselpegydtIVGEQGAG----LSGGQRQRIAIARALIHN 156
|
170
....*....|....*..
gi 23956078 540 PHMLFLDEPTNHLDIET 556
Cdd:cd03252 157 PRILIFDEATSALDYES 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
93-303 |
3.27e-10 |
|
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: 60.66 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGkREVPIPE---HIDIYHLTREMPPSEKT------ 162
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN-GLVEPTSgsvLIDGTDINKLKGKALRQlrrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 163 ---------PLQCVME---------VDTERAMLER--EAERlahEDAeceklmelYERLEELD-ADKAEMRASRIlhglg 221
Cdd:cd03256 82 mifqqfnliERLSVLEnvlsgrlgrRSTWRSLFGLfpKEEK---QRA--------LAALERVGlLDKAYQRADQL----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 222 ftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACvwlEEELKTFKRI------LVLVS-HSQDFLN 294
Cdd:cd03256 146 -------------SGGQQQRVAIARALMQQPKLILADEPVASLDPASS---RQVMDLLKRInreegiTVIVSlHQVDLAR 209
|
....*....
gi 23956078 295 GVCTNIIHM 303
Cdd:cd03256 210 EYADRIVGL 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
430-596 |
3.30e-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: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 430 RVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGRY-------------HQHLQEQLDLDLSPleyMMKCY 492
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingVDVTAAPPADRpvsmlfqennlfaHLTVEQNVGLGLSP---GLKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 493 PEikEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGG 570
Cdd:cd03298 103 AE--DRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETK 179
|
170 180
....*....|....*....|....*...
gi 23956078 571 M--MLVSHDFRLIQQVAQEIWVCEKQTI 596
Cdd:cd03298 180 MtvLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
95-308 |
3.65e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 60.08 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLlsaigkrevpipehidIYHLTREMPPSEKTP----LQCVMEV 170
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTT----------------IKMLTTLLKPTSGRAtvagHDVVREP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREAERLAHEDA-ECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALF 249
Cdd:cd03265 69 REVRRRIGIVFQDLSVDDElTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 250 IRPFMLLLDEPTNHLDLDA--CVW--LEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTraHVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
235-296 |
4.73e-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: 4.73e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD------LDACVwleEELKTFKRILVLVSHSQDFLNGV 296
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAI---RALKARGATVVVITHRPSLLAAV 533
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
95-311 |
5.40e-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: 59.62 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQelLSDTKLELN---SGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHL----TRE---MPPsektpl 164
Cdd:cd03297 1 MLCVDIEKR--LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKkinLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 qcvmevdTER--AMLEREAERLAHedaeceklMELYERLE----ELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGW 238
Cdd:cd03297 73 -------QQRkiGLVFQQYALFPH--------LNVRENLAfglkRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 239 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMHNKKLKYY 311
Cdd:cd03297 137 KQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
401-616 |
5.71e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGP----CIYNnLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV----------- 465
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferrALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 ----KIGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGLTGK-QQVSPIrNLSDGQKCRVCLA 533
Cdd:PRK13634 82 plrkKVGIVFQFPEHQLfeetvekDICFGPMNFGV---SEEDAKQKAREMIELVGLPEElLARSPF-ELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 534 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM--MLVSHDFRLIQQVAQEIWVCEKQTITKW--PGDILAYK 607
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLttVLVTHSMEDAARYADQIVVMHKGTVFLQgtPREIFADP 237
|
....*....
gi 23956078 608 EHLKSKLVD 616
Cdd:PRK13634 238 DELEAIGLD 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
430-588 |
6.16e-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: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 430 RVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQE---------QLDLDLSPLE--YMMKCYPEIKE- 497
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRigvvfgqrsQLWWDLPAIDsfRLLKAIYRIPDa 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 498 --KEEMRKIIGRYGLTGKQQVsPIRNLSDGQ--KCRVCLAWLawQNPHMLFLDEPTNHLDIETIDALADAINEF--EGG- 570
Cdd:COG4586 130 eyKKRLDELVELLDLGELLDT-PVRQLSLGQrmRCELAAALL--HRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGt 206
|
170
....*....|....*....
gi 23956078 571 -MMLVSHDFRLIQQVAQEI 588
Cdd:COG4586 207 tILLTSHDMDDIEALCDRV 225
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
91-303 |
7.77e-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: 59.33 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTF--HGQ-----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLtremppSEKTP 163
Cdd:TIGR02324 2 LEVEDLSKTFtlHQQggvrlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHE------GAWVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 164 LQCVmevdTERAMLE-REAE------------RLAHEDAECEKLMEL-YERleeldaDKAEMRASRILHGLGFTPAMQRK 229
Cdd:TIGR02324 76 LAQA----SPREVLEvRRKTigyvsqflrvipRVSALEVVAEPLLERgVPR------EAARARARELLARLNIPERLWHL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 230 KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL---DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHM 303
Cdd:TIGR02324 146 PPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVMDV 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
400-590 |
9.81e-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: 59.06 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI--------------RKHS 463
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 HVKIGRYHQHLQEQLDldlsPLeymMKCYPEIKE---------KEEMRKIIGRYGLTGKQQVSPIRN-----LSDGQKCR 529
Cdd:cd03257 81 RKEIQMVFQDPMSSLN----PR---MTIGEQIAEplrihgklsKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 530 VCLAW-LAwQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:cd03257 154 VAIARaLA-LNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
91-311 |
1.48e-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: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP------IPEHIDIYHLTREMP----- 157
Cdd:cd03263 1 LQIRNLTKTYKKGTKpaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtsgtayINGYSIRTDRKAARQslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 158 ------PSEKTPLQCvmevdteramlereaerlahedaeceklMELYERLEELDADKAEMRASRILHGLGFTPamQRKKL 231
Cdd:cd03263 81 pqfdalFDELTVREH----------------------------LRFYARLKGLPKSEIKEEVELLLRVLGLTD--KANKR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 232 -KDFSGGWRMRVALARALFIRPFMLLLDEPTnhLDLDAC----VW--LEEELKtfKRILVLVSHSQDFLNGVCTNIIHMH 304
Cdd:cd03263 131 aRTLSGGMKRKLSLAIALIGGPSVLLLDEPT--SGLDPAsrraIWdlILEVRK--GRSIILTTHSMDEAEALCDRIAIMS 206
|
....*..
gi 23956078 305 NKKLKYY 311
Cdd:cd03263 207 DGKLRCI 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
401-593 |
1.65e-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: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-KHSHVK---IGRYHQHL- 474
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILlDGVDIRdlnLRWLRSQIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 475 ---QEQLDLDLSPLEYMMKCYPEIKEKEEMR--------KII----GRY----GLTGKQqvspirnLSDGQKCRVCLAWL 535
Cdd:cd03249 81 lvsQEPVLFDGTIAENIRYGKPDATDEEVEEaakkanihDFImslpDGYdtlvGERGSQ-------LSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 536 AWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRL--IQQvAQEIWVCEK 593
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLstIRN-ADLIAVLQN 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
95-308 |
2.19e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.18 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVpipehIDIYHLTREmPPSEKTPLQCVMEVDTER 174
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE-----ITSGDLIVD-GLKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 175 AMLEREAERLAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFM 254
Cdd:PRK09493 80 GMVFQQFYLFPHLTA-LENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956078 255 LLLDEPTNHLD-------LDACVWLEEELKTfkriLVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:PRK09493 158 MLFDEPTSALDpelrhevLKVMQDLAEEGMT----MVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
95-266 |
2.22e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GkrEVPIPE-HIDIY-HLTREMPPSE--KTplqcvme 169
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsG--ELSPDSgEVRLNgRPLADWSPAElaRR------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 170 vdteRAMLeREAERLA-----HEDAEceklMELYERLEELDADKAEMRAsrilhglgftpAMQRKKLKDF--------SG 236
Cdd:PRK13548 78 ----RAVL-PQHSSLSfpftvEEVVA----MGRAPHGLSRAEDDALVAA-----------ALAQVDLAHLagrdypqlSG 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 23956078 237 GWRMRVALARAL------FIRPFMLLLDEPTNHLDL 266
Cdd:PRK13548 138 GEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
401-617 |
2.42e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCI---YNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------------KH 462
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 463 SHVKIGRYHQHLQEQL-------DLDLSPLEYmmkCYPEIKEKEEMRKIIGRYGLtgKQQV---SPIrNLSDGQKCRVCL 532
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfentvlkDVEFGPKNF---GFSEDEAKEKALKWLKKVGL--SEDLiskSPF-ELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 533 AWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHDFRLIQQVAQEIWVCEKQTITKW--PGDILAYK 607
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHasPKEIFSDK 236
|
250
....*....|
gi 23956078 608 EHLKSKLVDE 617
Cdd:PRK13641 237 EWLKKHYLDE 246
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
401-588 |
2.46e-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: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGR----- 469
Cdd:cd03268 1 LKTNDLTKTY-GKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyQKNIEALRRigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 470 ----YHQHLQEQLDLDLSPLEYMmkcypeiKEKEEMRKIIGRYGL--TGKQQVspiRNLSDGQKCRVCLAWLAWQNPHML 543
Cdd:cd03268 79 eapgFYPNLTARENLRLLARLLG-------IRKKRIDEVLDVVGLkdSAKKKV---KGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23956078 544 FLDEPTNHLDIETIDALADAI---NEFEGGMMLVSHDFRLIQQVAQEI 588
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELIlslRDQGITVLISSHLLSEIQKVADRI 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
400-626 |
2.51e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDGPCIYNNLeFGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR--------------- 460
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRAL-FDIDLEVKkgsyTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 461 KHSHVKIGRYHQHLQEQL-------DLDLSPLEYMMkcypeikEKEEMRKIIGR----YGLTGK-QQVSPIRnLSDGQKC 528
Cdd:PRK13643 80 KPVRKKVGVVFQFPESQLfeetvlkDVAFGPQNFGI-------PKEKAEKIAAEklemVGLADEfWEKSPFE-LSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 529 RVCLAWLAWQNPHMLFLDEPTNHLD----IETIDaLADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKW--PGD 602
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCgtPSD 230
|
250 260
....*....|....*....|....
gi 23956078 603 ILAYKEHLKSklvdEEPQLTKRTH 626
Cdd:PRK13643 231 VFQEVDFLKA----HELGVPKATH 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
98-310 |
2.79e-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: 57.50 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 98 LTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHL-TREMPPSEKtPLqcvmevdterAM 176
Cdd:cd03298 6 IRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdVTAAPPADR-PV----------SM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 177 LEREAERLAHEDAECEKLMELYERLEELDADKAEMRAsrILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLL 256
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEV--ALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956078 257 LDEPTNHLD-------LDACVWLEEELKTfkrILVLVSHSQDFLNGVCTNIIHMHNKKLKY 310
Cdd:cd03298 152 LDEPFAALDpalraemLDLVLDLHAETKM---TVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
200-308 |
3.22e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 57.36 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 200 RLEELDADKAEMRASRILHGLGFTPAMQRK--KLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDAcv 270
Cdd:COG1136 112 LLAGVSRKERRERARELLERVGLGDRLDHRpsQL---SGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL-- 186
|
90 100 110
....*....|....*....|....*....|....*...
gi 23956078 271 wLEEELKTFKRILVLVSHSQDFLNgVCTNIIHMHNKKL 308
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 ... |
401-581 |
3.35e-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: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR----KHSHVKIGRYHQHL-- 474
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgiDISTIPLEDLRSSLti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 475 --QE------QLDLDLSPleymmkcYPEIKEKEEMRKI-IGRYGLtgkqqvspirNLSDGQKCRVCLAWLAWQNPHMLFL 545
Cdd:cd03369 87 ipQDptlfsgTIRSNLDP-------FDEYSDEEIYGALrVSEGGL----------NLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 23956078 546 DEPTNHLDIETiDALADAI--NEFEGGMML-VSHDFRLI 581
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 ... |
401-593 |
3.52e-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: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQH-LQEQL- 478
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-DIREVTLDsLRRAIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 479 --------------------DLDLSPLEYMMKC-----YPEIKE-KEEMRKIIGRYGLtgkqqvspirNLSDGQKCRVCL 532
Cdd:cd03253 79 vvpqdtvlfndtigynirygRPDATDEEVIEAAkaaqiHDKIMRfPDGYDTIVGERGL----------KLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 533 AWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEK 593
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLSTIVN-ADKIIVLKD 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
91-308 |
3.59e-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: 57.73 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--------------------- 149
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpvqernvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 150 YHLTREMPPSEKTPLqcvmevdterAMLEREAERLAHEDAECEKLMELYE--RLEELdadkaemrASRILHGLgftpamq 227
Cdd:cd03296 83 YALFRHMTVFDNVAF----------GLRVKPRSERPPEAEIRAKVHELLKlvQLDWL--------ADRYPAQL------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 228 rkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHldLDACVwlEEELKTFKRIL--------VLVSHSQDFLNGVCTN 299
Cdd:cd03296 138 -------SGGQRQRVALARALAVEPKVLLLDEPFGA--LDAKV--RKELRRWLRRLhdelhvttVFVTHDQEEALEVADR 206
|
....*....
gi 23956078 300 IIHMHNKKL 308
Cdd:cd03296 207 VVVMNKGRI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
106-291 |
3.83e-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: 57.35 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIyhltREMPPsektplqcvmevdteramlERE 180
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkDI----TNLPP-------------------EKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 181 AERLAHEDAECEKLMELYERLE----ELDADKAEM--RASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARALFIRPFM 254
Cdd:cd03299 72 DISYVPQNYALFPHMTVYKNIAyglkKRKVDKKEIerKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23956078 255 LLLDEPTNHLDLDACVWLEEELKTFKR---ILVL-VSHSQD 291
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKefgVTVLhVTHDFE 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
95-289 |
4.42e-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: 57.19 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPE-----------------HIDIYHLTREM- 156
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkdiydlDVDVLELRRRVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 157 ------PPSEKTplqcVME--VDTERAMLEREAERLAHEDAECEKLMELYERLeeldADKaemrasriLHGLGFtpamqr 228
Cdd:cd03260 85 mvfqkpNPFPGS----IYDnvAYGLRLHGIKLKEELDERVEEALRKAALWDEV----KDR--------LHALGL------ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 229 kklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHS 289
Cdd:cd03260 143 ------SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
89-297 |
4.92e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.33 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 89 TDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKreVPIPEHIDIYHltREMPPSEKTPLQCVM 168
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFAR--LLTPQSGTVFL--GDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 169 EVdterAMLEREaeRLAHEDAECEKLME--------LYERLEELDADKAE--MRASRILHglgftpaMQRKKLKDFSGGW 238
Cdd:PRK11231 77 RL----ALLPQH--HLTPEGITVRELVAygrspwlsLWGRLSAEDNARVNqaMEQTRINH-------LADRRLTDLSGGQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 239 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVLVSHSqdfLNGVC 297
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRlmrELNTQGKTVVTVLHD---LNQAS 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
91-289 |
6.98e-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: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFH----GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREvpipehidiyhltremPPSEKTPL-- 164
Cdd:COG1116 8 LELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLE----------------KPTSGEVLvd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 -QCVMEVDTERAMLereaerlAHEDAecekLM---------ELYERLEELDADKAEMRASRILHGLGftpamqrkkLKDF 234
Cdd:COG1116 72 gKPVTGPGPDRGVV-------FQEPA----LLpwltvldnvALGLELRGVPKAERRERARELLELVG---------LAGF 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 235 --------SGGWRMRVALARALFIRPFMLLLDEPTNHLD----LDACVWLEEELKTFKRILVLVSHS 289
Cdd:COG1116 132 edayphqlSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
401-580 |
7.02e-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: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPC--IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRY- 470
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 HQHL----QeQLDL--DLSPLEY----MMKCYPEIKEKEEM-RKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAwQ 538
Cdd:cd03255 81 RRHIgfvfQ-SFNLlpDLTALENvelpLLLAGVPKKERRERaEELLERVGLGDRLNHYP-SELSGGQQQRVAIArALA-N 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23956078 539 NPHMLFLDEPTNHLDIET----IDALADaINEFEG-GMMLVSHDFRL 580
Cdd:cd03255 158 DPKIILADEPTGNLDSETgkevMELLRE-LNKEAGtTIVVVTHDPEL 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
203-265 |
8.37e-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: 8.37e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 203 ELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG4172 395 GLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
203-265 |
8.51e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 8.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 203 ELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK15134 395 TLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
95-266 |
8.77e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 56.66 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPSE------KTPLQ--C 166
Cdd:COG4559 6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKL----------------LTGELTPSSgevrlnGRPLAawS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 167 VMEVDTERAMLEREAE--------------RLAH--EDAECEKLMElyERLEELDADkaeMRASRILHGLgftpamqrkk 230
Cdd:COG4559 70 PWELARRRAVLPQHSSlafpftveevvalgRAPHgsSAAQDRQIVR--EALALVGLA---HLAGRSYQTL---------- 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23956078 231 lkdfSGGWRMRVALARAL-------FIRPFMLLLDEPTNHLDL 266
Cdd:COG4559 135 ----SGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
235-291 |
8.96e-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: 8.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELktfKRIL-------VLVSHSQD 291
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL---RRLQrelgitfIYVTHDQE 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
401-564 |
1.16e-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: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGRYHQH--- 473
Cdd:cd03254 3 IEFENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgIDIRDISRKSLRSMigv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 -LQEQLDLDLSPLEYMMKCYPEIKEKEEMR--KIIGRYGLTGK------QQVSPI-RNLSDGQKCRVCLAWLAWQNPHML 543
Cdd:cd03254 82 vLQDTFLFSGTIMENIRLGRPNATDEEVIEaaKEAGAHDFIMKlpngydTVLGENgGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180
....*....|....*....|.
