|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-527 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 718.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 4 VTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEERVLD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 84 VVIKGHERLYEVMKEKDEIYMKPDFSDEDGIRAAELEGEFAEMNGWNAEADAASLLSGLGISADLHDKQMSELENNQKVK 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 164 VLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYDFWYQS 243
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 244 SQLAQKMAQEQNKKKEEKIKELQDFIARFSANASKSKQATSRKKQLEKIELDDIQPSSrRYPYVKFTPEREIGNDLLTVQ 323
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRD-KTVEIRFPPPERLGKKVLELE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 324 GLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFFEgvDMNLV 403
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDP--DKTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 404 DWLRQYAPEDeqTETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGL 483
Cdd:COG0488 398 DELRDGAPGG--TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499595078 484 ASFKGSIIFTSYDFEFINTIANRVIDLNQsGGLsKEVP--YEEYLQ 527
Cdd:COG0488 476 DDFPGTVLLVSHDRYFLDRVATRILEFED-GGV-REYPggYDDYLE 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-531 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 668.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEER 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHERLYEVMKEKDEIYMKPDFSDEDGIRAAELEGEFAEMNGWNAEADAASLLSGLGISADLHDKQMSELENNQ 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 161 KVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYDFW 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 241 YQSSQLAQKMAQEQNKKKEEKIKELQDFIARFSANASKSKQATSRKKQLEKIELDDIQPSSRRYPYVKFTPEREIGNDLL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 321 TVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFFEGvDM 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFEN-DL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 401 NLVDWLRQYAPE--DEQTetfLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITA 478
Cdd:PRK15064 400 TLFDWMSQWRQEgdDEQA---VRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIES 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499595078 479 VNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSGGLSKEVPYEEYLQEIGV 531
Cdd:PRK15064 477 LNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-504 |
1.16e-82 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 267.57 E-value: 1.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 12 GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGeIDSQ-TGHVSMGKDERLAVLKQDHFAYEEERVLDVVIKGHE 90
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 91 RLYEVMKEKDEIYMKpdFSDED------GIRAAELEGEFAEMNGWNAE------ADAASLLSGlgisadlhDKQMSELEN 158
Cdd:TIGR03719 95 EIKDALDRFNEISAK--YAEPDadfdklAAEQAELQEIIDAADAWDLDsqleiaMDALRCPPW--------DADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYD 238
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 239 FWYQssQLAQKMAQEQNkkkeeKIKELQDFIA------RFSANA--SKSKQATSRKKQL------EKIELDDIQ-PSSRR 303
Cdd:TIGR03719 245 SWLE--QKQKRLEQEEK-----EESARQKTLKrelewvRQSPKGrqAKSKARLARYEELlsqefqKRNETAEIYiPPGPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 304 ypyvkftpereIGNDLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTS 383
Cdd:TIGR03719 318 -----------LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 384 LSYFpkDNSEffEGVDMNLVDWLRQYAPEDEQT----ETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSA 459
Cdd:TIGR03719 387 LAYV--DQSR--DALDPNKTVWEEISGGLDIIKlgkrEIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499595078 460 NVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIA 504
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA 507
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-496 |
9.09e-82 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 267.42 E-value: 9.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEEr 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHERLYEVMKEKDEIYMKpdfsdEDGIRAAELEGEFAEMNGWNAEADAASLLSGLGISADLHDKQMSELENNQ 160
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQLHDANER-----NDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 161 KVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYDFW 240
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 241 YQssQLAQKMAQEQN--KKKEEKIKELQDFIARFSANASKSKQATSRKKQLEKIELddIQPSSRRYPY-VKFTPEREIGN 317
Cdd:PRK10636 235 EV--QRATRLAQQQAmyESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLPN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 318 DLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFFEG 397
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 vDMNLVDWLRQYAPedEQTETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESIT 477
Cdd:PRK10636 391 -DESPLQHLARLAP--QELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490
....*....|....*....
gi 499595078 478 AVNDGLASFKGSIIFTSYD 496
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHD 486
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-504 |
3.72e-75 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 247.72 E-value: 3.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 12 GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGeIDSQ-TGHVSMGKDERLAVLKQDHFAYEEERVLDVVIKGHE 90
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEfEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 91 RLYEVMKEKDEIYMK----PDFSDEDGIRAAELEGEFAEMNGWNAEadaasllSGLGISAD-LH----DKQMSELENNQK 161
Cdd:PRK11819 97 EVKAALDRFNEIYAAyaepDADFDALAAEQGELQEIIDAADAWDLD-------SQLEIAMDaLRcppwDAKVTKLSGGER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYdfwy 241
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 242 qSSQLAQK---MAQEQNkkkeeKIKELQDFIA------RFSANA--SKSK---------QATSRKKQLEKIELdDIQPSS 301
Cdd:PRK11819 246 -SSWLEQKakrLAQEEK-----QEAARQKALKrelewvRQSPKArqAKSKarlaryeelLSEEYQKRNETNEI-FIPPGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 302 RrypyvkftpereIGNDLLTVQGLSKTIdGEKVL-DNISFTMNPNdkAIL--IGDSEIAKTTLLKILAGEMEPDEGTFKW 378
Cdd:PRK11819 319 R------------LGDKVIEAENLSKSF-GDRLLiDDLSFSLPPG--GIVgiIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 379 GVTTSLSYF--------PKDN--SEFFEGVDMNLVDwlrqyapedeQTETFLRGFLGRMLFSGEEVKKKASVLSGGEKVR 448
Cdd:PRK11819 384 GETVKLAYVdqsrdaldPNKTvwEEISGGLDIIKVG----------NREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNR 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 449 CMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIA 504
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIA 509
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-503 |
2.49e-72 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 242.16 E-value: 2.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEER 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHERLYEVMKEKDEI--YMKPDFSDEDGIRAAELEGEFAEMNGWNAEADAASLLSGLGISADlhdKQMSELEN 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDIshLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 239 FWY------------QSSQLAQKMAQEQnkkkeekIKELQDFIARFSAN-----ASKSKQaTSRKKQLE-----KIELDD 296