gi 23956078 544 FLDEPTNHLDIETIDALADAI 564
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEAL 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
398-576 |
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 23956078 398 PPVIMVQNVSFkyTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH-------VKIGRY 470
Cdd:PRK13543 9 PPLLAAHALAF--SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 HQHLqEQLDLDLSPLEYM-MKCYPEIKEKEEM-RKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLaWQNPHMLF-LDE 547
Cdd:PRK13543 87 LGHL-PGLKADLSTLENLhFLCGLHGRRAKQMpGSALAIVGLAGYED-TLVRQLSAGQKKRLALARL-WLSPAPLWlLDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 23956078 548 PTNHLDIETIDALADAINEF---EGGMMLVSH 576
Cdd:PRK13543 164 PYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
404-593 |
1.23e-08 |
|
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: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 404 QNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-----------RKHSHVKIGRYH 471
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyeHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 472 QH-------LQEQLDLDLSPLEYMmkCYPEIKEKEEMRKIIGRY--------GLTGKQqvspirnLSDGQKCRVCLAWLA 536
Cdd:cd03248 95 QEpvlfarsLQDNIAYGLQSCSFE--CVKEAAQKAHAHSFISELasgydtevGEKGSQ-------LSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 537 WQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLVSHDFRLIQQvAQEIWVCEK 593
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDG 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
111-308 |
1.23e-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: 57.89 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 111 LELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVPIPEhiDIYHLTREMPPSEKTPLQCVmevdterAMLEREAE 182
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsGEVNVRVGD--EWVDMTKPGPDGRGRAKRYI-------GILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 183 RLAHEDAecekLMELYERLE-ELDADKAEMRASRILHGLGFTPAMQRKKLKDF----SGGWRMRVALARALFIRPFMLLL 257
Cdd:TIGR03269 376 LYPHRTV----LDNLTEAIGlELPDELARMKAVITLKMVGFDEEKAEEILDKYpdelSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 258 DEPTNHLD-------LDACVWLEEEL-KTFkrilVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:TIGR03269 452 DEPTGTMDpitkvdvTHSILKAREEMeQTF----IIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
200-289 |
1.42e-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: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 200 RLEELDADKAEMRASRILHGLGftpamqrkkLKDF--------SGGWRMRVALARALFIRPFMLLLDEPTNHLD----LD 267
Cdd:cd03293 99 ELQGVPKAEARERAEELLELVG---------LSGFenayphqlSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQ 169
|
90 100
....*....|....*....|..
gi 23956078 268 ACVWLEEELKTFKRILVLVSHS 289
Cdd:cd03293 170 LQEELLDIWRETGKTVLLVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
91-308 |
1.51e-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: 55.76 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLsaigKrevpipehidiyHLTREMPPSEKTplqcvMEV 170
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLL----K------------LIIGLLRPDSGE-----ILV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTER--AMLEREAERLAHE-----------DAeceklMELYE----RLEE---LDADKAEMRASRILH--GLgftPAMQR 228
Cdd:COG1127 65 DGQDitGLSEKELYELRRRigmlfqggalfDS-----LTVFEnvafPLREhtdLSEAEIRELVLEKLElvGL---PGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 229 KKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMH 304
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLA 216
|
....
gi 23956078 305 NKKL 308
Cdd:COG1127 217 DGKI 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
432-555 |
1.57e-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: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 432 ALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQHLQEQL-----DLDLSP-------LEYM--MKCYPEIKE 497
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ-DVLKQPQKLRRRIgylpqEFGVYPnftvrefLDYIawLKGIPSKEV 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 498 KEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIE 555
Cdd:cd03264 108 KARVDEVLELVNLGDRAK-KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
401-588 |
1.61e-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: 55.65 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKHSHv 465
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalRQLRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 KIGRYHQHLQ--EQLDL----------DLSPLEYMMKCYPEIkEKEEMRKIIGRYGLTGK--QQVSpirNLSDGQKCRVC 531
Cdd:cd03256 79 QIGMIFQQFNliERLSVlenvlsgrlgRRSTWRSLFGLFPKE-EKQRALAALERVGLLDKayQRAD---QLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 532 LAWLAWQNPHMLFLDEPTNHLDIET----IDALADaINEFEGGMMLVS-HDFRLIQQVAQEI 588
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsrqvMDLLKR-INREEGITVIVSlHQVDLAREYADRI 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
201-308 |
1.67e-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: 55.52 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 201 LEELDADKAEMRASRILH--GLGftpamQR-----KKLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------L 266
Cdd:COG4181 115 LELAGRRDARARARALLErvGLG-----HRldhypAQL---SGGEQQRVALARAFATEPAILFADEPTGNLDaatgeqiI 186
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 23956078 267 DACVWLEEELKTfkrILVLVSHSQDfLNGVCTNIIHMHNKKL 308
Cdd:COG4181 187 DLLFELNRERGT---TLVLVTHDPA-LAARCDRVLRLRAGRL 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
431-594 |
1.77e-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: 55.49 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDGMIR--------KHSHVKI---GRYHQHLQEQLDLDLSPLEYMMkcypEIKEKE 499
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEieldtvsyKPQYIKAdyeGTVRDLLSSITKDFYTHPYFKT----EIAKPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 500 EMRKIIgrygltgKQQVspiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF----EGGMMLVS 575
Cdd:cd03237 104 QIEQIL-------DREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVE 173
|
170
....*....|....*....
gi 23956078 576 HDFRLIQQVAQEIWVCEKQ 594
Cdd:cd03237 174 HDIIMIDYLADRLIVFEGE 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
430-589 |
1.85e-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: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 430 RVALVGPNGAGKSTLLKLLTgellptdGMIRKHSHVkigryhqHLQEQLDLDLSPLE---------------YMMKCY-- 492
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMA-------GLLPGQGEI-------LLNGRPLSDWSAAElarhraylsqqqsppFAMPVFqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 493 ---------PEIKEKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQ-----NPH--MLFLDEPTNHLDIET 556
Cdd:COG4138 90 lalhqpagaSSEAVEQLLAQLAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVAQ 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 23956078 557 IDALADAINEF--EGGMMLVS-HDFRLIQQVAQEIW 589
Cdd:COG4138 169 QAALDRLLRELcqQGITVVMSsHDLNHTLRHADRVW 204
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
92-302 |
1.88e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 55.73 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIY---HLTREMPPSEKTPL---- 164
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILfkgQDLLELEPDERARAglfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 --QCVMEV-DTERAMLEREAERlAHEDAECEKLMELYERLEELDadkaEMRASrilhgLGFTPAMQRKKLKD-FSGGWRM 240
Cdd:TIGR01978 82 afQYPEEIpGVSNLEFLRSALN-ARRSARGEEPLDLLDFEKLLK----EKLAL-----LDMDEEFLNRSVNEgFSGGEKK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 241 RVALARALFIRPFMLLLDEPTNHLDLDA------CVwleEELKTFKRILVLVSHSQDFLNGVCTNIIH 302
Cdd:TIGR01978 152 RNEILQMALLEPKLAILDEIDSGLDIDAlkivaeGI---NRLREPDRSFLIITHYQRLLNYIKPDYVH 216
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
509-626 |
2.14e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 509 GLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEI 588
Cdd:PRK10636 137 GFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 23956078 589 WVCEKQTITKWPGDILAYKEHLKSKLVDE----EPQLTKRTH 626
Cdd:PRK10636 217 IHIEQQSLFEYTGNYSSFEVQRATRLAQQqamyESQQERVAH 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
192-322 |
2.99e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 192 EKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKL--KDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDA- 268
Cdd:PRK09473 118 EQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVq 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 269 --CVWLEEELKT-FKRILVLVSHSQDFLNGVCTNIIHMhnkklkyYTGNYDQYVKTR 322
Cdd:PRK09473 198 aqIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVM-------YAGRTMEYGNAR 247
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
424-590 |
3.03e-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: 55.04 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLD----TRVALVGPNGAGKSTLLKLLTGELLPTDGMI--------RKHSH-------------------------VK 466
Cdd:COG0411 22 DVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditGLPPHriarlgiartfqnprlfpeltvlenVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 467 IGRyHQHLQEQLDLDLSPLEYMMKcyPEIKEKEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRV----CLAwlawQNPHM 542
Cdd:COG0411 102 VAA-HARLGRGLLAALLRLPRARR--EEREARERAEELLERVGLADRADE-PAGNLSYGQQRRLeiarALA----TEPKL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23956078 543 LFLDEPT---NHLDIETIDALADAINEFEG-GMMLVSHDFRLIQQVAQEIWV 590
Cdd:COG0411 174 LLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVV 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
95-290 |
3.42e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLtrempPSEKTPLQCV-- 167
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqDITHV-----PAENRHVNTVfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 168 -------MEVDTERAMLEREAERLAHEDAEceKLMELYE--RLEEldadkaemrasrilhglgftpaMQRKKLKDFSGGW 238
Cdd:PRK09452 94 syalfphMTVFENVAFGLRMQKTPAAEITP--RVMEALRmvQLEE----------------------FAQRKPHQLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 239 RMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQ 290
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQ 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
234-307 |
3.53e-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: 3.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF--KRILVLVSHSqdfLNGV--CTNIIHMHNKK 307
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALakGKTVIVIAHR---LSTIrdADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
401-588 |
3.67e-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: 53.34 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhlqeqldL 480
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-------------------I 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 481 DLSPLEYMMKCYPEIKEKEEMrkIIGRYGL----TGKQQVSpiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIET 556
Cdd:cd03229 60 DGEDLTDLEDELPPLRRRIGM--VFQDFALfphlTVLENIA--LGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 23956078 557 ---IDALADAINEFEG-GMMLVSHDFRLIQQVAQEI 588
Cdd:cd03229 136 rreVRALLKSLQAQLGiTVVLVTHDLDEAARLADRV 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
91-317 |
4.02e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.48 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DI---------------- 149
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtDVsrlhardrkvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 150 YHLTREMPPSEKtplqcvmeVDTERAMLEREaERLaHEDAECEKLMELYE--RLEELdadkaemrASRIlhglgftPAmq 227
Cdd:PRK10851 83 YALFRHMTVFDN--------IAFGLTVLPRR-ERP-NAAAIKAKVTQLLEmvQLAHL--------ADRY-------PA-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 228 rkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHldLDACV------WLEEELKTFKRILVLVSHSQDFLNGVCTNII 301
Cdd:PRK10851 136 -----QLSGGQKQRVALARALAVEPQILLLDEPFGA--LDAQVrkelrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
250
....*....|....*.
gi 23956078 302 HMHNkklkyytGNYDQ 317
Cdd:PRK10851 209 VMSQ-------GNIEQ 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
91-308 |
4.09e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.29 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP----IpeHIDIYHLTReMPPSEktplq 165
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtsgqV--LVNGQDLSR-LKRRE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 cvmevdteRAMLEReaeRL--AHEDAeceKLmeLYER---------LEELDADKAEM--RASRILH--GLGftpamqrKK 230
Cdd:COG2884 74 --------IPYLRR---RIgvVFQDF---RL--LPDRtvyenvalpLRVTGKSRKEIrrRVREVLDlvGLS-------DK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 231 LKDF----SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACvwlEEELKTFKRI------LVLVSHSQDFLNGVCTNI 300
Cdd:COG2884 131 AKALphelSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS---WEIMELLEEInrrgttVLIATHDLELVDRMPKRV 207
|
....*...
gi 23956078 301 IHMHNKKL 308
Cdd:COG2884 208 LELEDGRL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
432-588 |
4.20e-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: 53.82 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 432 ALVGPNGAGKSTLLKLLTGELLPTDGMIR-KHSHVKIGRYHQ--HLQEQ--LDLDLSPLEYMM-----KCYPEIKEKEEM 501
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLDIAARNRigYLPEErgLYPKMKVIDQLVylaqlKGLKKEEARRRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 502 RKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHDF 578
Cdd:cd03269 110 DEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQM 188
|
170
....*....|
gi 23956078 579 RLIQQVAQEI 588
Cdd:cd03269 189 ELVEELCDRV 198
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
105-265 |
5.11e-08 |
|
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: 53.81 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 105 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKRevpIPEHIDIYH--LTREMPPSEKTPLQCVMEVDTERAMLE---- 178
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGqiLFNGQPRKPDQFQKCVAYVRQDDILLPgltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 179 REAERLAhedAECeklmelyeRLEEL--DADKAEMRASRILHGLGFTPAmQRKKLKDFSGGWRMRVALARALFIRPFMLL 256
Cdd:cd03234 99 RETLTYT---AIL--------RLPRKssDAIRKKRVEDVLLRDLALTRI-GGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
....*....
gi 23956078 257 LDEPTNHLD 265
Cdd:cd03234 167 LDEPTSGLD 175
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
401-623 |
6.36e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIY---NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGM-----------IRKHSHVK 466
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 467 -----IGRYHQHLQEQL-------DLDLSPL---EYMMKCYPEIKEKEEMRKIIGRYGltgkqQVSPIRnLSDGQKCRVC 531
Cdd:PRK13645 87 rlrkeIGLVFQFPEYQLfqetiekDIAFGPVnlgENKQEAYKKVPELLKLVQLPEDYV-----KRSPFE-LSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 532 LAWLAWQNPHMLFLDEPTNHLDIETIDalaDAINEFE-------GGMMLVSHDFRLIQQVAQEIWVC-EKQTITKW-PGD 602
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEE---DFINLFErlnkeykKRIIMVTHNMDQVLRIADEVIVMhEGKVISIGsPFE 237
|
250 260
....*....|....*....|.
gi 23956078 603 ILAYKEhLKSKLVDEEPQLTK 623
Cdd:PRK13645 238 IFSNQE-LLTKIEIDPPKLYQ 257
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
205-291 |
6.57e-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: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 205 DADKAEMRAS--RILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL----DACVWLEEELKT 278
Cdd:TIGR02142 102 RARPSERRISfeRVIELLGIGHLLGRLP-GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAE 180
|
90
....*....|...
gi 23956078 279 FKRILVLVSHSQD 291
Cdd:TIGR02142 181 FGIPILYVSHSLQ 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
417-576 |
8.45e-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: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 417 IYNNLEFGIDLDTRVALVGPNGAGKST--LLKLLTGELLPTDGMIRKhshvkigryhqhLQEQLDLDLSPLEymmkCYPE 494
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTllRLLAGALKGTPVAGCVDV------------PDNQFGREASLID----AIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 495 IKEKEEMRKIIGRYGLTGKQQ-VSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALA----DAINEFEG 569
Cdd:COG2401 109 KGDFKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVArnlqKLARRAGI 188
|
....*..
gi 23956078 570 GMMLVSH 576
Cdd:COG2401 189 TLVVATH 195
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
91-291 |
8.66e-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: 53.03 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPipEHIDIYHLTREM---PPSEKtplqcv 167
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEP--TSGRIYIGGRDVtdlPPKDR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 168 mevdtERAMLEREAERLAHedaeceklMELYE------RLEELDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMR 241
Cdd:cd03301 73 -----DIAMVFQNYALYPH--------MTVYDniafglKLRKVPKDEIDERVREVAELLQIEHLLDRKP-KQLSGGQRQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23956078 242 VALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQD 291
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtttIYVTHDQV 192
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
92-288 |
1.07e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.87 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-----------------GKR--EVPI-PEHIDIY- 150
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspafsasgevllnGRRltALPAeQRRIGILf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 151 -------HLTRE------MPPSEKtplqcvmevdteramleREAERLAHEDAeceklmelyerLEELDadkaemrasriL 217
Cdd:COG4136 83 qddllfpHLSVGenlafaLPPTIG-----------------RAQRRARVEQA-----------LEEAG-----------L 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 218 HGLGF-TPAmqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD--LDACV--WLEEELKTFKRILVLVSH 288
Cdd:COG4136 124 AGFADrDPA-------TLSGGQRARVALLRALLAEPRALLLDEPFSKLDaaLRAQFreFVFEQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
397-612 |
1.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.70 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKYTkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----------RK---HS 463
Cdd:PRK13636 2 EDYILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysRKglmKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 HVKIGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGltgkqqVSPIRN-----LSDGQKCRVC 531
Cdd:PRK13636 81 RESVGMVFQDPDNQLfsasvyqDVSFGAVNLKL---PEDEVRKRVDNALKRTG------IEHLKDkpthcLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 532 LAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGM----MLVSHDFRLIQQVAQEIWVCEKQTIT--KWPGDILA 605
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgltiIIATHDIDIVPLYCDNVFVMKEGRVIlqGNPKEVFA 231
|
....*..
gi 23956078 606 YKEHLKS 612
Cdd:PRK13636 232 EKEMLRK 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
424-584 |
1.18e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.53 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLltgellptdgmIRKHSHVKIGRYHQHLQEQLDLDLSPLE------YMMKCYP 493
Cdd:cd03217 18 GVNLTIKkgevHALMGPNGSGKSTLAKT-----------IMGHPKYEVTEGEILFKGEDITDLPPEErarlgiFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 494 E----IKEKEEMRKIigRYGLTGkqqvspirnlsdGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-- 567
Cdd:cd03217 87 PeipgVKNADFLRYV--NEGFSG------------GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLre 152
|
170
....*....|....*...
gi 23956078 568 EG-GMMLVSHDFRLIQQV 584
Cdd:cd03217 153 EGkSVLIITHYQRLLDYI 170
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
432-590 |
1.21e-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: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 432 ALVGPNGAGKSTLLKLLTGELLPTDG-----------MIRKHSHVKIGRYHQHLQEQLDLD------LSPLEYMMKCYPE 494
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGtvdlagvdlhgLSRRARARRVALVEQDSDTAVPLTvrdvvaLGRIPHRSLWAGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 495 IKEKEEM-RKIIGRYGLTGKQQVSpIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM 571
Cdd:TIGR03873 111 SPHDAAVvDRALARTELSHLADRD-MSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELaaTGVT 189
|
170 180
....*....|....*....|
gi 23956078 572 MLVS-HDFRLIQQVAQEIWV 590
Cdd:TIGR03873 190 VVAAlHDLNLAASYCDHVVV 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
399-586 |
1.37e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-----------KI 467
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQHLQEQL-------DLDLS------PLEYMMkcypeikekEEMRKIIGRYGLTGKQQVSPIRnLSDGQKCRVCLAW 534
Cdd:PRK13635 84 GMVFQNPDNQFvgatvqdDVAFGlenigvPREEMV---------ERVDQALRQVGMEDFLNREPHR-LSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956078 535 LAWQNPHMLFLDEPTNHLD-------IETIDALADainefEGGMMLVS--HDfrlIQQVAQ 586
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrrevLETVRQLKE-----QKGITVLSitHD---LDEAAQ 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
431-589 |
1.39e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTlLKLLTGELLPTDGMIR-------KHSHVKIGRYHQHLQEQ------------LDLDLSPleymmKC 491
Cdd:PRK03695 25 LHLVGPNGAGKST-LLARMAGLLPGSGSIQfagqpleAWSAAELARHRAYLSQQqtppfampvfqyLTLHQPD-----KT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 492 YPEIKEKeEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQ-----NPH--MLFLDEPTNHLDIETIDALADAI 564
Cdd:PRK03695 99 RTEAVAS-ALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180
....*....|....*....|....*...
gi 23956078 565 NEF--EGGMMLVS-HDFRLIQQVAQEIW 589
Cdd:PRK03695 177 SELcqQGIAVVMSsHDLNHTLRHADRVW 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
100-288 |
1.50e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 51.85 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 100 FHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI---------------GKREVPIPEHIdiyHLTREMPpseKTPL 164
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagvlrptsgtvrragGARVAYVPQRS---EVPDSLP---LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 QCVMevdteramLEREAERlahedaeceklmELYERLEELDadkaEMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVAL 244
Cdd:NF040873 76 DLVA--------MGRWARR------------GLWRRLTRDD----RAAVDDALERVGLA-DLAGRQLGELSGGQRQRALL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23956078 245 ARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF---KRILVLVSH 288
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
420-576 |
1.53e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 420 NLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHShVKIGR----YHQHL-----QEQLDLDLSPLE---- 486
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-EPIRRqrdeYHQDLlylghQPGIKTELTALEnlrf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 487 --YMMKCYPEikekEEMRKIIGRYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 564
Cdd:PRK13538 98 yqRLHGPGDD----EALWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*
gi 23956078 565 NEF--EGGM-MLVSH 576
Cdd:PRK13538 173 AQHaeQGGMvILTTH 187
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
400-593 |
1.61e-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: 52.58 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------RKH 462
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 463 SHvKIGRYHQHLQ--------EQLDLdlsPLEYMMKCYPEIKEK-EEMRKIIGrygLTGKQQVSPiRNLSDGQKCRVCLA 533
Cdd:cd03258 81 RR-RIGMIFQHFNllssrtvfENVAL---PLEIAGVPKAEIEERvLELLELVG---LEDKADAYP-AQLSGGQKQRVGIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 534 WLAWQNPHMLFLDEPTNHLDIET---IDALADAIN-EFEGGMMLVSHDFRLIQQVAQEIWVCEK 593
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETtqsILALLRDINrELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
95-265 |
1.81e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSM---LLSAIGKREVP--IPEHIDIYHLtremppsektPLQcvme 169
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGniIIDDEDISLL----------PLH---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 170 vdtERAM-----LEREA---ERLAHEDaeceKLMELYERLEELDADKAEMRASRILHGlgFTPAMQRKKL-KDFSGGWRM 240
Cdd:PRK10895 74 ---ARARrgigyLPQEAsifRRLSVYD----NLMAVLQIRDDLSAEQREDRANELMEE--FHIEHLRDSMgQSLSGGERR 144
|
170 180
....*....|....*....|....*
gi 23956078 241 RVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVD 169
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
424-554 |
1.93e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.85 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDG----------------------MIRKHSH----------VKI 467
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGevrlngrpladwspaelarrraVLPQHSSlsfpftveevVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHqHLQEQLDLDLSPLEYMMKCypeikekeemrkiigryGLTGKQQvSPIRNLSDGQKCRVCLA------WLAWQNPH 541
Cdd:PRK13548 100 GRAP-HGLSRAEDDALVAAALAQV-----------------DLAHLAG-RDYPQLSGGEQQRVQLArvlaqlWEPDGPPR 160
|
170
....*....|...
gi 23956078 542 MLFLDEPTNHLDI 554
Cdd:PRK13548 161 WLLLDEPTSALDL 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
401-596 |
1.99e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGP---CIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-----------RKHSHV- 465
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkVKLSDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 -KIGRYHQHLQEQL-------DLDLSPLEYMMKcYPEIKE--KEEMrKIIGRYGLTGKQQvSPIrNLSDGQKCRVCLAWL 535
Cdd:PRK13637 83 kKVGLVFQYPEYQLfeetiekDIAFGPINLGLS-EEEIENrvKRAM-NIVGLDYEDYKDK-SPF-ELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 536 AWQNPHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTI 596
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
104-291 |
2.12e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.86 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 104 ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTrempPSEKTPLQCVMEVDTERAMLEREAER 183
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT----ITHKTKDKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 184 LAHEDAeCEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNH 263
Cdd:PRK13646 97 QLFEDT-VEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|..
gi 23956078 264 LDLDACVWLEEELKTFK----RILVLVSHSQD 291
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtdenKTIILVSHDMN 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
103-266 |
2.12e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.77 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 103 QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSEKTPLQCVME-----VDT 172
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgePLAKLNRAQRKAFRRDIQMVFQdsisaVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 ERAMLEREAERLAHedaeceklmelyerLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRP 252
Cdd:PRK10419 105 RKTVREIIREPLRH--------------LLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170
....*....|....
gi 23956078 253 FMLLLDEPTNHLDL 266
Cdd:PRK10419 171 KLLILDEAVSNLDL 184
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
417-603 |
2.47e-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: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 417 IYNNLEFGIDLD----TRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGR-------------YHQHLQ 475
Cdd:COG3840 10 RYGDFPLRFDLTiaagERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngQDLTALPPAErpvsmlfqennlfPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 476 EQLDLDLSPleymmKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAWQNPHMLfLDEPTNHLDI 554
Cdd:COG3840 90 QNIGLGLRP-----GLKLTAEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALArCLVRKRPILL-LDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23956078 555 ----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQE-IWVCEKQTItkWPGDI 603
Cdd:COG3840 163 alrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRvLLVADGRIA--ADGPT 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
88-288 |
2.59e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.42 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 88 STDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSEKTPLQCV 167
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 168 MEVDTERAMLEREAERLAhedaeceKLMELYERLEeldadkaemrASRILHGlgftpAMQRkklkdFSGGWRMRVALARA 247
Cdd:PRK09544 82 LPLTVNRFLRLRPGTKKE-------DILPALKRVQ----------AGHLIDA-----PMQK-----LSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23956078 248 LFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSH 288
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSH 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
93-308 |
2.60e-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: 51.37 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIY---HLTREMPPsektplqcvme 169
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILfkgEDITDLPP----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 170 vdTERAmlereaerlahedaeceklmelyerleeldadkaemrasrilhGLGFTPAMQRK------KLKD--------FS 235
Cdd:cd03217 72 --EERA-------------------------------------------RLGIFLAFQYPpeipgvKNADflryvnegFS 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 236 GGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRI---LVLVSHSQDFLNGVCTNIIH-MHNKKL 308
Cdd:cd03217 107 GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEgksVLIITHYQRLLDYIKPDRVHvLYDGRI 183
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
401-577 |
2.69e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIY---NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI------------------ 459
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkalDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 460 ------------RKHSHVK-----IGRYHQHLQEQL-------DLDLSPLEYMMkcyPEIKEKEEMRKIIGRYGLTGKQ- 514
Cdd:PRK13651 83 vleklviqktrfKKIKKIKeirrrVGVVFQFAEYQLfeqtiekDIIFGPVSMGV---SKEEAKKRAAKYIELVGLDESYl 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 515 QVSPIrNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD----IETIDALaDAINEFEGGMMLVSHD 577
Cdd:PRK13651 160 QRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIF-DNLNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
400-596 |
3.03e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.30 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----------RKHSHVK--I 467
Cdd:PRK13644 1 MIRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfSKLQGIRklV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQHLQEQL-------DLDLSPLEYmmkCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNP 540
Cdd:PRK13644 80 GIVFQNPETQFvgrtveeDLAFGPENL---CLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 541 HMLFLDEPTNHLDIETIDALADAINEF-EGGMMLV--SHDFRLIqQVAQEIWVCEKQTI 596
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVyiTHNLEEL-HDADRIIVMDRGKI 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-553 |
3.06e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.91 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 391 PPCGKIPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------- 460
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpara 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 461 KHSHVKIGRYHQHlqEQLDLDLSPLE----YMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLA 536
Cdd:PRK13536 110 RLARARIGVVPQF--DNLDLEFTVREnllvFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170
....*....|....*..
gi 23956078 537 WQNPHMLFLDEPTNHLD 553
Cdd:PRK13536 188 INDPQLLILDEPTTGLD 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
106-311 |
3.12e-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: 51.76 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrevpipehidIYhltremPPSEKTplqcvmeVDTER---AMLEreae 182
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG----------IY------PPDSGT-------VTVRGrvsSLLG---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 183 rLAHE-DAECEKLMELYERLEELDADKAEMRAsRILHGLGFT--PAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDE 259
Cdd:cd03220 91 -LGGGfNPELTGRENIYLNGRLLGLSRKEIDE-KIDEIIEFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 260 PTNHLDL---DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYY 311
Cdd:cd03220 169 VLAVGDAafqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
91-308 |
3.30e-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: 51.81 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP----IpeHIDIYHLTReMPPSEKT 162
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtsgsV--LVDGTDLTL-LSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 163 PLQCVM-------EVDTERAMLEREAE--RLAHEDAEceklmELYERLEELD-----ADKAEMRASRIlhglgftpamqr 228
Cdd:cd03258 79 KARRRIgmifqhfNLLSSRTVFENVALplEIAGVPKA-----EIEERVLELLelvglEDKADAYPAQL------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 229 kklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACvwlEEELKTFKRI-------LVLVSHSQDFLNGVCTNII 301
Cdd:cd03258 142 ------SGGQKQRVGIARALANNPKVLLCDEATSALDPETT---QSILALLRDInrelgltIVLITHEMEVVKRICDRVA 212
|
....*..
gi 23956078 302 HMHNKKL 308
Cdd:cd03258 213 VMEKGEV 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
92-289 |
3.79e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 51.29 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTFHGQELLSDtkLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLtremPPSEKtPLqc 166
Cdd:COG3840 3 RLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqDLTAL----PPAER-PV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 167 vmevdterAMLEREAERLAHedaeceklMELYE----------RLEELDADKAEMRASRI-LHGLGftpamQRK--KLkd 233
Cdd:COG3840 74 --------SMLFQENNLFPH--------LTVAQniglglrpglKLTAEQRAQVEQALERVgLAGLL-----DRLpgQL-- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 234 fSGGWRMRVALARALfIR--PfMLLLDEPTNHLD-------LDacvWLEEELKTFKRILVLVSHS 289
Cdd:COG3840 131 -SGGQRQRVALARCL-VRkrP-ILLLDEPFSALDpalrqemLD---LVDELCRERGLTVLMVTHD 189
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
93-267 |
4.27e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.54 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI------GKREVPIpEHIDIYHLtremppSEKTPLQC 166
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIngtltpTAGTVLV-AGDDVEAL------SARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 167 VMEVDTERAmlereaerLAHE-DAECEKLMELYERLEELD-ADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVAL 244
Cdd:PRK09536 79 VASVPQDTS--------LSFEfDVRQVVEMGRTPHRSRFDtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180
....*....|....*....|...
gi 23956078 245 ARALFIRPFMLLLDEPTNHLDLD 267
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDIN 173
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
95-303 |
5.07e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI--DIYHLTREMPPsektplqcvmEVDT 172
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwlDGEHIQHYASK----------EVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 ERAMLEREA---------ERLAHEDAECEKLMELYeRLEELDADKAEMRASRILHglgftpaMQRKKLKDFSGGWRMRVA 243
Cdd:PRK10253 82 RIGLLAQNAttpgditvqELVARGRYPHQPLFTRW-RKEDEEAVTKAMQATGITH-------LADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 244 LARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR----ILVLVSHSqdfLNGVCTNIIHM 303
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQACRYASHL 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
403-577 |
5.14e-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: 50.60 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYTKDGpcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVKIGR--------- 469
Cdd:cd03259 3 LKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPERrnigmvfqd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 470 Y----HQHLQEQLDLDLSpleymMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAwQNPHMLF 544
Cdd:cd03259 81 YalfpHLTVAENIAFGLK-----LRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALArALA-REPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 23956078 545 LDEPTNHLD----IETIDALADAINEFEGGMMLVSHD 577
Cdd:cd03259 154 LDEPLSALDaklrEELREELKELQRELGITTIYVTHD 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
206-291 |
5.25e-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: 52.03 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 206 ADKAEMRAS--RILHGLGFTPAMQRK--KLkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDacvWLE- 273
Cdd:COG4148 105 APRAERRISfdEVVELLGIGHLLDRRpaTL---SGGERQRVAIGRALLSSPRLLLMDEPLAALDlarkaeiLP---YLEr 178
|
90 100
....*....|....*....|.
gi 23956078 274 --EELktfkRILVL-VSHSQD 291
Cdd:COG4148 179 lrDEL----DIPILyVSHSLD 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
399-577 |
5.31e-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: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGmirkhsHVKIGRYHQHLQEQL 478
Cdd:TIGR02868 333 PTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG------EVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 479 DL--------------DLSPLEYMMKCYPEIKEkEEMRKIIGRYGLTgkqqvSPIRNLSD---------------GQKCR 529
Cdd:TIGR02868 406 EVrrrvsvcaqdahlfDTTVRENLRLARPDATD-EELWAALERVGLA-----DWLRALPDgldtvlgeggarlsgGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23956078 530 VCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHD 577
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
401-577 |
5.46e-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: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtKDGPCIYNNLEfGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR------KHSHVKIGRY 470
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALE-DISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 HQH--------LQEQLDLdlsPLEymMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAwQNPH 541
Cdd:cd03293 79 FQQdallpwltVLDNVAL---GLE--LQGVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALArALA-VDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23956078 542 MLFLDEPTNHLDIET----IDALADAINEFEGGMMLVSHD 577
Cdd:cd03293 152 VLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
401-590 |
5.49e-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: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtkDGPCIYNnlefGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQHLQE 476
Cdd:cd03261 1 IELRGLTKSF--GGRTVLK----GVDLDVRrgeiLAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-DISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 477 QLDL-------------DLS-------PL-EYMMKCYPEIKEKEEMRkiIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-W 534
Cdd:cd03261 74 RLRRrmgmlfqsgalfdSLTvfenvafPLrEHTRLSEEEIREIVLEK--LEAVGLRGAEDLYP-AELSGGMKKRVALArA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 535 LAwQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM--MLVSHDFRLIQQVAQEIWV 590
Cdd:cd03261 151 LA-LDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLtsIMVTHDLDTAFAIADRIAV 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
95-305 |
5.52e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 51.19 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHiDIYHL-------- 152
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItgfyrptsgrilfdGRDITGLPPH-RIARLgiartfqn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 153 TREMPpsEKTPLQCVM-----------EVDTERAMLEREAERLAHEDAeceklMELYERLEeLdADKAEMRASRILHGlg 221
Cdd:COG0411 88 PRLFP--ELTVLENVLvaaharlgrglLAALLRLPRARREEREARERA-----EELLERVG-L-ADRADEPAGNLSYG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 222 ftpamQRKklkdfsggwrmRVALARALFIRPFMLLLDEPT---NHLDLDACVWLEEELKTFKRI-LVLVSHSQDFLNGVC 297
Cdd:COG0411 157 -----QQR-----------RLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGItILLIEHDMDLVMGLA 220
|
....*...