Cdd:PRK11147 240 QYLlekeealrveelQNAEFDRKLAQEE-------VWIRQGIKARRTRNegrvrALKALR-RERSERREvmgtaKMQVEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 297 iqpSSRRypyvkftpereiGNDLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF 376
Cdd:PRK11147 312 ---ASRS------------GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 377 KWGVTTSLSYFPKDNSEF--FEGVDMNLVDWlRQYAPEDEQTETFLrGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKM 454
Cdd:PRK11147 377 HCGTKLEVAYFDQHRAELdpEKTVMDNLAEG-KQEVMVNGRPRHVL-GYLQDFLFHPKRAMTPVKALSGGERNRLLLARL 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499595078 455 MLSSANVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFI-NTI 503
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTV 504
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-501 |
4.63e-69 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 235.52 E-value: 4.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 8 SLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILS-GEIDS-----QTGHVS---MGKDERL--AVLKQD---- 72
Cdd:PLN03073 184 SISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDGipkncQILHVEqevVGDDTTAlqCVLNTDiert 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAYEEERVLDvviKGHERLYEVMKEKDEIYMKpDFSDEDGI--RAAELEGEFAEMNGWNAEADAASLLSGLGISADLHD 150
Cdd:PLN03073 264 QLLEEEAQLVA---QQRELEFETETGKGKGANK-DGVDKDAVsqRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 151 KQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 231 KLYVGNYDFWYQSSQLAQKMAQEQNKKKEEKIKELQDFIARFSANASKSKQATSRKKQLEKIELDDIQPSSRRYPYVKFT 310
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPDYKFEFPT 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 311 PEREIGNDLLTVQGLSKTIDGEKVL-DNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFpk 389
Cdd:PLN03073 500 PDDRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVF-- 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 390 dNSEFFEGVDMN---LVDWLRQYAPEDEQTetfLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDE 466
Cdd:PLN03073 578 -SQHHVDGLDLSsnpLLYMMRCFPGVPEQK---LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
490 500 510
....*....|....*....|....*....|....*
gi 499595078 467 PTNHLDLESITAVNDGLASFKGSIIFTSYDFEFIN 501
Cdd:PLN03073 654 PSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-514 |
2.05e-53 |
|
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: 177.26 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKdnseffegvd 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 mnlvdwlrqyapedeqtetflrgflgrmlfsgeevkkkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAV 479
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 499595078 480 NDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSG 514
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-240 |
1.51e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 186.42 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHfayeeeR 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ------E 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDvvikGHERLYEVMKekdeiymkpDFSDEDGiraaelegefaemngwnaEADAASLLSGLGISADLHDKQMSELENNQ 160
Cdd:COG0488 389 ELD----PDKTVLDELR---------DGAPGGT------------------EQEVRGYLGRFLFSGDDAFKPVGVLSGGE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 161 KVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYDFW 240
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-229 |
7.63e-46 |
|
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: 157.23 E-value: 7.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQdhfayeeerv 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvvikgherlyevmkekdeiymkpdfsdedgiraaelegefaemngwnaeadaaslLSGlGisadlhdkqmselennQK 161
Cdd:cd03221 71 ---------------------------------------------------------LSG-G----------------EK 76
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGK 229
Cdd:cd03221 77 MRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-238 |
3.20e-37 |
|
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: 137.68 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD---ERLAVLKQDHFAY 76
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDvrkEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEervldvvikghERLYEVMKEKDEIymkpdfsdedgiraaELEGEFAEMNGWNAEADAASLLSGLGISADLhDKQMSEL 156
Cdd:COG4555 81 DE-----------RGLYDRLTVRENI---------------RYFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 157 ENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHIADLDFGKIkLY 233
Cdd:COG4555 134 STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV-VA 212
|
....*
gi 499595078 234 VGNYD 238
Cdd:COG4555 213 QGSLD 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
1.84e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 127.47 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAVL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDlaslsrrelaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQDHFAYEEERVLDVVIKG---HERLYEVMKEKDEiymkpdfsdedgiraaelegefaemngwnAEADAAslLSGLGIsA 146
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrypHLGLFGRPSAEDR-----------------------------EAVEEA--LERTGL-E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 147 DLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIP-AISWLEdfLI-----NFDNTVIVVSHDrhfLN---N 217
Cdd:COG1120 129 HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhQLEVLE--LLrrlarERGRTVVMVLHD---LNlaaR 203
|
250
....*....|...
gi 499595078 218 VCTHIADLDFGKI 230
Cdd:COG1120 204 YADRLVLLKDGRI 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
4.86e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.25 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKD---------ERLAVLKQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDvardpaevrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 DHFAYEEERVLDVVikgherlyevmkekdeiymkpdfsdedgiraaELEGEFAEMNGWNAEADAASLLSGLGIsADLHDK 151
Cdd:COG1131 81 EPALYPDLTVRENL--------------------------------RFFARLYGLPRKEARERIDELLELFGL-TDAADR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIADLDFG 228
Cdd:COG1131 128 KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
..
gi 499595078 229 KI 230
Cdd:COG1131 208 RI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-226 |
5.62e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.56 E-value: 5.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDerlAVLKQDHFAYEEER- 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKP---LEKERKRIGYVPQRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 ---------VLDVVIKG---HERLYEVMKEKDEiymkpdfsdedgiraaelegefaemngwnAEADAAslLSGLGISaDL 148
Cdd:cd03235 78 sidrdfpisVRDVVLMGlygHKGLFRRLSKADK-----------------------------AKVDEA--LERVGLS-EL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 149 HDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAIswlEDFLINFDN------TVIVVSHDRHFLNNVCTHI 222
Cdd:cd03235 126 ADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ---EDIYELLRElrregmTILVVTHDLGLVLEYFDRV 202
|
....
gi 499595078 223 ADLD 226
Cdd:cd03235 203 LLLN 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
7.85e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 7.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDERLAvlkQDHFAY--- 76
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRRA---RRRIGYvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEE-------RVLDVV---IKGHERLYEVMKEKDeiymkpdfsdedgiRAAelegefaemngwnaeADAAslLSGLGIsA 146
Cdd:COG1121 83 RAEvdwdfpiTVRDVVlmgRYGRRGLFRRPSRAD--------------REA---------------VDEA--LERVGL-E 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 147 DLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIA 223
Cdd:COG1121 131 DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVL 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
2.03e-30 |
|
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: 117.58 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFAyeeer 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLW-NGEPIRDAREDYRR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 vlDVVIKGHErlyevmkekDEIymKPDFSdedgirAAELEGEFAEMNGWNA-EADAASLLSGLGIsADLHDKQMSELENN 159
Cdd:COG4133 76 --RLAYLGHA---------DGL--KPELT------VRENLRFWAALYGLRAdREAIDEALEAVGL-AGLADLPVRQLSAG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNV 218
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
6.23e-29 |
|
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: 112.49 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD---------ERLAVLKQ 71
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDikkepeevkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 DHFAYEEERVLDVVikgherlyevmkekdeiymkpDFSdedgiraaelegefaemngwnaeadaasllsgLGisadlhdk 151
Cdd:cd03230 81 EPSLYENLTVRENL---------------------KLS--------------------------------GG-------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 152 qmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHIADLDFG 228
Cdd:cd03230 100 --------MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNG 171
|
..
gi 499595078 229 KI 230
Cdd:cd03230 172 RI 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-237 |
8.23e-27 |
|
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: 114.26 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAyeeerv 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDA------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDvvikGHERLYEVMKEKDEIymkpdfsdedgiraaelegefaeMNGWNAEADAASLLSGLGISADLHDKQMSELENNQK 161
Cdd:TIGR03719 397 LD----PNKTVWEEISGGLDI-----------------------IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGER 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIadLDF---GKIKLYVGNY 237
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFegdSHVEWFEGNF 526
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
319-530 |
6.13e-26 |
|
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: 106.10 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW----------GVTTSLSYFP 388
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkeprEARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 kDNSEFFEGvdMNLVDWLRQYAP----EDEQTETFLRGFLGRMLFSgEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLL 464
Cdd:COG4555 81 -DERGLYDR--LTVRENIRYFAElyglFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 465 DEPTNHLDLESITAVNDGLASFKGS---IIFTSYDFEFINTIANRVIDLNQsGGLSKEVPYEEYLQEIG 530
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEgktVLFSSHIMQEVEALCDRVVILHK-GKVVAQGSLDELREEIG 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-512 |
6.56e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.28 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTS--------LSYFP 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkpLSAMpppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 KDNSEFFEGVDMNLVDW--LRQYAPEDEQtetfLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDE 466
Cdd:COG4619 81 QEPALWGGTVRDNLPFPfqLRERKFDRER----ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499595078 467 PTNHLDLESITAVNDGLASFK----GSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-229 |
1.65e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 102.32 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVsmgkderlavlkqdhfayeeervl 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 83 dvVIKGHERLYEVMKE-KDEIYMKPDfsdedgiraaelegefaemngwnaeadaaslLSGlGisadlhdkqmselennQK 161
Cdd:cd00267 57 --LIDGKDIAKLPLEElRRRIGYVPQ-------------------------------LSG-G----------------QR 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIADLDFGK 229
Cdd:cd00267 87 QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-230 |
2.27e-25 |
|
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: 102.90 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKDerlavLKQdhfayeeerv 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKD-----LAS---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvvikgherlyevMKEKdeiymkpdfsdedgiraaelegEFAEMNGWNAEAdaaslLSGLGIsADLHDKQMSELENNQK 161
Cdd:cd03214 66 --------------LSPK----------------------ELARKIAYVPQA-----LELLGL-AHLADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF----DNTVIVVSHDrhfLNNV---CTHIADLDFGKI 230
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLarerGKTVVMVLHD---LNLAaryADRVILLKDGRI 176
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
2.95e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.40 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG-----------------------EIDSQTGH 57
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvrlfgerrggedvwELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 58 VSMGKDERLavlkqdhfaYEEERVLDVVIKGherLYEVMkekdEIYMKPDfsDEDGIRAAElegefaemngwnaeadaas 137
Cdd:COG1119 83 VSPALQLRF---------PRDETVLDVVLSG---FFDSI----GLYREPT--DEQRERARE------------------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 138 LLSGLGIsADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSH 210
Cdd:COG1119 126 LLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-230 |
2.27e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.66 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAVLK 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPlsampppewrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 71 QDHFAYEEeRVLDvvikgherlyevmkekdeiymkpDFSDEDGIRAAELEGEfaemngwnaeaDAASLLSGLGISADLHD 150
Cdd:COG4619 81 QEPALWGG-TVRD-----------------------NLPFPFQLRERKFDRE-----------RALELLERLGLPPDILD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 151 KQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLD 226
Cdd:COG4619 126 KPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLE 205
|
....