gi 23956078 298 TNIIHMHN 305
Cdd:COG0411 221 DRIVVLDF 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
431-590 |
6.48e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDlDLSPLEYMMKC--YPEIKEKEEMRKIIgRY 508
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLT-GIENIEFKMLCmgFKRKEIKAMTPKII-EF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 509 GLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHDFRLIQQVA 585
Cdd:PRK13546 131 SELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQFC 210
|
....*.
gi 23956078 586 QEI-WV 590
Cdd:PRK13546 211 TKIaWI 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
424-590 |
7.00e-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: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR----------------------KHSH----------VKI 467
Cdd:COG4559 19 DVSLTLRpgelTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspwelarrravlpQHSSlafpftveevVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQHLQEQLDLDLsPLEYMMKCypeikekeemrkiigryGLTGKQQvspiRN---LSDGQKCRVCLAW-LA--WQNPH 541
Cdd:COG4559 99 GRAPHGSSAAQDRQI-VREALALV-----------------GLAHLAG----RSyqtLSGGEQQRVQLARvLAqlWEPVD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 542 M----LFLDEPTNHLDI-------ETIDALADAinefEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:COG4559 157 GgprwLFLDEPTSALDLahqhavlRLARQLARR----GGGVVAVLHDLNLAAQYADRILL 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
398-580 |
7.60e-07 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 50.43 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 398 PPVIMVQNVSFKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI---------------- 459
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 460 --RKHshvKIG----RYH--QHL--QEQLDLdlsPLEYMMKCYPEIKEKeeMRKIIGRYGLTGKQQVSPiRNLSDGQKCR 529
Cdd:COG1136 82 rlRRR---HIGfvfqFFNllPELtaLENVAL---PLLLAGVSRKERRER--ARELLERVGLGDRLDHRP-SQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 530 VCLA-WLAwQNPHMLFLDEPTNHLDIET----IDALADAINEFEGGMMLVSHDFRL 580
Cdd:COG1136 153 VAIArALV-NRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPEL 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
91-288 |
7.77e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKRevpipehIDIYHLTR-------------EMP 157
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRL-------IELYPEARvsgevyldgqdifKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 158 PSE-KTPLQCVMEVDT--------ERAMLEREAERLAHEDAEC-EKLMELYERLEELDADKAEMRAsrilhglgftPAMQ 227
Cdd:PRK14247 77 VIElRRRVQMVFQIPNpipnlsifENVALGLKLNRLVKSKKELqERVRWALEKAQLWDEVKDRLDA----------PAGK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 228 rkklkdFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSH 288
Cdd:PRK14247 147 ------LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
106-276 |
8.03e-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: 50.54 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPipEHIDIYHLTREMppSEKTPLQcvMEVDTERAMLE----REA 181
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP--TSGGVILEGKQI--TEPGPDR--MVVFQNYSLLPwltvREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 182 ERLAHEDAEceklmelyerleeLDADKAEMRA--SRILHGLGFTPAmQRKKLKDFSGGWRMRVALARALFIRPFMLLLDE 259
Cdd:TIGR01184 75 IALAVDRVL-------------PDLSKSERRAivEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170
....*....|....*..
gi 23956078 260 PTNHLDLDACVWLEEEL 276
Cdd:TIGR01184 141 PFGALDALTRGNLQEEL 157
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
408-608 |
1.16e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 408 FKYtKDGPCIYN-NLEFGIDLDTrvALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-------------KIGRYHQH 473
Cdd:PRK13638 9 FRY-QDEPVLKGlNLDFSLSPVT--GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 LQEQL---DLDlSPLEYMMKCYpEIKEKEEMRKIIGRYGLTGKQQV--SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEP 548
Cdd:PRK13638 86 PEQQIfytDID-SDIAFSLRNL-GVPEAEITRRVDEALTLVDAQHFrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 549 TNHLD-------IETIDALADAINEfeggMMLVSHDFRLIQQVAQEIWV-CEKQTITKW-PGDILAYKE 608
Cdd:PRK13638 164 TAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVlRQGQILTHGaPGEVFACTE 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
425-594 |
1.24e-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: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 425 IDLDTRVAL-VGPNGAGKST-----------LLKLLTGELLPTDGMIRKHShvKIGRYHQHLQEQLDLD------LSPLE 486
Cdd:cd03240 18 IEFFSPLTLiVGQNGAGKTTiiealkyaltgELPPNSKGGAHDPKLIREGE--VRAQVKLAFENANGKKytitrsLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 487 YMMKCYpeikeKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAW-LAWQ-----NPHMLFLDEPTNHLDIETID-A 559
Cdd:cd03240 96 NVIFCH-----QGESNWPLLD----------MRGRCSGGEKVLASLIIrLALAetfgsNCGILALDEPTTNLDEENIEeS 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 23956078 560 LADAINEFEGG----MMLVSHDFRLIqQVAQEIWVCEKQ 594
Cdd:cd03240 161 LAEIIEERKSQknfqLIVITHDEELV-DAADHIYRVEKD 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
235-265 |
1.28e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.06 E-value: 1.28e-06
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK11247 135 SGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
401-577 |
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 23956078 401 IMVQNVSFKYTkDGPCIYN-NLEF---GIdldtrVALVGPNGAGKSTLLKLLTGELLPTDGMI----------------- 459
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDvSLTIpkgGI-----TALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvattpsrelak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 460 -----RKHSHVKI----------GRY-----------HQHLQEQLD-LDLSPLEymmkcypeikekeemrkiiGRYgltg 512
Cdd:COG4604 76 rlailRQENHINSrltvrelvafGRFpyskgrltaedREIIDEAIAyLDLEDLA-------------------DRY---- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 513 kqqvspIRNLSDGQKCRVCLAW-LAwQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHD 577
Cdd:COG4604 133 ------LDELSGGQRQRAFIAMvLA-QDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
401-554 |
1.46e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.01 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGpcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGM-------IRKHSHVKIGRYHQH 473
Cdd:PRK11231 3 LRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 LQEQLdldLSPleymmkcypeikEKEEMRKII-----------GRYGLTGKQQVS--------------PIRNLSDGQKC 528
Cdd:PRK11231 81 LPQHH---LTP------------EGITVRELVaygrspwlslwGRLSAEDNARVNqameqtrinhladrRLTDLSGGQRQ 145
|
170 180
....*....|....*....|....*.
gi 23956078 529 RVCLAWLAWQNPHMLFLDEPTNHLDI 554
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
233-307 |
1.50e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.43 E-value: 1.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 233 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLD---LDACVWLEEEL-KTFKRILVLVSHSQDFLNGVCTNIIHMHNKK 307
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
206-290 |
1.61e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 206 ADKAEMR-----ASRILHgLGftpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL---- 276
Cdd:PRK11000 105 AKKEEINqrvnqVAEVLQ-LA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIsrlh 180
|
90
....*....|....
gi 23956078 277 KTFKRILVLVSHSQ 290
Cdd:PRK11000 181 KRLGRTMIYVTHDQ 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
94-330 |
1.66e-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: 49.33 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 94 INLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHLTREMPPSEKTPLQCV 167
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqDVSDLRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 168 MEvDT---------ERAMLEREAERLAHEDAEcEKLMELYERLEeLDADKAEMrasrilhglgftpAMQrkklkdFSGGW 238
Cdd:cd03292 84 FQ-DFrllpdrnvyENVAFALEVTGVPPREIR-KRVPAALELVG-LSHKHRAL-------------PAE------LSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 239 RMRVALARALFIRPFMLLLDEPTNHLDLDacvwleeelkTFKRILVLVSHSQDflNGVcTNIIHMHNKKLkyytgnYDQY 318
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPD----------TTWEIMNLLKKINK--AGT-TVVVATHAKEL------VDTT 202
|
250
....*....|..
gi 23956078 319 VKTRLELEENQM 330
Cdd:cd03292 203 RHRVIALERGKL 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
95-291 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTF-HGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPSEKTPL---QCVMEV 170
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI----------------NRLIEPTSGEIFidgEDIREQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERamLER-------EAERLAHedAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKD-FSGGWRMRV 242
Cdd:cd03295 69 DPVE--LRRkigyviqQIGLFPH--MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHeLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23956078 243 ALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQD 291
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHDID 197
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
91-265 |
1.73e-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: 49.61 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-------------GKREVPIPEHiDIYHLTREM- 156
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlleepdsgtitvDGEDLTDSKK-DINKLRRKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 157 ---------PpsEKTPLQCVME----VdteRAMLEREAERLAhedaeceklMELYERLEeLdADKAEMRASRIlhglgft 223
Cdd:COG1126 81 mvfqqfnlfP--HLTVLENVTLapikV---KKMSKAEAEERA---------MELLERVG-L-ADKADAYPAQL------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23956078 224 pamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG1126 138 -----------SGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
421-588 |
1.82e-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: 49.29 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 421 LEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigryhqhLQEQLDLDLSPLEYM---------MKC 491
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------------TVDGFDVVKEPAEARrrlgfvsdsTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 492 YPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSD-----------------GQKCRVCLAWLAWQNPHMLFLDEPTNHLDI 554
Cdd:cd03266 90 YDRLTARENLEYFAGLYGLKGDELTARLEELADrlgmeelldrrvggfstGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 23956078 555 ETIDALADAINEF--EGGMMLVS-HDFRLIQQVAQEI 588
Cdd:cd03266 170 MATRALREFIRQLraLGKCILFStHIMQEVERLCDRV 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
106-311 |
1.92e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.31 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKrevpipehidIYhltremPPSEKTpLQCVMEVdteRAMLE------- 178
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG----------IL------EPTSGR-VEVNGRV---SALLElgagfhp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 179 ----REaerlahedaecekLMELYERLeeLDADKAEMRA--SRILH--GLG-F--TPamqrkkLKDFSGGWRMRVALARA 247
Cdd:COG1134 102 eltgRE-------------NIYLNGRL--LGLSRKEIDEkfDEIVEfaELGdFidQP------VKTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 248 LFIRPFMLLLDEptnhldldacvWL-----------EEELKTFK---RILVLVSHSQDFLNGVCTNIIHMHNKKLKYY 311
Cdd:COG1134 161 TAVDPDILLVDE-----------VLavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
91-307 |
2.02e-06 |
|
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: 48.82 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVP-IPEHIDIYHLTREMPpsek 161
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdsGEVLFDgKPLDIAARNRIGYLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 162 tplqcvmevdTERAMLEREAERlahedaecEKLMELyERLEELDADKAEMRASRILHGLGFTPaMQRKKLKDFSGGWRMR 241
Cdd:cd03269 77 ----------EERGLYPKMKVI--------DQLVYL-AQLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 242 VALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKK 307
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
228-289 |
2.05e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 2.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 228 RKKLKDF----SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHS 289
Cdd:PRK14267 140 KDRLNDYpsnlSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHS 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-553 |
2.22e-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: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLpTDGMI---------------RKHSHV 465
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIqidgvswnsvtlqtwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 ---KIGRYHQHLQEQLDldlsPLEYMmkcypeikEKEEMRKIIGRYGLTGKQQVSPIR----------NLSDGQKCRVCL 532
Cdd:TIGR01271 1297 ipqKVFIFSGTFRKNLD----PYEQW--------SDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyVLSNGHKQLMCL 1364
|
170 180
....*....|....*....|.
gi 23956078 533 AWLAWQNPHMLFLDEPTNHLD 553
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLD 1385
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
522-590 |
2.27e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 2.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 522 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
401-576 |
2.71e-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: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFkYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTL--------LKLLTGELLPTDG---MIRKHSHVKIGR 469
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLfralaglwPWGSGRIGMPEGEdllFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 470 yhqhLQEQLdldlspleymmkCYPEIKEkeemrkiigrygltgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPT 549
Cdd:cd03223 80 ----LREQL------------IYPWDDV------------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180
....*....|....*....|....*..
gi 23956078 550 NHLDIETIDALADAINEFEGGMMLVSH 576
Cdd:cd03223 120 SALDEESEDRLYQLLKELGITVISVGH 146
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-599 |
2.79e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 413 DGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-----------------KIGRYHQHLQ 475
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidaiklrkEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 476 EQLDLDL-SPLEYMMKCYpEIKEKEEMRKI-------IGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDE 547
Cdd:PRK14246 101 PFPHLSIyDNIAYPLKSH-GIKEKREIKKIveeclrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23956078 548 PTNHLDIETIDALADAINEF--EGGMMLVSHDFRLIQQVAQEIWVCEKQTITKW 599
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
106-291 |
2.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.35 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLT-------REMPPSEKTpLQCVMEVDTERAMLE 178
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqKEIKPVRKK-VGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 179 REAERLAHEDaecEKLMELYERLEELDADKAEMrasrilhgLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLD 258
Cdd:PRK13643 101 TVLKDVAFGP---QNFGIPKEKAEKIAAEKLEM--------VGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 23956078 259 EPTNHLDLDACVwleEELKTFKRI------LVLVSHSQD 291
Cdd:PRK13643 170 EPTAGLDPKARI---EMMQLFESIhqsgqtVVLVTHLMD 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-553 |
2.84e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 394 GKIPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR----------KHS 463
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 HVKIGRYHQHlqEQLDLDLSPLEYMMkcypeikekeemrkIIGRY-GLTGKQ-----------------QVSPIRNLSDG 525
Cdd:PRK13537 79 RQRVGVVPQF--DNLDPDFTVRENLL--------------VFGRYfGLSAAAaralvppllefaklenkADAKVGELSGG 142
|
170 180
....*....|....*....|....*...
gi 23956078 526 QKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
235-309 |
2.86e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLDL----DACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLK 309
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
234-288 |
3.68e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 3.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLD--ACVW-----LEEELKTfkrILVLVSH 288
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSvqAQVLnlmmdLQQELGL---SYVFISH 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
52-288 |
4.06e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.44 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 52 TTGDGEVDLLTKELEDFEMKKAAARAVTGVlashpNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKS- 130
Cdd:PRK13536 8 EEAPRRLELSPIERKHQGISEAKASIPGSM-----STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 131 ---MLLSAIGKRE-------VPIPEHIDIYHLTREMPPS------EKTPLQCVMEVDTERAMLEREAErlahedAECEKL 194
Cdd:PRK13536 83 iarMILGMTSPDAgkitvlgVPVPARARLARARIGVVPQfdnldlEFTVRENLLVFGRYFGMSTREIE------AVIPSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 195 MElYERLEeldaDKAEMRASrilhglgftpamqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE 274
Cdd:PRK13536 157 LE-FARLE----SKADARVS------------------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
250
....*....|....*...
gi 23956078 275 ELKTF----KRILvLVSH 288
Cdd:PRK13536 214 RLRSLlargKTIL-LTTH 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
95-265 |
4.06e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPipehiDIYHLTREMPPSEKTPLQCVMEvdTER 174
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAP-----DAGEVHYRMRDGQLRDLYALSE--AER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 175 AMLEREAERLAHEDAE-------------CEKLMEL----YERLEELDAD---KAEMRASRIlhglgftpamqrkklkD- 233
Cdd:PRK11701 84 RRLLRTEWGFVHQHPRdglrmqvsaggniGERLMAVgarhYGDIRATAGDwleRVEIDAARI----------------Dd 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 23956078 234 ----FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK11701 148 lpttFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
519-562 |
4.07e-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: 4.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 23956078 519 IRNLSDGQKCRVCLAW-LAWqNPHMLFLDEPTNHLD-------IETIDALAD 562
Cdd:cd03213 109 LRGLSGGERKRVSIALeLVS-NPSLLFLDEPTSGLDsssalqvMSLLRRLAD 159
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
230-265 |
4.31e-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: 4.31e-06
10 20 30
....*....|....*....|....*....|....*.
gi 23956078 230 KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:cd03213 108 KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
102-265 |
4.36e-06 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 47.87 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPSEKTPLQCVMEVDTERAMLEREA 181
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRI----------------LAGLSPPLAGRVLLNGGPLDFQRDSIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 182 ERLAHEDAeCEKLMELYERLEELDADKA-----EMRASRILHGLGFTPAMQrkklkdFSGGWRMRVALARALFIRPFMLL 256
Cdd:cd03231 76 LYLGHAPG-IKTTLSVLENLRFWHADHSdeqveEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWI 148
|
....*....
gi 23956078 257 LDEPTNHLD 265
Cdd:cd03231 149 LDEPTTALD 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
345-443 |
4.87e-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: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 345 NYIARFGHGSAKLARQAQSkektLQKMMASglTERVVS--DKTLSFYFPPCGKIPPPV---IMVQNVSFKYTKDGPcIYN 419
Cdd:COG1132 285 LYLLRLFGPLRQLANVLNQ----LQRALAS--AERIFEllDEPPEIPDPPGAVPLPPVrgeIEFENVSFSYPGDRP-VLK 357
|
90 100
....*....|....*....|....