gi 499595078 227 FGKI 230
Cdd:COG4619 206 AGRL 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-529 |
6.68e-24 |
|
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: 105.27 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG------------------------EIDSQTGH 57
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 58 V------SMGKDE----------------RLAVLKQDHFA-YEEERVLDVVIKG-HERLYEvmkEKDEIYMKPDFsdedg 113
Cdd:TIGR03269 81 PcpvcggTLEPEEvdfwnlsdklrrrirkRIAIMLQRTFAlYGDDTVLDNVLEAlEEIGYE---GKEAVGRAVDL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 114 IRAAELEGEFAEMngwnaeadaASLLSGlgisadlhdkqmselenNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAI-- 191
Cdd:TIGR03269 153 IEMVQLSHRITHI---------ARDLSG-----------------GEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTak 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 192 ---SWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLyVGNYDfwyqssqlaqkmaqeqnkkkeekikelqDF 268
Cdd:TIGR03269 206 lvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE-EGTPD----------------------------EV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 269 IARFSANASKSKQATsrkkqlekielddiqpssrrypyvkftpEREIGNDLLTVQGLSK---TIDGE--KVLDNISFTMN 343
Cdd:TIGR03269 257 VAVFMEGVSEVEKEC----------------------------EVEVGEPIIKVRNVSKryiSVDRGvvKAVDNVSLEVK 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 344 PNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF------KWGVTTSLSYFPKDNSEFFEGVDMNLVDWLRQYAPEDEQTE 417
Cdd:TIGR03269 309 EGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 418 TF---LRGFLGRML---------FSGEEVK----KKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVND 481
Cdd:TIGR03269 389 AIgleLPDELARMKavitlkmvgFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTH 468
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 499595078 482 GLASFKGSI----IFTSYDFEFINTIANRViDLNQSGGLSKEVPYEEYLQEI 529
Cdd:TIGR03269 469 SILKAREEMeqtfIIVSHDMDFVLDVCDRA-ALMRDGKIVKIGDPEEIVEEL 519
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-230 |
7.85e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 99.21 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSmgkderlavLKQDHFAYEEE-- 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---------FDGKSYQKNIEal 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGHErLYEVMKEKDEIYMKpdfSDEDGIRaaelegefaemngwNAEADAASLLSGLGISADLHDKQMSeLENN 159
Cdd:cd03268 72 RRIGALIEAPG-FYPNLTARENLRLL---ARLLGIR--------------KKRIDEVLDVVGLKDSAKKKVKGFS-LGMK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 160 QKVKVllAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03268 133 QRLGI--ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-231 |
8.55e-24 |
|
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: 99.25 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGD-RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAvlkqdhfayeEERV 81
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----------KERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvvikghERLYEVMKEKDEIYMKPDFSDEDGIRAAELEgefaemngwNAEADAASLLSGLGISaDLHDKQMSELENNQK 161
Cdd:cd03226 71 --------KSIGYVMQDVDYQLFTDSVREELLLGLKELD---------AGNEQAETVLKDLDLY-ALKERHPLSLSGGQK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLD---IPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIK 231
Cdd:cd03226 133 QRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-229 |
1.49e-23 |
|
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: 98.69 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGD--RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDERLAVLKQ-------- 71
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKElrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 ----DH--FAyeeERVLDVVIKGHERLYEvmkEKDEIYMKpdfsdedgiraaelegefaemngwnaeadAASLLSGLGIS 145
Cdd:cd03225 81 fqnpDDqfFG---PTVEEEVAFGLENLGL---PEEEIEER-----------------------------VEEALELVGLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 146 aDLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHI 222
Cdd:cd03225 126 -GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRV 204
|
....*..
gi 499595078 223 ADLDFGK 229
Cdd:cd03225 205 IVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-512 |
1.53e-23 |
|
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: 97.47 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWgvttslsyfpkdnseffEGVD 399
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------LGKD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 M--NLVDWLRQ--YAPEDeqtetflRGFLGRMlfSGEEVKKkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLES 475
Cdd:cd03230 64 IkkEPEEVKRRigYLPEE-------PSLYENL--TVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499595078 476 ITAVND---GLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03230 131 RREFWEllrELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-237 |
3.37e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 103.27 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEER- 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKt 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHerlyevmkekDEIYMkpdfsdedgiraaeleGEFaEMNgwnaeadAASLLSGLGISADLHDKQMSELENNQ 160
Cdd:PRK11819 405 VWEEISGGL----------DIIKV----------------GNR-EIP-------SRAYVGRFNFKGGDQQKKVGVLSGGE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 161 KVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIadLDF---GKIKLYVGNY 237
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFegdSQVEWFEGNF 528
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-188 |
4.57e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAVL 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLnGRPlaawspwelaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQD---HFAYeeeRVLDVVIKGHERLYEVMKEKDEIymkpdfsdedgIRAAelegefaeMngwnAEADAASL-------L 139
Cdd:COG4559 81 PQHsslAFPF---TVEEVVALGRAPHGSSAAQDRQI-----------VREA--------L----ALVGLAHLagrsyqtL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499595078 140 SGlGisadlhdKQmselennQKV---KVL--LAQSLFGEPDVLLLDEPTNGLDI 188
Cdd:COG4559 135 SG-G-------EQ-------QRVqlaRVLaqLWEPVDGGPRWLFLDEPTSALDL 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-233 |
8.69e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.64 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFAY-EEE 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRRRIGYlPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RvldvvikgheRLYEVMKEKDEI-YMkpdfsdedgiraAELEGefaeMNGWNAEADAASLLSGLGIsADLHDKQMSELE- 157
Cdd:COG4152 80 R----------GLYPKMKVGEQLvYL------------ARLKG----LSKAEAKRRADEWLERLGL-GDRANKKVEELSk 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 158 -NNQKVKvlLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF-DN--TVIVVSHDrhfLNNV---CTHIADLDFGKI 230
Cdd:COG4152 133 gNQQKVQ--LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaAKgtTVIFSSHQ---MELVeelCDRIVIINKGRK 207
|
...
gi 499595078 231 KLY 233
Cdd:COG4152 208 VLS 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-512 |
1.66e-22 |
|
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: 95.62 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG----------VTTSLSYFP 388
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepirdaredYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 kDNSEFFEgvDMNLVDWLRQYA------PEDEQTETFLRGF-LGRMLfsgeevKKKASVLSGGEKVRCMLSKMMLSSANV 461
Cdd:COG4133 82 -HADGLKP--ELTVRENLRFWAalyglrADREAIDEALEAVgLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499595078 462 LLLDEPTNHLDLESITAVNDGLASFK---GSIIFTSYDFEFINtiANRVIDLNQ 512
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
3.31e-22 |
|
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: 92.71 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 335 LDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG-----------VTTSLSYFPKDNSEF-----FEGV 398
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFprltvRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595078 399 DMNLVDWLRQYAPEDEQTETFLRGfLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
5.53e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 94.18 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGnCYGLIGANGAGKSTFLKILSGEIDSQTGHVsmgkderlavlkqdhfayeeeRV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI---------------------RI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVvikgherlyEVMKEKDEI-----YMKPDFSDEDGIRAAELEGEFAEMNGWN---AEADAASLLSGLGIsADLHDKQM 153
Cdd:cd03264 59 DGQ---------DVLKQPQKLrrrigYLPQEFGVYPNFTVREFLDYIAWLKGIPskeVKARVDEVLELVNL-GDRAKKKI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISwledflINFDN---------TVIVVSHDRHFLNNVCTHIAD 224
Cdd:cd03264 129 GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD-PEER------IRFRNllselgedrIVILSTHIVEDVESLCNQVAV 201
|
....*..
gi 499595078 225 LDFGKIK 231
Cdd:cd03264 202 LNKGKLV 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-528 |
1.27e-21 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 98.48 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 335 LDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTSLSYFPKDNSE------FFEGVDmNLVDW 405
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlIVARLQQDPPRNVEgtvydfVAEGIE-EQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 406 LRQY---------APEDE------------------QTETFLRGFLGRMLFSGEevkKKASVLSGGEKVRCMLSKMMLSS 458
Cdd:PRK11147 98 LKRYhdishlvetDPSEKnlnelaklqeqldhhnlwQLENRINEVLAQLGLDPD---AALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 459 ANVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSGGLSKEVPYEEYLQE 528
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLE 244
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
3.89e-21 |
|
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: 87.63 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 223 ADLDFGKIKLYVGNYDFWYQSSQLAQKMAQEQNKKKEEKIKELQDFIARFSANASKSKQATSRKKQLEKIEldDIQPSSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKME--RIEKPER 78
|
....*..
gi 499595078 303 RYPYVKF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
5.60e-21 |
|
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: 92.41 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFA----- 75
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF-DGRDITGLPPHRIArlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 --------YEEERVLD-VVIKGHERLYEvmkekdeiYMKPDFSDEDGIRAAELEgefaemngwnAEADAASLLSGLGIsA 146
Cdd:COG0411 83 rtfqnprlFPELTVLEnVLVAAHARLGR--------GLLAALLRLPRARREERE----------ARERAEELLERVGL-A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 147 DLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLI----NFDNTVIVVSHDRHFLNNVCTHI 222
Cdd:COG0411 144 DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRrlrdERGITILLIEHDMDLVMGLADRI 223
|
....*...
gi 499595078 223 ADLDFGKI 230
Cdd:COG0411 224 VVLDFGRV 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-233 |
5.88e-21 |
|
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: 91.19 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFAY-EEER 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIGYlPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 vldvvikgheRLYEVMKEKDE-IYMkpdfsdedgiraAELEGefaeMNGWNAEADAASLLSGLGISaDLHDKQMSELENN 159
Cdd:cd03269 80 ----------GLYPKMKVIDQlVYL------------AQLKG----LKKEEARRRIDEWLERLELS-EYANKRVEELSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIADLDFGKIKLY 233
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-230 |
7.71e-21 |
|
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: 91.24 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRF-GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKDERLAVLKQ-------- 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRElrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 ----DH--FAyeeERVLDVVIKGHERLyevmkekdeiymkpdfsdedGIRAAELEgefaemngwnAEADAAslLSGLGIS 145
Cdd:COG1122 81 fqnpDDqlFA---PTVEEDVAFGPENL--------------------GLPREEIR----------ERVEEA--LELVGLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 146 aDLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHI 222
Cdd:COG1122 126 -HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRV 204
|
....*...
gi 499595078 223 ADLDFGKI 230
Cdd:COG1122 205 IVLDDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-508 |
1.09e-20 |
|
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: 95.36 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF--GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQ---TGHVS-MGKD----------E 64
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLlDGRDllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 65 RLAVLKQDHfayeeERVLDVVIKGherlyevmkekDEIymkpdfsdEDGIRAAELEGEfaemngwNAEADAASLLSGLGI 144
Cdd:COG1123 84 RIGMVFQDP-----MTQLNPVTVG-----------DQI--------AEALENLGLSRA-------EARARVLELLEAVGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 145 sADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSHDRHFLNNVCT 220
Cdd:COG1123 133 -ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIAD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 221 HIADLDFGKIklyvgnydfwyqssqlaqkmaQEQNkkkeekikelqdfiarfsanasKSKQATSRKKQLEKIELDDIQPS 300
Cdd:COG1123 212 RVVVMDDGRI---------------------VEDG----------------------PPEEILAAPQALAAVPRLGAARG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 301 SRRypyvkftPEREIGNDLLTVQGLSKT-----IDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT 375
Cdd:COG1123 249 RAA-------PAAAAAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 376 FkwgvttslsyfpkdnseFFEGVDMNLVDW--LRQYAP-------------------EDEQTETfLRgFLGRMlfSGEEV 434
Cdd:COG1123 322 I-----------------LFDGKDLTKLSRrsLRELRRrvqmvfqdpysslnprmtvGDIIAEP-LR-LHGLL--SRAER 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 435 KKKA-----SV-------------LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD-------LESITAVNDglaSFKGS 489
Cdd:COG1123 381 RERVaelleRVglppdladrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQR---ELGLT 457
|
570
....*....|....*....
gi 499595078 490 IIFTSYDFEFINTIANRVI 508
Cdd:COG1123 458 YLFISHDLAVVRYIADRVA 476
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-512 |
1.51e-20 |
|
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: 88.46 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 321 TVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDnseffegvdm 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 401 nlvdWLRQYApedeqtetflrgflgrMLFSgeevkkkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVN 480
Cdd:cd00267 71 ----LRRRIG----------------YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 499595078 481 DGLASFKG---SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-235 |
1.51e-20 |
|
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: 90.12 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKL----FEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgkdERLAVLKQdhfAY 76
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV---DGFDVVKE---PA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEERVLDVViKGHERLYEVMKEKDEIymkpdfsdedgiraaELEGEFAEMNGWNAEADAASLLSGLGIsADLHDKQMSEL 156
Cdd:cd03266 75 EARRRLGFV-SDSTGLYDRLTARENL---------------EYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 157 ENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIADLDFGKIkLY 233
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVVVLHRGRV-VY 216
|
..