gi 23956078 420 NLEFGIDLDTRVALVGPNGAGKST 443
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKST 381
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
207-309 |
5.13e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.48 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 207 DKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwLEEELKTFKRI---- 282
Cdd:PRK13634 119 EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG---RKEMMEMFYKLhkek 195
|
90 100 110
....*....|....*....|....*....|
gi 23956078 283 ---LVLVSHSQDFLNGVCTNIIHMHNKKLK 309
Cdd:PRK13634 196 gltTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
432-588 |
6.00e-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: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 432 ALVGPNGAGKSTLLKLLTGELLPTDG--MIRKHSHVK--------IGRYHQHLqeQLDLDLSPLEYM-----MKCYPEIK 496
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPTSGraTVAGHDVVReprevrrrIGIVFQDL--SVDDELTGWENLyiharLYGVPGAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 497 EKEEMRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGM--M 572
Cdd:cd03265 108 RRERIDELLDFVGLLEAAD-RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeEFGMtiL 186
|
170
....*....|....*.
gi 23956078 573 LVSHDFRLIQQVAQEI 588
Cdd:cd03265 187 LTTHYMEEAEQLCDRV 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
419-595 |
6.09e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 419 NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTD---------------------GMIRKHSHVKIGR-------- 469
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGgtillrgqhieglpghqiarmGVVRTFQHVRLFRemtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 470 ---YHQHLQEQLdldLSPLeYMMKCYPEiKEKEEMRKI---IGRYGLTgkqQVS--PIRNLSDGQKCRVCLAWLAWQNPH 541
Cdd:PRK11300 102 lvaQHQQLKTGL---FSGL-LKTPAFRR-AESEALDRAatwLERVGLL---EHAnrQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 542 MLFLDEPTNHLD-IETID--ALADAI-NEFEGGMMLVSHDFRLIQQVAQEIWVCEKQT 595
Cdd:PRK11300 174 ILMLDEPAAGLNpKETKEldELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
399-588 |
6.13e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYtKDGPC---IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG------------------ 457
Cdd:PRK11629 4 ILLQCDNLCKRY-QEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 458 MIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAW 537
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 538 QNPHMLFLDEPTNHLDIETIDALADAINEFE----GGMMLVSHDFRLIQQVAQEI 588
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-327 |
6.84e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 92 HIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgKREVPIPE-----------------HIDIYHLTR 154
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIYDskikvdgkvlyfgkdifQIDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 155 E--MPPSEKTPLQCVMEVDTERAMLEREAERlahEDAECEKLMElyERLEELDADKAemrasriLHGLGFTPAMQrkklk 232
Cdd:PRK14246 91 EvgMVFQQPNPFPHLSIYDNIAYPLKSHGIK---EKREIKKIVE--ECLRKVGLWKE-------VYDRLNSPASQ----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 233 dFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHSQDFLNGVCTNIIHMHNKKLKY 310
Cdd:PRK14246 154 -LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
250
....*....|....*..
gi 23956078 311 YTGNYDQYVKTRLELEE 327
Cdd:PRK14246 233 WGSSNEIFTSPKNELTE 249
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
200-265 |
7.00e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 47.93 E-value: 7.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 200 RLEELDADKAEMRASRILHGLGFTPAmQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG4525 102 RLRGVPKAERRARAEELLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
95-265 |
7.35e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.77 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKReVPiPEHIDIyhlTREMPPsektplqcVMEVDTER 174
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF-VP-YQHGSI---TLDGKP--------VEGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 175 AMLEREAERLAHEDAECEKLMELyeRLEELDADKAEMRASRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRPFM 254
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGL--QLAGVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIARALAANPQL 149
|
170
....*....|.
gi 23956078 255 LLLDEPTNHLD 265
Cdd:PRK11248 150 LLLDEPFGALD 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
85-291 |
8.31e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.67 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 85 HPNSTDVHIINLSLTFHGQEL--LSDTKLELNSGRRYGLIGLNGIGKSMLLSAigkrevpipehidiyhLTREMPPSE-- 160
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQL----------------LTRAWDPQQge 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 161 ----KTPLQCVMEvDTERAMLE-------------REAERLAHEDAECEKLMELYER--LEELDADKAEMRA-----SRI 216
Cdd:PRK11160 397 illnGQPIADYSE-AALRQAISvvsqrvhlfsatlRDNLLLAAPNASDEALIEVLQQvgLEKLLEDDKGLNAwlgegGRQ 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 217 LhglgftpamqrkklkdfSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDacvwleeelkTFKRIL-VLVSHSQD 291
Cdd:PRK11160 476 L-----------------SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE----------TERQILeLLAEHAQN 524
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
401-597 |
9.36e-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: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLltgellptdgmirkhshvkIGRYHQHLQEQLDL 480
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQL-------------------LTGDLKPQQGEITL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 481 DLSPLEymmkcypeiKEKEEMRKIIGRYgltgKQQV----SPIRN-----LSDGQKCRVCLAWLAWQNPHMLFLDEPTNH 551
Cdd:cd03247 62 DGVPVS---------DLEKALSSLISVL----NQRPylfdTTLRNnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23956078 552 LDIETIDALADAINEF--EGGMMLVSHDFRLIQQVaQEIWVCEKQTIT 597
Cdd:cd03247 129 LDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
235-265 |
9.96e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 9.96e-06
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
424-597 |
1.02e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.39 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDG-MIRKHSHVKIGRYHQHL--QE------QLDL--DLSPLEYM 488
Cdd:PRK09493 19 NIDLNIDqgevVVIIGPSGSGKSTLLRCINKLEEITSGdLIVDGLKVNDPKVDERLirQEagmvfqQFYLfpHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 489 MkcYPEIK----EKEEMRKI----IGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIE----- 555
Cdd:PRK09493 99 M--FGPLRvrgaSKEEAEKQarelLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhev 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23956078 556 --TIDALADainefEG-GMMLVSHDFRLIQQVAQEIWVCEKQTIT 597
Cdd:PRK09493 176 lkVMQDLAE-----EGmTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
91-289 |
1.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKR-----EVPIPEHIDIYHltremppsektplQ 165
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFN-------------Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 CVMEVDTERAMLEREAErLAHED------------AECEKLMELYERLEELDADKAEMRAS----RILHGLgftpamqRK 229
Cdd:PRK14258 75 NIYERRVNLNRLRRQVS-MVHPKpnlfpmsvydnvAYGVKIVGWRPKLEIDDIVESALKDAdlwdEIKHKI-------HK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 230 KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK----RILVLVSHS 289
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
400-618 |
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 23956078 400 VIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLP---------TDGMIRKHSHV----- 465
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGITLTAKTVwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 KIGRYHQHLQEQL-------DLDLSpLEYmmKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQ 538
Cdd:PRK13640 85 KVGIVFQNPDNQFvgatvgdDVAFG-LEN--RAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 539 NPHMLFLDEPTNHLDIE------------------TIDALADAINEFEGG-MMLVSHDFRLIQQVA-QEIWvcEKQTITK 598
Cdd:PRK13640 161 EPKIIILDESTSMLDPAgkeqilklirklkkknnlTVISITHDIDEANMAdQVLVLDDGKLLAQGSpVEIF--SKVEMLK 238
|
250 260
....*....|....*....|
gi 23956078 599 WPGDILAYKEHLKSKLVDEE 618
Cdd:PRK13640 239 EIGLDIPFVYKLKNKLKEKG 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
84-266 |
1.15e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 84 SHPNSTDVHII--NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGkrevpipehidiyhltREMPPSEK 161
Cdd:PRK10575 3 EYTNHSDTTFAlrNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG----------------RHQPPSEG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 162 TPLQCVMEVDT-ERAMLEREAERLAHE--DAECEKLMELYE-----------RLEELDADKAEMRASRIlhglGFTPAMQ 227
Cdd:PRK10575 67 EILLDAQPLESwSSKAFARKVAYLPQQlpAAEGMTVRELVAigrypwhgalgRFGAADREKVEEAISLV----GLKPLAH 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23956078 228 RkkLKD-FSGGWRMRVALARALFIRPFMLLLDEPTNHLDL 266
Cdd:PRK10575 143 R--LVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
401-605 |
1.21e-05 |
|
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: 46.91 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----------------RKHSH 464
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpvelrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 465 V--KIGRY-HQHLQEQLDLDLSPLEymmkcYPEIKEKEEMRKIIGRYGLTGKQ--QVSPiRNLSDGQKCRVCLAWLAWQN 539
Cdd:cd03295 80 ViqQIGLFpHMTVEENIALVPKLLK-----WPKEKIRERADELLALVGLDPAEfaDRYP-HELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 540 PHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHD----FRLiqqvAQEIWVCEKQTITKW--PGDILA 605
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDideaFRL----ADRIAIMKNGEIVQVgtPDEILR 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
207-266 |
1.22e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.12 E-value: 1.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 207 DKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDL 266
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
102-265 |
1.34e-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: 46.71 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEH--IDIYHLTREMPPSEKTPLQCVMEVDT------- 172
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlVDGHDLALADPAWLRRQVGVVLQENVlfnrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 ERAMLEREAERLaHEDAECEKLMELYERLEELDADKAEMRASRilhGLGFtpamqrkklkdfSGGWRMRVALARALFIRP 252
Cdd:cd03252 94 DNIALADPGMSM-ERVIEAAKLAGAHDFISELPEGYDTIVGEQ---GAGL------------SGGQRQRIAIARALIHNP 157
|
170
....*....|...
gi 23956078 253 FMLLLDEPTNHLD 265
Cdd:cd03252 158 RILIFDEATSALD 170
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
401-623 |
1.38e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.43 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLeFGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR---------------K 461
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRAL-FDVNLTIEdgsyTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 462 HSHVKIGRYHQHLQEQL-------DLDLSPLEYmmkcypEIKEKEEMRKIIGRYGLTGKQQVSPIRN---LSDGQKCRVC 531
Cdd:PRK13649 82 QIRKKVGLVFQFPESQLfeetvlkDVAFGPQNF------GVSQEEAEALAREKLALVGISESLFEKNpfeLSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 532 LAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEIWVCEKQTITK--WPGDILAY 606
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMtiVLVTHLMDDVANYADFVYVLEKGKLVLsgKPKDIFQD 235
|
250
....*....|....*..
gi 23956078 607 KEHLKSKLVDeEPQLTK 623
Cdd:PRK13649 236 VDFLEEKQLG-VPKITK 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
398-588 |
1.52e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 398 PPVIMVQNVSFKYtkdGPCIYNNlefGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR--------KHSHV 465
Cdd:COG3845 3 PPALELRGITKRF---GGVVAND---DVSLTVRpgeiHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvriRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 ----KIGRYHQHLQ--------EQLDLDLSPLEYM---MKcypeiKEKEEMRKIIGRYGLtgkqQVSP---IRNLSDGQK 527
Cdd:COG3845 77 aialGIGMVHQHFMlvpnltvaENIVLGLEPTKGGrldRK-----AARARIRELSERYGL----DVDPdakVEDLSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 528 CRV----CLawlaWQNPHMLFLDEPTNHLDIETIDALADAINEF--EG-GMMLVSHDFRLIQQVAQEI 588
Cdd:COG3845 148 QRVeilkAL----YRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKLREVMAIADRV 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
89-324 |
1.57e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.93 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 89 TDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTrEMPPSEKTPlQCVM 168
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR----------------HLS-GLITGDKSA-GSHI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 169 EV---DTERA-MLEREAERLAHEDAECEKLMELYERLEELD--------------------ADKAEMRASRILHGLGFTP 224
Cdd:PRK09984 65 ELlgrTVQREgRLARDIRKSRANTGYIFQQFNLVNRLSVLEnvligalgstpfwrtcfswfTREQKQRALQALTRVGMVH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 225 -AMQRkkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVS-HSQDFLNGVCTN 299
Cdd:PRK09984 145 fAHQR--VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgITVVVTlHQVDYALRYCER 222
|
250 260
....*....|....*....|....*
gi 23956078 300 IIHMHNKKLkYYTGNYDQYVKTRLE 324
Cdd:PRK09984 223 IVALRQGHV-FYDGSSQQFDNERFD 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
401-567 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHShVKIGRYHQH-LQEQLD 479
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG-VDISKIGLHdLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 480 L--------------DLSPLEYmmkcYPEikekEEMRKIIGRYGLTGKQQVSPIR----------NLSDGQKCRVCLAWL 535
Cdd:cd03244 82 IipqdpvlfsgtirsNLDPFGE----YSD----EELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARA 153
|
170 180 190
....*....|....*....|....*....|..
gi 23956078 536 AWQNPHMLFLDEPTNHLDIETIDALADAINEF 567
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
404-566 |
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 23956078 404 QNVSFKYTKDGPCIYNnLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPT------DGM-IRKhshVKIGRYHQHL-- 474
Cdd:PRK13657 338 DDVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQsgriliDGTdIRT---VTRASLRRNIav 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 475 --QEQLDLDLSPLEYMMKCYPEIKEkEEMRK--------------------IIGRYGltgkqqvspiRNLSDGQKCRVCL 532
Cdd:PRK13657 414 vfQDAGLFNRSIEDNIRVGRPDATD-EEMRAaaeraqahdfierkpdgydtVVGERG----------RQLSGGERQRLAI 482
|
170 180 190
....*....|....*....|....*....|....
gi 23956078 533 AWLAWQNPHMLFLDEPTNHLDIETIDALADAINE 566
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
121-294 |
1.91e-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: 46.06 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 121 LIGLNGIGKSMLLSAIgkrevpipehidIYHLTREMPPSEKtplqcvmEVDTERAMLeREAERLAhedaeceklmelYER 200
Cdd:cd03240 27 IVGQNGAGKTTIIEAL------------KYALTGELPPNSK-------GGAHDPKLI-REGEVRA------------QVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 201 LEELDADKAEMRASRILH----------GLGFTPAMQ-RKKLkdfSGGWRM------RVALARALFIRPFMLLLDEPTNH 263
Cdd:cd03240 75 LAFENANGKKYTITRSLAilenvifchqGESNWPLLDmRGRC---SGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 23956078 264 LDLDACVW-----LEEELKTFKRILVLVSHSQDFLN 294
Cdd:cd03240 152 LDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
95-289 |
2.10e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.31 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPE-----------HiDIYhltremppsekTP 163
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEvtitgsivyngH-NIY-----------SP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 164 LQCVMEVDTERAMLEREAERLAhedaeceklMELYE------RLEELDaDKAEMRAS--RILHGlgftpAMQRKKLKD-- 233
Cdd:PRK14239 78 RTDTVDLRKEIGMVFQQPNPFP---------MSIYEnvvyglRLKGIK-DKQVLDEAveKSLKG-----ASIWDEVKDrl 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956078 234 ------FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSHS 289
Cdd:PRK14239 143 hdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRS 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
95-269 |
2.13e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.02 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLsaigkrevpipehidiyhltREM----PPSEKTplqcvMEV 170
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLL--------------------RLIagllPPAAGT-----IKL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLEREAER---LAHEDAeCEKLMELYERLE---------ELDADKAemrASRI-LHGLGFTPAmqrkklKDFSGG 237
Cdd:PRK13539 62 DGGDIDDPDVAEAchyLGHRNA-MKPALTVAENLEfwaaflggeELDIAAA---LEAVgLAPLAHLPF------GYLSAG 131
|
170 180 190
....*....|....*....|....*....|...
gi 23956078 238 WRMRVALARAL-FIRPfMLLLDEPTNHLDLDAC 269
Cdd:PRK13539 132 QKRRVALARLLvSNRP-IWILDEPTAALDAAAV 163
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
234-310 |
2.27e-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: 2.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLngvctniiHMHNKKLKY 310
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLW--------KFHDRVLDL 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
207-290 |
2.53e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.60 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 207 DKAEM--RASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEP-TNhldLDAC--VWLEEELKTFKR 281
Cdd:COG3839 106 PKAEIdrRVREAAELLGLEDLLDRKP-KQLSGGQRQRVALGRALVREPKVFLLDEPlSN---LDAKlrVEMRAEIKRLHR 181
|
90
....*....|...
gi 23956078 282 IL----VLVSHSQ 290
Cdd:COG3839 182 RLgtttIYVTHDQ 194
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
121-288 |
2.82e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 121 LIGLNGIGKSMLLSAI-----GKREVPIPEHIDIYHltremPPSEKTPLQCVMEVDTERAMLER---EAERLAHEDAE-- 190
Cdd:COG0419 28 IVGPNGAGKSTILEAIryalyGKARSRSKLRSDLIN-----VGSEEASVELEFEHGGKRYRIERrqgEFAEFLEAKPSer 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 191 ---------CEKLMELYERLEELDAD----KAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALfirpfMLLL 257
Cdd:COG0419 103 kealkrllgLEIYEELKERLKELEEAlesaLEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL-----SLIL 177
|
170 180 190
....*....|....*....|....*....|....
gi 23956078 258 DepTNHLDldacvwlEEELKTFKRIL---VLVSH 288
Cdd:COG0419 178 D--FGSLD-------EERLERLLDALeelAIITH 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
520-590 |
2.83e-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: 2.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 520 RNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETI----DALADAINEFEGGMMLVSHDFRLIQQVAQE-IWV 590
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKaIWL 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
397-583 |
2.85e-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: 45.89 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKY-TKDGP-CIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV--------- 465
Cdd:COG4181 5 SAPIIELRGLTKTVgTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 ------KIGRYHQhlQEQLDLDLSPLEYMMkcYP-EIKE----KEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAW 534
Cdd:COG4181 85 arlrarHVGFVFQ--SFQLLPTLTALENVM--LPlELAGrrdaRARARALLERVGLGHRLDHYP-AQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23956078 535 LAWQNPHMLFLDEPTNHLDIETIDALAD---AINEfEGG--MMLVSHDFRLIQQ 583
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDllfELNR-ERGttLVLVTHDPALAAR 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
93-265 |
2.98e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQ----ELLSDTKLELNSGRRYGLIGLNGIGKSML-LSAIgkREVPIPEHI----DI-YHLTREMPPSEKT 162
Cdd:PRK15134 8 IENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTaLSIL--RLLPSPPVVypsgDIrFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 163 plqcVMEVDTER-AMLEREAERLAHEDAECEKlmELYERLEELDADKAEMRASRILHGLGFTPAMQ-RKKLKDF----SG 236
Cdd:PRK15134 86 ----LRGVRGNKiAMIFQEPMVSLNPLHTLEK--QLYEVLSLHRGMRREAARGEILNCLDRVGIRQaAKRLTDYphqlSG 159
|
170 180
....*....|....*....|....*....
gi 23956078 237 GWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
95-260 |
3.09e-05 |
|
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: 45.61 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVP-----IPEHIDIYHltreMPPSEKTPL----- 164
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdsgkiLLDGQDITK----LPMHKRARLgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 -QcvmEVDTERAMLEREAERLAHEDAECEKlmelYERLEELDADKAEMRASRILHGLGFTpamqrkklkdFSGGWRMRVA 243
Cdd:cd03218 81 pQ---EASIFRKLTVEENILAVLEIRGLSK----KEREEKLEELLEEFHITHLRKSKASS----------LSGGERRRVE 143
|
170
....*....|....*..
gi 23956078 244 LARALFIRPFMLLLDEP 260
Cdd:cd03218 144 IARALATNPKFLLLDEP 160
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
95-291 |
3.15e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQELLSDtkLELNSGRRYGLIGLNGIGKSMLLSAIGKreVPIPEHIDIY-----HltREMPPSeKTPLqcvme 169
Cdd:PRK10771 6 DITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAG--FLTPASGSLTlngqdH--TTTPPS-RRPV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 170 vdterAMLEREAERLAHEDAECEKLMELYERLEELDADKAEMRAsrILHGLGFTPAMQRKKlKDFSGGWRMRVALARALF 249
Cdd:PRK10771 74 -----SMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHA--IARQMGIEDLLARLP-GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23956078 250 IRPFMLLLDEPTNHLD---------LDACVWLEEELKtfkriLVLVSHSQD 291
Cdd:PRK10771 146 REQPILLLDEPFSALDpalrqemltLVSQVCQERQLT-----LLMVSHSLE 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
194-265 |
3.35e-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: 3.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 194 LMELYERLEELDADKAEMRASRILHGLGFTPAMQRkkLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG0444 109 IAEPLRIHGGLSKAEARERAIELLERVGLPDPERR--LDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
522-580 |
3.53e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.54 E-value: 3.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 522 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDFRL 580
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQL 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
431-590 |
3.65e-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: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDGMIrkHSHVKIGRYHQHLQEqlDLDLSPLEYMMKCYPEI----KEKEEmrkIIG 506
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISP--DYDGTVEEFLRSANTDDfgssYYKTE---IIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 507 RYGLTgKQQVSPIRNLSDGQKCRV----CLAwlawQNPHMLFLDEPTNHLDIETIDALADAINEF----EGGMMLVSHDF 578
Cdd:COG1245 442 PLGLE-KLLDKNVKDLSGGELQRVaiaaCLS----RDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDI 516
|
170
....*....|..
gi 23956078 579 RLIQQVAQEIWV 590
Cdd:COG1245 517 YLIDYISDRLMV 528
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
228-288 |
3.76e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 3.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 228 RKKLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR--ILVLVSH 288
Cdd:PRK14243 142 KDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTH 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
401-596 |
3.87e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.39 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKdgpciyNNLEFGIDL-----DTRVaLVGPNGAGKSTLLKLLTGELLPTDGMI---------RKHSHVK 466
Cdd:PRK11124 3 IQLNGINCFYGA------HQALFDITLdcpqgETLV-LLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 467 IGR------------YH--QHLQEQLDLdlspLEYMMKCYPEIKE--KEEMRKIIGRYGLTGKQQVSPIrNLSDGQKCRV 530
Cdd:PRK11124 76 AIRelrrnvgmvfqqYNlwPHLTVQQNL----IEAPCRVLGLSKDqaLARAEKLLERLRLKPYADRFPL-HLSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 531 CLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGGM--MLVSHDFRLIQQVAQEIWVCEKQTI 596
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaETGItqVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
418-576 |
3.96e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.34 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 418 YNNLEFGIDLDT----RVALVGPNGAGKSTLLKLLTGELLPTDGMIR----KHSHVKIGRY-------------HQHLQE 476
Cdd:PRK10771 11 YHHLPMRFDLTVergeRVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqDHTTTPPSRRpvsmlfqennlfsHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 477 QLDLDLSPleyMMKCYPEikEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLA-WLAWQNPhMLFLDEPTNHLD-- 553
Cdd:PRK10771 91 NIGLGLNP---GLKLNAA--QREKLHAIARQMGIEDLLARLP-GQLSGGQRQRVALArCLVREQP-ILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*
gi 23956078 554 --IETIDALADAINEFEGGMMLVSH 576
Cdd:PRK10771 164 lrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
414-575 |
4.04e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.86 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 414 GPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshvkigryhqhLQEQLDLDLSPLEYM----- 488
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-------------LDGGDIDDPDVAEAChylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 489 ---MKcyPEIKEKEEM---RKIIG-----------RYGLTGKQQVsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNH 551
Cdd:PRK13539 81 rnaMK--PALTVAENLefwAAFLGgeeldiaaaleAVGLAPLAHL-PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 23956078 552 LDIETIDALADAINEF--EGGMMLVS 575
Cdd:PRK13539 158 LDAAAVALFAELIRAHlaQGGIVIAA 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
430-584 |
4.38e-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: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 430 RVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVK--IGryhqhLQEQLDLDLSPLEY-MMKC------YPEIKEKEE 500
Cdd:cd03220 50 RIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSslLG-----LGGGFNPELTGRENiYLNGrllglsRKEIDEKID 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 501 mrKIIGRYGLtGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGGMM--LVSHD 577
Cdd:cd03220 125 --EIIEFSEL-GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlKQGKTviLVSHD 201
|
....*..
gi 23956078 578 FRLIQQV 584
Cdd:cd03220 202 PSSIKRL 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
395-583 |
4.39e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.36 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 395 KIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKhSHVKIGRYHQ-- 472
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIADYSEaa 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 473 ------------H-----LQEQLDLDLspleymmkcyPEIKEkEEMRKIIGRYGLtGK--QQVSPI--------RNLSDG 525
Cdd:PRK11160 412 lrqaisvvsqrvHlfsatLRDNLLLAA----------PNASD-EALIEVLQQVGL-EKllEDDKGLnawlgeggRQLSGG 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 526 QKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQ 583
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNktVLMITHRLTGLEQ 539
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
210-291 |
4.54e-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: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 210 EMRASRILHGLGFTpAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL----KTFKRILVL 285
Cdd:cd03294 138 EERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELlrlqAELQKTIVF 216
|
....*.
gi 23956078 286 VSHSQD 291
Cdd:cd03294 217 ITHDLD 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
95-265 |
4.91e-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: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 95 NLSLTFHGQE--LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIgkrevpipehidiyhlTREMPPSEKTplqcvmevdt 172
Cdd:cd03247 5 NVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL----------------TGDLKPQQGE---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 173 eraMLEREAERLAHEDAECEKLMELYERleeldadkAEMRASRILHGLGftpamqrkklKDFSGGWRMRVALARALFIRP 252
Cdd:cd03247 59 ---ITLDGVPVSDLEKALSSLISVLNQR--------PYLFDTTLRNNLG----------RRFSGGERQRLALARILLQDA 117
|
170
....*....|...
gi 23956078 253 FMLLLDEPTNHLD 265
Cdd:cd03247 118 PIVLLDEPTVGLD 130
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
200-265 |
4.95e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 4.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 200 RLEELDADKAEMRASRILHGLGFTPAMQRKKLKdFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
106-308 |
5.90e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.21 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI--YHLTREmppsekTPLQCVMEVDTERAMLEREAER 183
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagYHITPE------TGNKNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 184 LAHEDAECEKLMELYERLEELDaDKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNH 263
Cdd:PRK13641 97 QLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23956078 264 LDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTNIIHMHNKKL 308
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
103-294 |
6.16e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 103 QELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTREMPpseKTPLQCVMEV-----DTERAML 177
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR----------------LLAGALK---GTPVAGCVDVpdnqfGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 178 EReaerLAHEDaeceklmelyerleeldaDKAEmrASRILHGLGF-TPAMQRKKLKDFSGGWRMRVALARALFIRPFMLL 256
Cdd:COG2401 104 DA----IGRKG------------------DFKD--AVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23956078 257 LDEPTNHLD-LDACVW---LEEELKTFKRILVLVSHSQDFLN 294
Cdd:COG2401 160 IDEFCSHLDrQTAKRVarnLQKLARRAGITLVVATHHYDVID 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
424-590 |
6.57e-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: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIRKHshvkiGRYHQHlqeqldldLSPleymmkcypeikeKE 499
Cdd:cd03216 18 GVSLSVRrgevHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GKEVSF--------ASP-------------RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 500 EMRKIIGR-YGLTG--KQQVSPIRNLSdgqkcrvclawlawQNPHMLFLDEPTNHLDIETIDALADAINEF--EG-GMML 573
Cdd:cd03216 72 ARRAGIAMvYQLSVgeRQMVEIARALA--------------RNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIF 137
|
170
....*....|....*..
gi 23956078 574 VSHDFRLIQQVAQEIWV 590
Cdd:cd03216 138 ISHRLDEVFEIADRVTV 154
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
234-265 |
6.83e-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: 6.83e-05
10 20 30
....*....|....*....|....*....|..
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
235-288 |
7.13e-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: 7.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLdACVWLEEELKTFK-RILVLVSH 288
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 ... |
521-590 |
7.34e-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: 7.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 521 NLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADA-----INEFEGGMMLVSHDfrlIQQVAQEIWV 590
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHK---LQYLPHADWI 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
424-554 |
8.00e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 45.22 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSHVKIGRyhqhlqeqlDLDLSPLEYMMKCY 492
Cdd:PRK09536 21 GVDLSVRegslVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddveALSARAASR---------RVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 493 PEIKEKEEM-----RKIIGRYGLTGKQQVS--------------PIRNLSDGQKCRVCLA-WLAWQNPhMLFLDEPTNHL 552
Cdd:PRK09536 92 FDVRQVVEMgrtphRSRFDTWTETDRAAVEramertgvaqfadrPVTSLSGGERQRVLLArALAQATP-VLLLDEPTASL 170
|
..
gi 23956078 553 DI 554
Cdd:PRK09536 171 DI 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
102-303 |
8.03e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.84 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSaigkrevpipehidiyHLTREMPPSEKTPLQCVMEVDTERA--MLER 179
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQ----------------NLNGILKPSSGRILFDGKPIDYSRKglMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 180 EAERLAHEDAECEKL-MELYERLE------ELDADKAEMRASRILHGLGFTPaMQRKKLKDFSGGWRMRVALARALFIRP 252
Cdd:PRK13636 82 ESVGMVFQDPDNQLFsASVYQDVSfgavnlKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 253 FMLLLDEPTNHLD----LDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHM 303
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
197-303 |
8.22e-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: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 197 LYERLEELDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEEL 276
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
90 100 110
....*....|....*....|....*....|
gi 23956078 277 KTF---KRILVLVSHSQDFLNGVCTNIIHM 303
Cdd:TIGR01257 2114 VSIireGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
399-575 |
8.70e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.87 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYtKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkhshVKIGRYHQHLQEQL 478
Cdd:PRK15056 5 AGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS----ILGQPTRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 479 DLDLSPLEYMMKCYPEIKEKEEMrkiIGRYGLTG---------KQQVSP--------------IRNLSDGQKCRVCLAWL 535
Cdd:PRK15056 80 VAYVPQSEEVDWSFPVLVEDVVM---MGRYGHMGwlrrakkrdRQIVTAalarvdmvefrhrqIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23956078 536 AWQNPHMLFLDEPTNHLDIETIDALADAINEF--EGGMMLVS 575
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELrdEGKTMLVS 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
233-293 |
8.98e-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: 8.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 233 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEE-----LKTFKRILVLVSHSQDFL 293
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
395-443 |
9.60e-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: 9.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 23956078 395 KIPPPVIMVQNVSFKYTKDGPcIYNNLEFGIDLDTRVALVGPNGAGKST 443
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
494-577 |
1.06e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 494 EIKEKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI-ETIDAlADAINEFEGG-- 570
Cdd:PRK13409 195 EVVERLGLENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrQRLNV-ARLIRELAEGky 263
|
....*..
gi 23956078 571 MMLVSHD 577
Cdd:PRK13409 264 VLVVEHD 270
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
162-590 |
1.21e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 162 TPLQCVMEVDTERAMLEREAERLAHEDAecekLMELYERLEELDADKAEMRASRILHGLgftpamqrkklkdfSGGWRMR 241
Cdd:PRK10261 115 TSLNPVFTVGEQIAESIRLHQGASREEA----MVEAKRMLDQVRIPEAQTILSRYPHQL--------------SGGMRQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 242 VALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL----VLVSHSQDFLNGVCTNIIHMHNKKlKYYTGNYDQ 317
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsmgvIFITHDMGVVAEIADRVLVMYQGE-AVETGSVEQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 318 --------YVKTRLEleenqmkrfhwEQDQIAHMK--NYIARFGHGSakLARQAQSKEKTLQKMMASGltERVVSDKTLS 387
Cdd:PRK10261 256 ifhapqhpYTRALLA-----------AVPQLGAMKglDYPRRFPLIS--LEHPAKQEPPIEQDTVVDG--EPILQVRNLV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 388 FYFPPCG----KIPPPVIMVQNVSFkytkdgpciynNLEFGIDLdtrvALVGPNGAGKSTLLKLLTGELLPTDGMIRKHS 463
Cdd:PRK10261 321 TRFPLRSgllnRVTREVHAVEKVSF-----------DLWPGETL----SLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 hvkigryhQHLQEQLDLDLSPLEYMMKC-----YPEIKEK-------------------EEMRK----IIGRYGLTGKQQ 515
Cdd:PRK10261 386 --------QRIDTLSPGKLQALRRDIQFifqdpYASLDPRqtvgdsimeplrvhgllpgKAAAArvawLLERVGLLPEHA 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 516 VSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:PRK10261 458 WRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
401-560 |
1.26e-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: 44.07 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLpTDGMIrkhshvkigryhqhlqeQLD- 479
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDI-----------------QIDg 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 480 --LDLSPLEYMMKCYPEIKEK--------------------EEMRKIIGRYGLTGKQQVSPIR----------NLSDGQK 527
Cdd:cd03289 65 vsWNSVPLQKWRKAFGVIPQKvfifsgtfrknldpygkwsdEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcVLSHGHK 144
|
170 180 190
....*....|....*....|....*....|...
gi 23956078 528 CRVCLAWLAWQNPHMLFLDEPTNHLDIETIDAL 560
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVI 177
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
397-577 |
1.26e-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: 43.92 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKY-TKDGPciYNNLEfGIDLDTR----VALVGPNGAGKSTllklltgeLLPTDGMIrkhshvkigRYH 471
Cdd:COG1116 4 AAPALELRGVSKRFpTGGGG--VTALD-DVSLTVAagefVALVGPSGCGKSTllrliaglEKPTSGEV---------LVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 472 QHLQEQLDLDLS--------------------PLEymMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVC 531
Cdd:COG1116 72 GKPVTGPGPDRGvvfqepallpwltvldnvalGLE--LRGVPKAERRERARELLELVGLAGFEDAYP-HQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23956078 532 LA-WLAwQNPHMLFLDEPTNHLDIETIDALAD---AINEFEG-GMMLVSHD 577
Cdd:COG1116 149 IArALA-NDPEVLLMDEPFGALDALTRERLQDellRLWQETGkTVLFVTHD 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
175-309 |
1.27e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 175 AMLEREAERLAHEDA-ECEKLMELYERLEELDADkaemrasrilhglgftpamqrkklkdFSGGWRMRVALARALFIRPF 253
Cdd:PRK10584 113 ALLRGESSRQSRNGAkALLEQLGLGKRLDHLPAQ--------------------------LSGGEQQRVALARAFNGRPD 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 254 MLLLDEPTNHLD-------LDACVWLEEELKTfkrILVLVSHSQDfLNGVCTNIIHMHNKKLK 309
Cdd:PRK10584 167 VLFADEPTGNLDrqtgdkiADLLFSLNREHGT---TLILVTHDLQ-LAARCDRRLRLVNGQLQ 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
424-581 |
1.28e-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: 43.79 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTR----VALVGPNGAGKSTLLklltgellptdGMIRKHSHVKIGRYHQHLQEQLDLDLSPLE------YMMKCYP 493
Cdd:TIGR01978 18 GVNLTVKkgeiHAIMGPNGSGKSTLS-----------KTIAGHPSYEVTSGTILFKGQDLLELEPDEraraglFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 494 E----IKEKEEMRKIIGryGLTGKQQVSPI------------------------RNL----SDGQKCRVCLAWLAWQNPH 541
Cdd:TIGR01978 87 EeipgVSNLEFLRSALN--ARRSARGEEPLdlldfekllkeklalldmdeeflnRSVnegfSGGEKKRNEILQMALLEPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23956078 542 MLFLDEPTNHLDIETIDALADAINEF---EGGMMLVSHDFRLI 581
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLL 207
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
425-578 |
1.31e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 425 IDLDTRVAL-VGPNGAGKST---------LLKLLTGELLPTDGMIRKHSHVKI--------GRYH--------------- 471
Cdd:COG0419 19 IDFDDGLNLiVGPNGAGKSTileairyalYGKARSRSKLRSDLINVGSEEASVelefehggKRYRierrqgefaefleak 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 472 -QHLQEQLD--LDLSPLEYMMKCYPEIKEKEEmRKIIGRYGLTGKQQV--------SPIRNLSDGQKCRVCLAWLAwqnp 540
Cdd:COG0419 99 pSERKEALKrlLGLEIYEELKERLKELEEALE-SALEELAELQKLKQEilaqlsglDPIETLSGGERLRLALADLL---- 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 23956078 541 hMLFLDepTNHLDIETIDALADAINEfeggMMLVSHDF 578
Cdd:COG0419 174 -SLILD--FGSLDEERLERLLDALEE----LAIITHVI 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
408-576 |
1.46e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 408 FKYTKDGPCIY--NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQL----DLD 481
Cdd:PRK13545 28 FFRSKDGEYHYalNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtgieNIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 482 LSPLeyMMKCYPEiKEKEEMRKIIgRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALA 561
Cdd:PRK13545 108 LKGL--MMGLTKE-KIKEIIPEII-EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170
....*....|....*...