gi 499595078 234 VG 235
Cdd:cd03266 217 EG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-188 |
1.52e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAVL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLnGRPladwspaelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQDH---FAYeeeRVLDVVIKGHERLYEVMKEKDEIymkpdfsdedgiraaelegefaemngwnaeADAASLLSGLgisA 146
Cdd:PRK13548 82 PQHSslsFPF---TVEEVVAMGRAPHGLSRAEDDAL------------------------------VAAALAQVDL---A 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499595078 147 DLHDKQMSELENNQKVKVLLAQSL------FGEPDVLLLDEPTNGLDI 188
Cdd:PRK13548 126 HLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-213 |
3.48e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 10 RFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQdhfayeeervldvvikgH 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-----------------R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 90 ERLYEVMkekdeiymkPdfsdedgIRAAELE--GEFAEMNGW-----NAEADAASLLSGLGIsADLHDKQMSELENNQKV 162
Cdd:NF040873 64 SEVPDSL---------P-------LTVRDLVamGRWARRGLWrrltrDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 163 KVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDfLINF----DNTVIVVSHDRH 213
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIA-LLAEeharGATVVVVTHDLE 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
330-511 |
4.09e-20 |
|
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: 88.47 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG-------VTTSLSYFPKDNSE---FFEGVD 399
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakERRKSIGYVMQDVDyqlFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 MNLVDWLRQYAPEDEQTETFLRgflgRMLFSGEEVKKKASvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD---LESI 476
Cdd:cd03226 91 EELLLGLKELDAGNEQAETVLK----DLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERV 165
|
170 180 190
....*....|....*....|....*....|....*
gi 499595078 477 TAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLN 511
Cdd:cd03226 166 GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
5.64e-20 |
|
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: 89.03 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF-DGEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 -------YEEERVLDVVIKGHERlyevmkekdeiymkpdfSDEDGIRAAELEGEFAEmngwnAEADAASLLSGLGIsADL 148
Cdd:cd03219 80 tfqiprlFPELTVLENVMVAAQA-----------------RTGSGLLLARARREERE-----ARERAEELLERVGL-ADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 149 HDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGL---DIPAIS-WLEDfLINFDNTVIVVSHDRHFLNNVCTHIAD 224
Cdd:cd03219 137 ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLnpeETEELAeLIRE-LRERGITVLLVEHDMDVVMSLADRVTV 215
|
....*.
gi 499595078 225 LDFGKI 230
Cdd:cd03219 216 LDQGRV 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-293 |
6.04e-20 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 93.31 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYeeer 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEF---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 vldvvikgherlyevmkekdeiyMKPDFSD-EDGIRAAELEgefaemngwnAEADAASLLSGLGISADLHDKQMSELENN 159
Cdd:PRK10636 388 -----------------------LRADESPlQHLARLAPQE----------LEQKLRDYLGGFGFQGDKVTEETRRFSGG 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYDF 239
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLED 514
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 240 WYQ-SSQLAQKMAQEQNKKKEEKIKELQDFIARFSANASKSKQATSRKKQLEKIE 293
Cdd:PRK10636 515 YQQwLSDVQKQENQTDEAPKENNANSAQARKDQKRREAELRTQTQPLRKEIARLE 569
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
1.41e-19 |
|
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: 85.39 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 17 FEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKDE----------RLAVLKQDHFAYEEERVLDVV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILlDGQDLtdderkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 86 IKGhERLYEVMKEKDeiymkpdfsdedgiraaelegefaemngwnaEADAASLLSGLGISADLHDK---QMSELENNQKV 162
Cdd:pfam00005 81 RLG-LLLKGLSKREK-------------------------------DARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQ 128
|
170 180
....*....|....*....|..
gi 499595078 163 KVLLAQSLFGEPDVLLLDEPTN 184
Cdd:pfam00005 129 RVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-523 |
2.35e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 317 NDLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT--FKWGVTTSL---------S 385
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTllFEGEDISTLkpeiyrqqvS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 386 YFPKDNSEFFEGVDMNLV-DW-LRQYAPEdeqtETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLL 463
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfPWqIRNQQPD----PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 464 LDEPTNHLDLESITAVND---GLASFKG-SIIFTSYDFEFINTiANRVIDLNQSGGLSKEVPYE 523
Cdd:PRK10247 161 LDEITSALDESNKHNVNEiihRYVREQNiAVLWVTHDKDEINH-ADKVITLQPHAGEMQEARYE 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
4.58e-19 |
|
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: 86.08 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQ-----TGHVS-MGKDerlaVLKQDHFA 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLlDGKD----IYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YEEERVLDVVikgherlyevmkekdeiYMKP---DFSDEDGIRAA-ELEGEfaemnGWNAEADA--ASLLSGLGISADLH 149
Cdd:cd03260 77 LELRRRVGMV-----------------FQKPnpfPGSIYDNVAYGlRLHGI-----KLKEELDErvEEALRKAALWDEVK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 150 DKQM-SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN--TVIVVSHD 211
Cdd:cd03260 135 DRLHaLGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
9.23e-19 |
|
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: 85.63 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHV--------SMGKDE------RLA 67
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisGLSEAElyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 68 VLKQD-------------------HFAYEEERVLDVVIkghERLYEVmkekdeiymkpdfsdedGIRAAElegefaemng 128
Cdd:cd03261 81 MLFQSgalfdsltvfenvafplreHTRLSEEEIREIVL---EKLEAV-----------------GLRGAE---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 129 wnaeadaasllsglgisadlhDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISWLEDFLIN-----FDN 203
Cdd:cd03261 131 ---------------------DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD-PIASGVIDDLIRslkkeLGL 188
|
250 260
....*....|....*....|....*..