gi 23956078 562 DAINEF-EGG--MMLVSH 576
Cdd:PRK13545 184 DKMNEFkEQGktIFFISH 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
232-288 |
1.50e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956078 232 KDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK----RILVLVSH 288
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAH 1417
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
234-288 |
1.54e-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: 1.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDAcvwLEEELKtfKRILVLVSH 288
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMK--GRTTIVIAH 533
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
431-590 |
1.58e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDGMIrkHSHVKIGRYHQHLQEqlDLDLSPLEYMMKCYPEIKE---KEEmrkIIGR 507
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKP--DYDGTVEDLLRSITDDLGSsyyKSE---IIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 508 YGLTgKQQVSPIRNLSDGQKCRV----CLAwlawQNPHMLFLDEPTNHLDIETIDALADAIN----EFEGGMMLVSHDFR 579
Cdd:PRK13409 441 LQLE-RLLDKNVKDLSGGELQRVaiaaCLS----RDADLYLLDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHDIY 515
|
170
....*....|.
gi 23956078 580 LIQQVAQEIWV 590
Cdd:PRK13409 516 MIDYISDRLMV 526
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
401-584 |
1.65e-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: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGmirkHSHVK--IGRYHQH----- 473
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG----HVHMKgsVAYVPQQawiqn 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 --LQEQLDL--DLSPLEY---MMKC--YPEIkekeEM-----RKIIGRYGLtgkqqvspirNLSDGQKCRVCLAWLAWQN 539
Cdd:TIGR00957 713 dsLRENILFgkALNEKYYqqvLEACalLPDL----EIlpsgdRTEIGEKGV----------NLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23956078 540 PHMLFLDEPTNHLDIETIDALADAINEFEGGM-----MLVSHDFRLIQQV 584
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQV 828
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
431-594 |
1.73e-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: 42.56 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigryhqhlqeqlDLDLSPLEYMmkcypeikekeemrkiigrygl 510
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------EWDGITPVYK---------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 511 tgKQQVSpirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF----EGGMMLVSHDFRLIQQVAQ 586
Cdd:cd03222 67 --PQYID----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSD 140
|
....*...
gi 23956078 587 EIWVCEKQ 594
Cdd:cd03222 141 RIHVFEGE 148
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
431-588 |
1.80e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.80 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDG----------MIR-KHSHVKIGRYHQ--HLQEQLDL---------DLSPLEYM 488
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtinLVRdKDGQLKVADKNQlrLLRTRLTMvfqhfnlwsHMTVLENV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 489 MKCYPEI------KEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALAD 562
Cdd:PRK10619 114 MEAPIQVlglskqEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR 193
|
170 180
....*....|....*....|....*....
gi 23956078 563 AINEF--EGG-MMLVSHDFRLIQQVAQEI 588
Cdd:PRK10619 194 IMQQLaeEGKtMVVVTHEMGFARHVSSHV 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
106-261 |
1.87e-04 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 43.19 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKREVPIPEHiDIYHL-------TREMPPSektpl 164
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTImgllpprsgsirfdGRDITGLPPH-ERARAgigyvpeGRRIFPE----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 165 qcvMEVDtERAMLEREAERLAHEDAECEKLMELYERLEEldadkaemrasrilhglgftpaMQRKKLKDFSGGWRMRVAL 244
Cdd:cd03224 90 ---LTVE-ENLLLGAYARRRAKRKARLERVYELFPRLKE----------------------RRKQLAGTLSGGEQQMLAI 143
|
170
....*....|....*..
gi 23956078 245 ARALFIRPFMLLLDEPT 261
Cdd:cd03224 144 ARALMSRPKLLLLDEPS 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
230-288 |
1.92e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 44.03 E-value: 1.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 230 KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF----KRILvLVSH 288
Cdd:PRK13537 135 KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlargKTIL-LTTH 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
235-265 |
1.92e-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: 1.92e-04
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
432-561 |
2.18e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.62 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 432 ALVGPNGAGKSTLLKLLTGELLPTDGMI-------RKHSHVKIGRYHQHLQEQLdldlSPLEYM-------MKCYPeike 497
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqplESWSSKAFARKVAYLPQQL----PAAEGMtvrelvaIGRYP---- 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 498 keeMRKIIGRYGLTGKQQV---------SPIRN-----LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI-ETIDALA 561
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) ... |
431-577 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPT----------DGMIRKHSHVKIGRYHQHLQE-QLD-------LDLSPLEYMMKCY 492
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwDEILDEFRGSELQNYFTKLLEgDVKvivkpqyVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 493 PEIKEKEE---MRKIIGRYGLTGKQQvSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIE---TIDALADAINE 566
Cdd:cd03236 109 ELLKKKDErgkLDELVDQLELRHVLD-RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAE 187
|
170
....*....|.
gi 23956078 567 FEGGMMLVSHD 577
Cdd:cd03236 188 DDNYVLVVEHD 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
106-353 |
2.53e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDI----------YHLTREMPPSEKTPLQCVMEVDTERA 175
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgsaaliaisSGLNGQLTGIENIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 176 MLEREAERLahEDAECEKLMElyerleeldadkaemrasrilhglgftpamqrKKLKDFSGGWRMRVALARALFIRPFML 255
Cdd:PRK13545 120 IKEIIPEII--EFADIGKFIY--------------------------------QPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 256 LLDEPTNHLD---LDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYY------TGNYDQYVKTRLELE 326
Cdd:PRK13545 166 VIDEALSVGDqtfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDEFLKKYNQMS 245
|
250 260
....*....|....*....|....*..
gi 23956078 327 ENQMKRFHWEQdqiahmknyIARFGHG 353
Cdd:PRK13545 246 VEERKDFREEQ---------ISQFQHG 263
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
105-288 |
2.55e-04 |
|
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: 42.84 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 105 LLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI--------------GKrevPIPEHIDIYhLTREmppsektplqcVMEV 170
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqggqvlldGK---PISQYEHKY-LHSK-----------VSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 171 DTERAMLERE-AERLAH--EDAECEKLMELyerleeldADKAemrasrilHGLGFTPAMQR-------KKLKDFSGGWRM 240
Cdd:cd03248 94 GQEPVLFARSlQDNIAYglQSCSFECVKEA--------AQKA--------HAHSFISELASgydtevgEKGSQLSGGQKQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23956078 241 RVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF--KRILVLVSH 288
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
223-304 |
2.74e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 223 TPAMQrKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSHSQDFLNGVCTN 299
Cdd:PRK10762 386 TPSME-QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDR 464
|
....*
gi 23956078 300 IIHMH 304
Cdd:PRK10762 465 ILVMH 469
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
401-596 |
2.84e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.23 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIY---NNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIR---------------KH 462
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 463 SHVKIGRYHQHLQEQL-------DLDLSPLEYMMkcypEIKE-KEEMRKIIGRYGLTGK-QQVSPIRnLSDGQKCRVCLA 533
Cdd:PRK13646 83 VRKRIGMVFQFPESQLfedtverEIIFGPKNFKM----NLDEvKNYAHRLLMDLGFSRDvMSQSPFQ-MSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 534 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEFE----GGMMLVSHDFRLIQQVAQEIWVCEKQTI 596
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
214-265 |
3.51e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 23956078 214 SRILHGLGFTPAMQRKkLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK13409 435 SEIIKPLQLERLLDKN-VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
207-291 |
3.51e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.81 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 207 DKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEELKT-FKRI--- 282
Cdd:PRK13649 119 EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG----RKELMTlFKKLhqs 194
|
90
....*....|..
gi 23956078 283 ---LVLVSHSQD 291
Cdd:PRK13649 195 gmtIVLVTHLMD 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
201-260 |
3.57e-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: 3.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 201 LE--ELDADKAEMRASRILHGLGFT-----PAMQrkklkdFSGGWRMRVALARALFIRPFMLLLDEP 260
Cdd:COG1137 103 LElrKLSKKEREERLEELLEEFGIThlrksKAYS------LSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
102-265 |
3.68e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.55 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHI-----DIYHL-TREMPPSEKtplQCVMEVDTERA 175
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLkNREVPFLRR---QIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 176 MLEREAErlaheDAECEKLMelyerLEELDADKAEMRASRILHGLGFTpamqrKKLKDF----SGGWRMRVALARALFIR 251
Cdd:PRK10908 91 LMDRTVY-----DNVAIPLI-----IAGASGDDIRRRVSAALDKVGLL-----DKAKNFpiqlSGGEQQRVGIARAVVNK 155
|
170
....*....|....
gi 23956078 252 PFMLLLDEPTNHLD 265
Cdd:PRK10908 156 PAVLLADEPTGNLD 169
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
401-564 |
3.91e-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: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKYTKDGPCIYNnlefgIDLD--TR--VALVGPNGAGKSTLLKLLTGELLPTDGMIR-------KHSH----- 464
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQN-----INLSvpSRgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsSLSHsvlrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 465 -------------------VKIGRYHQHLQEQLDLDLSPLEYMMKCYPEikekeemrkiiGRYGLTGKQQvspiRNLSDG 525
Cdd:PRK10790 416 gvamvqqdpvvladtflanVTLGRDISEEQVWQALETVQLAELARSLPD-----------GLYTPLGEQG----NNLSVG 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 23956078 526 QKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 564
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL 519
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
104-310 |
3.97e-04 |
|
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: 42.32 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 104 ELLSDTKLELNSGRRYGLIGLNGIGKSM---LLSAI-----GKREVP--IPEHIDIYHLTR-------------EMPPSE 160
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLlqptsGEVRVAglVPWKRRKKFLRRigvvfgqktqlwwDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 161 KTPLQcvmevdteRAMLEREAERLAHEDAECEKLMELyerleeldadkaemraSRILHglgfTPAMQrkklkdFSGGWRM 240
Cdd:cd03267 115 SFYLL--------AAIYDLPPARFKKRLDELSELLDL----------------EELLD----TPVRQ------LSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 241 RVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEELKTFKRILV--------LVSHSQDFLNGVCTNIIHMHNKKLKY 310
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVA----QENIRNFLKEYNrergttvlLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
233-305 |
4.34e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 4.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 233 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF----KRILVLVSHSQDFLNGVCTNIIHMHN 305
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
226-303 |
4.45e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.01 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 226 MQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTFKRILVL-VSHSQDFLNGvCTNII 301
Cdd:PRK10247 130 ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEiihRYVREQNIAVLwVTHDKDEINH-ADKVI 208
|
..
gi 23956078 302 HM 303
Cdd:PRK10247 209 TL 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
235-265 |
4.52e-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: 4.52e-04
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
209-331 |
4.69e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.77 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 209 AEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDldaCVWLEEELKTFKRI------ 282
Cdd:PRK13651 141 AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD---PQGVKEILEIFDNLnkqgkt 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 23956078 283 LVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLeLEENQMK 331
Cdd:PRK13651 218 IILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKF-LIENNME 265
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
431-553 |
4.85e-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: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPtdGMIRKHSHV----KIGRYHQHLQ----EQLDL---DLSPLEYMM--------KC 491
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLlngmPIDAKEMRAIsayvQQDDLfipTLTVREHLMfqahlrmpRR 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 492 YPEIKEKEEMRKIIGRYGL-----TGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:TIGR00955 132 VTKKEKRERVDEVLQALGLrkcanTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
401-596 |
5.15e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKY-TKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYH-QHLQEQL 478
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH-DLRDYTlASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 479 DLdLSPLEYMMK-------CYP--------EIKEKEEMR--------------KIIGRYGLtgkqqvspirNLSDGQKCR 529
Cdd:PRK11176 420 AL-VSQNVHLFNdtianniAYArteqysreQIEEAARMAyamdfinkmdngldTVIGENGV----------LLSGGQRQR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 530 VCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGG--MMLVSHDFRLIQQvAQEIWVCEKQTI 596
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
203-265 |
5.38e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.39 E-value: 5.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 203 ELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK15079 131 KLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
233-308 |
5.61e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.30 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 233 DFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwlEEEL--------KTFKRILVLVSHSQDFLNGVCTNIIHMH 304
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG----EEDFinlferlnKEYKKRIIMVTHNMDQVLRIADEVIVMH 225
|
....
gi 23956078 305 NKKL 308
Cdd:PRK13645 226 EGKV 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
496-563 |
5.67e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.70 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 496 KEKEEMRKIIGRYGL--TGKQQvsPIRNLSDG--QKcrVCLA-WLAwQNPHMLFLDEPTNHLDI-------ETIDALADA 563
Cdd:COG1129 369 RERALAEEYIKRLRIktPSPEQ--PVGNLSGGnqQK--VVLAkWLA-TDPKVLILDEPTRGIDVgakaeiyRLIRELAAE 443
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
400-576 |
5.75e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDG----PCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI-------RKHSHV--- 465
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtSDEENLwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 466 --KIGRYHQHLQEQL-------DLDLSPlEYMMKCYPEIKEK-EEMRKIIGRYgltgKQQVSPIRNLSDGQKCRVCLAWL 535
Cdd:PRK13633 84 rnKAGMVFQNPDNQIvativeeDVAFGP-ENLGIPPEEIRERvDESLKKVGMY----EYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23956078 536 AWQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSH 576
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
235-265 |
6.75e-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: 6.75e-04
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-578 |
7.95e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYTkdGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMiRKHSHVKIG-----RYHQH 473
Cdd:PRK14271 20 PAMAAVNLTLGFA--GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGgrsifNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 LQEQLDLDL---SPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQV-----------------SPIRnLSDGQKCRVCLA 533
Cdd:PRK14271 97 LEFRRRVGMlfqRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQArltevglwdavkdrlsdSPFR-LSGGQQQLLCLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23956078 534 WLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGM--MLVSHDF 578
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLtvIIVTHNL 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
91-136 |
7.99e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 7.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 23956078 91 VHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI 136
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI 47
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
235-288 |
8.04e-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: 8.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVSH 288
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
102-265 |
8.22e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.52 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 102 GQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-------GKREVPIPEhidiyhlTREMPPSEKtpLQCVMEVDTER 174
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyqGSLKINGIE-------LRELDPESW--RKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 175 AMLE---REAERLAHEDAECEKLMELYERleeldADKAEMrASRILHGLGFTPAMQRKKLkdfSGGWRMRVALARALFIR 251
Cdd:PRK11174 433 QLPHgtlRDNVLLGNPDASDEQLQQALEN-----AWVSEF-LPLLPQGLDTPIGDQAAGL---SVGQAQRLALARALLQP 503
|
170
....*....|....
gi 23956078 252 PFMLLLDEPTNHLD 265
Cdd:PRK11174 504 CQLLLLDEPTASLD 517
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
401-596 |
8.40e-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: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSfKYTKDGPCIyNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVK-----IGRYH 471
Cdd:cd03296 3 IEVRNVS-KRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPvqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 472 QH--------LQEQLDLDLSpLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHML 543
Cdd:cd03296 81 QHyalfrhmtVFDNVAFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 544 FLDEPTNHLDIETIDALADAINEFEGGM----MLVSHDFRLIQQVAQEIWVCEKQTI 596
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
214-265 |
8.52e-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: 8.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 23956078 214 SRILHGLGFTPAMQrKKLKDFSGGWRMRVALARALfIRPF-MLLLDEPTNHLD 265
Cdd:COG1245 437 TEIIKPLGLEKLLD-KNVKDLSGGELQRVAIAACL-SRDAdLYLLDEPSAHLD 487
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
93-294 |
8.78e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 41.21 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 93 IINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAI-GkrevpipehIDIYHLTR-----------EMPPse 160
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmG---------HPKYEVTSgsilldgedilELSP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 161 ktplqcvmevdTERA-----------------------MLEREAERLAHEDAEcEKLMELYERLEELDADKaEMrASRIL 217
Cdd:COG0396 72 -----------DERAragiflafqypveipgvsvsnflRTALNARRGEELSAR-EFLKLLKEKMKELGLDE-DF-LDRYV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 218 HGlgftpamqrkklkDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDAcvwLE------EELKTFKRILVLVSHSQD 291
Cdd:COG0396 138 NE-------------GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA---LRivaegvNKLRSPDRGILIITHYQR 201
|
...
gi 23956078 292 FLN 294
Cdd:COG0396 202 ILD 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
425-598 |
9.22e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 425 IDLDTRV----ALVGPNGAGKSTLLKLLTGELLPTDGMI----RKHSHVK--------IGRYHQHL--------QEQLDL 480
Cdd:PRK09700 24 VNLTVYPgeihALLGENGAGKSTLMKVLSGIHEPTKGTItinnINYNKLDhklaaqlgIGIIYQELsvideltvLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 481 DLSPLEYMMKC----YPEIKEKEEMrkIIGRYGLtgkqQVSP---IRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:PRK09700 104 GRHLTKKVCGVniidWREMRVRAAM--MLLRVGL----KVDLdekVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23956078 554 IETIDALADAINEFEG---GMMLVSHDFRLIQQvaqeiwVCEKQTITK 598
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKegtAIVYISHKLAEIRR------ICDRYTVMK 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
424-583 |
9.67e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 424 GIDLDTRVA----LVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHvKIGRYHQH----LQEQLDLDLSPLEYMMK----- 490
Cdd:PRK10908 20 GVTFHMRPGemafLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH-DITRLKNRevpfLRRQIGMIFQDHHLLMDrtvyd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 491 --CYPEI---KEKEEMRKIIG----RYGLTGKQQVSPIRnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDietiDALA 561
Cdd:PRK10908 99 nvAIPLIiagASGDDIRRRVSaaldKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALS 173
|
170 180
....*....|....*....|....*....
gi 23956078 562 DAI-------NEFEGGMMLVSHDFRLIQQ 583
Cdd:PRK10908 174 EGIlrlfeefNRVGVTVLMATHDIGLISR 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
235-305 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE-----ELKtFKRILVLVSHSQDFLNgVCTNIIHMHN 305
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLL-NNKTRILVTHQLQLLP-HADQIVVLDN 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
231-279 |
1.17e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 23956078 231 LKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF 279
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
106-443 |
1.23e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 106 LSDTK------LELNSGRRYGLIGLNGIGKSMLLSAI--------GKREVPIpEHI------DIYHLTREMPPSEKTPLQ 165
Cdd:PRK10938 13 LSDTKtlqlpsLTLNAGDSWAFVGANGSGKSALARALagelpllsGERQSQF-SHItrlsfeQLQKLVSDEWQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 166 CVMEVDTERAMleREAERLAHEDAE-CEKLMELyerleeldadkaemrasrilhgLGFTPAMQRKkLKDFSGGWRMRVAL 244
Cdd:PRK10938 92 SPGEDDTGRTT--AEIIQDEVKDPArCEQLAQQ----------------------FGITALLDRR-FKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 245 ARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKR---ILVLVshsqdfLNgvctniihmhnkklkyytgnydqyvkt 321
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLV------LN--------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 322 rleleenqmkRFhweqDQIAHMKNYIARFGhgSAKLARQAqSKEKTLQKMMASGL--TERVVsDKTLSFYFPPCGK--IP 397
Cdd:PRK10938 194 ----------RF----DEIPDFVQFAGVLA--DCTLAETG-EREEILQQALVAQLahSEQLE-GVQLPEPDEPSARhaLP 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 23956078 398 P--PVIMVQNVSFKYTkDGPcIYNNLEFGIDLDTRVALVGPNGAGKST 443
Cdd:PRK10938 256 AnePRIVLNNGVVSYN-DRP-ILHNLSWQVNPGEHWQIVGPNGAGKST 301
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
403-548 |
1.32e-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: 40.60 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 403 VQNVSFKYTKDgpCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRkHSHVKIGRYHQHLQEQLDL-- 480
Cdd:cd03218 3 AENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL-LDGQDITKLPMHKRARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 481 ---------DLS-------PLEYMMKCYPEIKEKEEmrkiigryGLTGKQQVSPIRN-----LSDGQKCRVCLAWLAWQN 539
Cdd:cd03218 80 lpqeasifrKLTveenilaVLEIRGLSKKEREEKLE--------ELLEEFHITHLRKskassLSGGERRRVEIARALATN 151
|
....*....
gi 23956078 540 PHMLFLDEP 548
Cdd:cd03218 152 PKFLLLDEP 160
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
400-578 |
1.33e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.23 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDGPC-IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSH-----------VKI 467
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGK----QQVSPIRnLSDGQKCRVCLAWLAWQNPHML 543
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRPEII 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 23956078 544 FLDEPTNHLD----IETIDALADAINEFEGGMMLVSHDF 578
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDL 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
204-265 |
1.35e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.94 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 204 LDADKAEMRASRILHGLGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
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 ... |
235-265 |
1.37e-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: 1.37e-03
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
400-577 |
1.38e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.87 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 400 VIMVQNVSFKYTKDGP-CIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHV-----------KI 467
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQHLQEQL-------DLDLSpLEYMMKCYPEIKEK-EEMRKIIGRYGLTGKQqvsPIRnLSDGQKCRVCLAWLAWQN 539
Cdd:PRK13650 84 GMVFQNPDNQFvgatvedDVAFG-LENKGIPHEEMKERvNEALELVGMQDFKERE---PAR-LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23956078 540 PHMLFLDEPTNHLD-------IETIDALADainefEGGMMLVS--HD 577
Cdd:PRK13650 159 PKIIILDEATSMLDpegrlelIKTIKGIRD-----DYQMTVISitHD 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
494-577 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 494 EIKEKEEMRKIIGRygltgkqqvsPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEF-EGG-- 570
Cdd:COG1245 195 ELAEKLGLENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaEEGky 264
|
....*..
gi 23956078 571 MMLVSHD 577
Cdd:COG1245 265 VLVVEHD 271
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
235-261 |
1.90e-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: 1.90e-03
10 20
....*....|....*....|....*..
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPT 261
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-576 |
2.40e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 2.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 517 SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGM--MLVSH 576
Cdd:PRK14247 142 APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMtiVLVTH 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
230-289 |
2.57e-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: 2.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956078 230 KLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEE---ELKTfKRILVLVSHS 289
Cdd:COG1117 147 RLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEElilELKK-DYTIVIVTHN 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
207-290 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 207 DKAEMRAsRILHG---LGFTPAMQRKKlKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRIL 283
Cdd:PRK11650 107 PKAEIEE-RVAEAariLELEPLLDRKP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRL 184
|
90
....*....|.
gi 23956078 284 ----VLVSHSQ 290
Cdd:PRK11650 185 kttsLYVTHDQ 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
205-265 |
2.76e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.71 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956078 205 DADKAEMR-ASRILHGLGFtpaMQRKKLK----------DFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK13657 435 DATDEEMRaAAERAQAHDF---IERKPDGydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
399-620 |
2.83e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 399 PVIMVQNVSFKYTKDGP--CIYNNLEFGIDLDTRVALVGPNGAGKS-TLLKLLTGELLP----TDGMIRKHS-------- 463
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGesllhase 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 464 ----HVKIGRYHQHLQEQLdLDLSPLEYMMKCYPEIKEKEE-MRKIIGRYGLTGKQQVSPIRN-----------LSDGQK 527
Cdd:PRK15134 84 qtlrGVRGNKIAMIFQEPM-VSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQaakrltdyphqLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 528 CRVCLAWLAWQNPHMLFLDEPTNHLDIeTIDA-----LADAINEFEGGMMLVSHDFRLIQQVAQEIWV-----CEKQTIT 597
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDV-SVQAqilqlLRELQQELNMGLLFITHNLSIVRKLADRVAVmqngrCVEQNRA 241
|
250 260
....*....|....*....|....
gi 23956078 598 KwpgDILAYKEH-LKSKLVDEEPQ 620
Cdd:PRK15134 242 A---TLFSAPTHpYTQKLLNSEPS 262
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
225-265 |
3.01e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 40.00 E-value: 3.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 23956078 225 AMQRKKLKDF--------SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK13635 124 ALRQVGMEDFlnrephrlSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
391-577 |
3.12e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.20 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 391 PPCGKIPPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrkhshvkigry 470
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 471 hqhlqeQLD-LDLS-------PLEYMMKCYP-----------------------EIKEK-EEMRKIIGRYGLTGKQQvsp 518
Cdd:PRK11607 77 ------MLDgVDLShvppyqrPINMMFQSYAlfphmtveqniafglkqdklpkaEIASRvNEMLGLVHMQEFAKRKP--- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 519 iRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDAL----ADAINEFEGGMMLVSHD 577
Cdd:PRK11607 148 -HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERVGVTCVMVTHD 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
417-556 |
3.15e-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: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 417 IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrKHSHvKIGRYHQ-------HLQEQLDLDLSPLEY-- 487
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-KHSG-RISFSPQtswimpgTIKDNIIFGLSYDEYry 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 488 ---MMKCYPE---IKEKEEMRKIIGRYGLTgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIET 556
Cdd:TIGR01271 519 tsvIKACQLEediALFPEKDKTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
234-288 |
3.18e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 3.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFK----RILVLVSH 288
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenRITIIIAH 638
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
95-137 |
3.21e-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: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 23956078 95 NLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIG 137
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS 48
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
234-289 |
3.24e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.69 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 234 FSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTF--KRILVLVSHS 289
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
467-577 |
3.43e-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: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 467 IGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQqvsPIRNLSDGQKcRV-CLAWLAWQNPH---M 542
Cdd:pfam13304 185 LQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGEL---PAFELSDGTK-RLlALLAALLSALPkggL 260
|
90 100 110
....*....|....*....|....*....|....*...
gi 23956078 543 LFLDEPTNHLDIETIDALADAINEFEGG---MMLVSHD 577
Cdd:pfam13304 261 LLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHS 298
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
423-443 |
3.67e-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: 3.67e-03
10 20
....*....|....*....|....*
gi 23956078 423 FGIDLDTR----VALVGPNGAGKST 443
Cdd:cd03224 17 FGVSLTVPegeiVALLGRNGAGKTT 41
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
401-590 |
3.87e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 401 IMVQNVSFKY-TKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDG-MIRKHSH-----------VKI 467
Cdd:PTZ00265 383 IQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHnlkdinlkwwrSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 468 GRYHQ------------------------HLQEQLD------------------------------LDLSPLEYMMKCYP 493
Cdd:PTZ00265 463 GVVSQdpllfsnsiknnikyslyslkdleALSNYYNedgndsqenknkrnscrakcagdlndmsntTDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 494 EIKEKE----EMRKIIGRY--GLTGKQQV---SPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAI 564
Cdd:PTZ00265 543 TIKDSEvvdvSKKVLIHDFvsALPDKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|
gi 23956078 565 NEFEGG----MMLVSHDFRLIqQVAQEIWV 590
Cdd:PTZ00265 623 NNLKGNenriTIIIAHRLSTI-RYANTIFV 651
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
201-265 |
4.00e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.71 E-value: 4.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 201 LEELDADKAEMRaSRILHGLGFTpAMQRKKLKD---FSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK13650 107 LENKGIPHEEMK-ERVNEALELV-GMQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
231-265 |
4.29e-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: 4.29e-03
10 20 30
....*....|....*....|....*....|....*
gi 23956078 231 LKdFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:COG5265 493 LK-LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
522-590 |
4.30e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956078 522 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI----ETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
522-590 |
4.43e-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: 4.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 522 LSDGQKCRVCLAW-LAwQNPHMLFLDEPTNHLDIeTIDA-----LADAINEFEGGMMLVSHDFRLIQQVAQEIWV 590
Cdd:COG4172 157 LSGGQRQRVMIAMaLA-NEPDLLIADEPTTALDV-TVQAqildlLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
417-556 |
4.88e-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: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 417 IYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIrKHSHvKIGRYHQ-------HLQEQLDLDLSPLEYMM 489
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-KHSG-RISFSSQfswimpgTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956078 490 K-----CYPE---IKEKEEMRKIIGRYGLTgkqqvspirnLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIET 556
Cdd:cd03291 130 KsvvkaCQLEediTKFPEKDNTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
207-261 |
5.08e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 39.62 E-value: 5.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 207 DKAEMR--ASRILHGLGFT--PamqRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPT 261
Cdd:COG1129 113 DWRAMRrrARELLARLGLDidP---DTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
397-577 |
5.10e-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: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKYtkDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTllklltgeLLPTDGMI----RKHSHVKIGRYH- 471
Cdd:COG3842 2 AMPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmiagfETPDSGRIlldgRDVTGLPPEKRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 472 ----QhlqeqlDLDLSPleYM-----------MKCYP--EIKEK-EEMRKIIgryGLTGKQQVSPiRNLSDGQKCRVCLA 533
Cdd:COG3842 80 gmvfQ------DYALFP--HLtvaenvafglrMRGVPkaEIRARvAELLELV---GLEGLADRYP-HQLSGGQQQRVALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23956078 534 -WLAwQNPHMLFLDEPTNHLD----IETIDALADAINEFEGGMMLVSHD 577
Cdd:COG3842 148 rALA-PEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
522-553 |
5.55e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.99 E-value: 5.55e-03
10 20 30
....*....|....*....|....*....|..
gi 23956078 522 LSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
405-588 |
5.64e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 39.30 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 405 NVSFKYTKdgpcIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKH----SHV-----KIGRYHQH-- 473
Cdd:PRK10851 9 KKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvSRLhardrKVGFVFQHya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 474 ------LQEQLDLDLSPLEYMMKCYPEIKEKEEMRkiigrygLTGKQQVSPIRN-----LSDGQKCRVCLAWLAWQNPHM 542
Cdd:PRK10851 85 lfrhmtVFDNIAFGLTVLPRRERPNAAAIKAKVTQ-------LLEMVQLAHLADrypaqLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23956078 543 LFLDEPTNHLDIETIDALADAI----NEFEGGMMLVSHDfrliQQVAQEI 588
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHD----QEEAMEV 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
208-293 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 208 KAEMRASRILHGLGFTPAMQRKKLKD----FSGGWRMRVALARALFIRPFMLLLDEPTNHLD-------LDACVWLEEEL 276
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVL 810
|
90
....*....|....*..
gi 23956078 277 KTFKRIlvLVSHSQDFL 293
Cdd:TIGR00957 811 KNKTRI--LVTHGISYL 825
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
519-553 |
5.82e-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: 5.82e-03
10 20 30
....*....|....*....|....*....|....*
gi 23956078 519 IRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLD 553
Cdd:cd03234 141 VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
235-265 |
6.06e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.40 E-value: 6.06e-03
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
397-588 |
6.21e-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: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 397 PPPVIMVQNVSFKYtkDGPCIYNnlefGIDLDTR----VALVGPNGAGKSTLLKLLTGELLPTDGMI------------- 459
Cdd:COG1127 2 SEPMIEVRNLTKSF--GDRVVLD----GVSLDVPrgeiLAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 460 -----RKhshvKIGRYHQH----------------LQEQLDLDlspleymmkcypeikeKEEMRKI----IGRYGLTGKQ 514
Cdd:COG1127 76 elyelRR----RIGMLFQGgalfdsltvfenvafpLREHTDLS----------------EAEIRELvlekLELVGLPGAA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 515 QVSPiRNLSDGQKCRVCLA-WLAwQNPHMLFLDEPTNHLDIETIDALADAINE----FEGGMMLVSHDFRLIQQVAQEI 588
Cdd:COG1127 136 DKMP-SELSGGMRKRVALArALA-LDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRV 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
423-443 |
6.31e-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: 6.31e-03
10 20
....*....|....*....|....*
gi 23956078 423 FGIDLDTR----VALVGPNGAGKST 443
Cdd:COG0410 20 HGVSLEVEegeiVALLGRNGAGKTT 44
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
208-265 |
6.54e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.06 E-value: 6.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 23956078 208 KAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:PRK13631 151 EAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
431-588 |
6.65e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 39.71 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 431 VALVGPNGAGKSTLLKLLTGELLPTDG-------------------MIRKHSHVKIGRYH--QHLQEQLDLDLsPLEYMM 489
Cdd:PRK10535 37 VAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqdvatldadalaqLRREHFGFIFQRYHllSHLTAAQNVEV-PAVYAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956078 490 KcyPEIKEKEEMRKIIGRYGLTGKQQVSPiRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDI---ETIDALADAINE 566
Cdd:PRK10535 116 L--ERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLRD 192
|
170 180
....*....|....*....|..
gi 23956078 567 FEGGMMLVSHDFRLIQQvAQEI 588
Cdd:PRK10535 193 RGHTVIIVTHDPQVAAQ-AERV 213
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
235-265 |
8.18e-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: 8.18e-03
10 20 30
....*....|....*....|....*....|.
gi 23956078 235 SGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
212-265 |
9.56e-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: 9.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956078 212 RASRILHGLGFTPAMQRK-----KLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLD 265
Cdd:TIGR00955 140 RVDEVLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| |