gi 499595078 204 TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03261 189 TSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-508 |
9.70e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.48 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 26 EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSmGKDERLAVLK-------QDHFA--YEEErvLDVVIKGH--ERLYE 94
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE-EEPSWDEVLKrfrgtelQNYFKklYNGE--IKVVHKPQyvDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 95 VMKEK-DEIYMKpdfSDEDGIrAAELEGEFAEMNGWNAEADAaslLSGlgisadlhdkqmSELEnnqkvKVLLAQSLFGE 173
Cdd:PRK13409 175 VFKGKvRELLKK---VDERGK-LDEVVERLGLENILDRDISE---LSG------------GELQ-----RVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 174 PDVLLLDEPTNGLDI-------PAISWLEDflinfDNTVIVVSHDRHFLN----NVctHIAdldFGKIKLY--------- 233
Cdd:PRK13409 231 ADFYFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDyladNV--HIA---YGEPGAYgvvskpkgv 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 234 -VG-NYdfwYQSSQLAqkmaqEQNKkkeekikelqdfiaRFsanaskskqatsRKKQLEkIELDDIQPSSRRYPYVKFTP 311
Cdd:PRK13409 301 rVGiNE---YLKGYLP-----EENM--------------RI------------RPEPIE-FEERPPRDESERETLVEYPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 312 -EREIGNDLLTVQGlsKTIDGEKVLdnisftmnpndkAILiGDSEIAKTTLLKILAGEMEPDEGTFKWGVTtsLSYFP-- 388
Cdd:PRK13409 346 lTKKLGDFSLEVEG--GEIYEGEVI------------GIV-GPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKPqy 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 -KDNSeffegvDMNLVDWLRQYAPEDE----QTEtFLRGF-LGRMLfsgeevKKKASVLSGGEKVRCMLSKMMLSSANVL 462
Cdd:PRK13409 409 iKPDY------DGTVEDLLRSITDDLGssyyKSE-IIKPLqLERLL------DKNVKDLSGGELQRVAIAACLSRDADLY 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499595078 463 LLDEPTNHLDLESITAVNDGLASF----KGSIIFTSYDFEFINTIANRVI 508
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-235 |
1.49e-18 |
|
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: 85.08 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 19 DVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGK----DERLAVLKQdhfayeeervLDVVIKGHERLYE 94
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRR----------IGVVFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 95 VMKEKDEIYMKPDFSDEDGIRAAELEGEFAEMngwnaeadaasllsgLGIsADLHDKQMSELENNQKVKVLLAQSLFGEP 174
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSEL---------------LDL-EELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 175 DVLLLDEPTNGLDIPAISWLEDFLINF----DNTVIVVSHDRHFLNNVCTHIADLDFGKIkLYVG 235
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
320-530 |
2.41e-18 |
|
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: 88.28 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEK-VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvTTSLSYFPKD-------- 390
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPAswrrqiaw 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 ---NSEFFEGvdmNLVDWLRQYAPE--DEQTETFLR-----GFLgRMLFSG--EEVKKKASVLSGGEKVRCMLSKMMLSS 458
Cdd:COG4988 416 vpqNPYLFAG---TIRENLRLGRPDasDEELEAALEaagldEFV-AALPDGldTPLGEGGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 459 ANVLLLDEPTNHLDLESITAVNDGLASFKGS--IIFTSYDFEFINtIANRVIDLNQsGGLSKEVPYEEYLQEIG 530
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLA-QADRILVLDD-GRIVEQGTHEELLAKNG 563
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
3.25e-18 |
|
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: 87.89 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRK-LFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQD----HFAY 76
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPAswrrQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEER-------VLDVVikgheRLYevmkekdeiymKPDFSDEDGIRAAELEG--EFAEM--NGWNAE-ADAASLLSGlGi 144
Cdd:COG4988 416 VPQNpylfagtIRENL-----RLG-----------RPDASDEELEAALEAAGldEFVAAlpDGLDTPlGEGGRGLSG-G- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 145 sadlhdkqmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF--DNTVIVVSHDRHFLNNvCTHI 222
Cdd:COG4988 478 ---------------QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQ-ADRI 541
|
....*...
gi 499595078 223 ADLDFGKI 230
Cdd:COG4988 542 LVLDDGRI 549
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-529 |
4.18e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.60 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTT------SLSYFP---K 389
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrRIGYVPqraE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 390 DNSEF----FEGVDMNLVD---WLRQYAPED--------EQTEtfLRGFLGRMLfsGEevkkkasvLSGGEKVRCMLSKM 454
Cdd:COG1121 86 VDWDFpitvRDVVLMGRYGrrgLFRRPSRADreavdealERVG--LEDLADRPI--GE--------LSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 455 MLSSANVLLLDEPTNHLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVIDLNQSG---GLSKEVPYEEYLQE 528
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLvahGPPEEVLTPENLSR 233
|
.
gi 499595078 529 I 529
Cdd:COG1121 234 A 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-230 |
4.98e-18 |
|
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: 87.58 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRK--LFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG----KDERLAVLKQdHFA 75
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDgidlRQIDPASLRR-QIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YeeervldvvikgherlyeVMKE--------KDEIYM-KPDFSDEDGIRAAELEG--EF-AEM-NGWNAE-ADAASLLSG 141
Cdd:COG2274 553 V------------------VLQDvflfsgtiRENITLgDPDATDEEIIEAARLAGlhDFiEALpMGYDTVvGEGGSNLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 142 lGisadlhdkqmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDipAISwlEDFLINF------DNTVIVVSHDRHFL 215
Cdd:COG2274 615 -G----------------QRQRLAIARALLRNPRILILDEATSALD--AET--EAIILENlrrllkGRTVIIIAHRLSTI 673
|
250
....*....|....*
gi 499595078 216 NNvCTHIADLDFGKI 230
Cdd:COG2274 674 RL-ADRIIVLDKGRI 687
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-230 |
5.93e-18 |
|
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: 84.36 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 10 RFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEI--DSQTGHVSmgkderlavlkqdhfayeeervldvvik 87
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLrpTSGTARVA---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 88 GherlYEVMKEKDE----IYMKPDFS--DED--GIRAAELEGEFAEMNGWNAEADAASLLS--GLGISADLHDKQMSele 157
Cdd:TIGR01188 54 G----YDVVREPRKvrrsIGIVPQYAsvDEDltGRENLEMMGRLYGLPKDEAEERAEELLElfELGEAADRPVGTYS--- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 158 NNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiP---AISW-LEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:TIGR01188 127 GGMRRRLDIAASLIHQPDVLFLDEPTTGLD-PrtrRAIWdYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
8.34e-18 |
|
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: 82.15 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRF--GDRKLF--EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG-------KDERLAVLK 70
Cdd:cd03255 1 IELKNLSKTYggGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 71 QDHFAYeeervldvVIKGHERLyevmkekdeiymkPDFSDEDGIraaELEGEFAEMNGWNAEADAASLLSGLGIsADLHD 150
Cdd:cd03255 81 RRHIGF--------VFQSFNLL-------------PDLTALENV---ELPLLLAGVPKKERRERAEELLERVGL-GDRLN 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 151 KQMSELENNQKVKVLLAQSLFGEPDVLLLDEPT------NGLDIPAIswLEDFLINFDNTVIVVSHDR 212
Cdd:cd03255 136 HYPSELSGGQQQRVAIARALANDPKIILADEPTgnldseTGKEVMEL--LRELNKEAGTTIVVVTHDP 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-229 |
9.31e-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: 81.08 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQDHfaYEEERV 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDEL--PPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVVIKgherlyevmkekdeiymkpdfsdedgiraaelegEFAEMNGWNAEADAASLLSGlgisadlhdkqmselenNQK 161
Cdd:cd03229 78 IGMVFQ----------------------------------DFALFPHLTVLENIALGLSG-----------------GQQ 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLI----NFDNTVIVVSHDRHFLNNVCTHIADLDFGK 229
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-211 |
1.88e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 80.54 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 12 GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDErlavlkqdhFAYEEERVLDVvikgHER 91
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP---------LDYSRKGLLER----RQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 92 LYEVMKEKDEIYMKPDFSDEDGIRAAELEGEFAEMNGWNAEAdaaslLSGLGISaDLHDKQMSELENNQKVKVLLAQSLF 171
Cdd:TIGR01166 70 VGLVFQDPDDQLFAADVDQDVAFGPLNLGLSEAEVERRVREA-----LTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499595078 172 GEPDVLLLDEPTNGLDIPAISWLEDFLINFD---NTVIVVSHD 211
Cdd:TIGR01166 144 MRPDVLLLDEPTAGLDPAGREQMLAILRRLRaegMTVVISTHD 186
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-231 |
2.05e-17 |
|
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: 81.01 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLF--EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGhvsmgkderlavlkqdhfayeee 79
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 rvlDVVIKGHerlyEVMKEKDEIYMK-----------PDFSDEDGIR-AAELEGEfaemNGWNAEADAASLLSGLGISaD 147
Cdd:cd03263 58 ---TAYINGY----SIRTDRKAARQSlgycpqfdalfDELTVREHLRfYARLKGL----PKSEIKEEVELLLRVLGLT-D 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 148 LHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDipaiSWLEDFLINF------DNTVIVVSHDRHFLNNVCTH 221
Cdd:cd03263 126 KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD----PASRRAIWDLilevrkGRSIILTTHSMDEAEALCDR 201
|
250
....*....|
gi 499595078 222 IADLDFGKIK 231
Cdd:cd03263 202 IAIMSDGKLR 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-512 |
2.32e-17 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 85.22 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 334 VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFFEGVDMNLVDWLRQYAPED 413
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 414 EQTE-------------------------------TFLRGfLGrmlFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVL 462
Cdd:PRK10636 96 AQLHdanerndghaiatihgkldaidawtirsraaSLLHG-LG---FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499595078 463 LLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-237 |
2.94e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 85.00 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEER-V 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKtV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVVIKGherlyevmkeKDEIymkpdfsdedgiraaelegefaEMNGWNAEAdaasllsgLGISADL--HDKQ----MSE 155
Cdd:PRK11147 401 MDNLAEG----------KQEV----------------------MVNGRPRHV--------LGYLQDFlfHPKRamtpVKA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 156 LENNQKVKVLLAQsLFGEPDVLL-LDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTH--IADLDfGKIKL 232
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFEGN-GKIGR 518
|
....*
gi 499595078 233 YVGNY 237
Cdd:PRK11147 519 YVGGY 523
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-512 |
3.28e-17 |
|
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: 79.18 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEK--VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvttslsyfpkdnseffeG 397
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-----------------G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 VDMNLVDW--LRQ---YAPEDEQtetflrgflgrmLFSGeevkkkaSV----LSGGEKVRCMLSKMMLSSANVLLLDEPT 468
Cdd:cd03246 64 ADISQWDPneLGDhvgYLPQDDE------------LFSG-------SIaeniLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499595078 469 NHLDLESITAVNDGLASFK---GSIIFTSYDFEFInTIANRVIDLNQ 512
Cdd:cd03246 125 SHLDVEGERALNQAIAALKaagATRIVIAHRPETL-ASADRILVLED 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-512 |
4.31e-17 |
|
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: 79.15 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFFEGVD 399
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-----------------LIDGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 mnlVDWLRQYAPEDEQTETFLrgFLGRMLFSGEEVKKK-ASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITA 478
Cdd:cd03229 64 ---LTDLEDELPPLRRRIGMV--FQDFALFPHLTVLENiALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 499595078 479 VNDGL----ASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03229 139 VRALLkslqAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-508 |
7.57e-17 |
|
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: 83.68 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 26 EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM--GKDErlaVLK-------QDHFA--YEEErvLDVVIKGH--ERL 92
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepSWDE---VLKrfrgtelQDYFKklANGE--IKVAHKPQyvDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 93 YEVMKEK-DEIYMKpdfSDEDGIrAAELEGEFAEMNGWNAEADAaslLSGlgisadlhdkqmSELEnnqkvKVLLAQSLF 171
Cdd:COG1245 173 PKVFKGTvRELLEK---VDERGK-LDELAEKLGLENILDRDISE---LSG------------GELQ-----RVAIAAALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 172 GEPDVLLLDEPTNGLDIP---AISWLEDFLINFDNTVIVVSHDrhflnnvcthIADLD---------------FGKI-KL 232
Cdd:COG1245 229 RDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHD----------LAILDyladyvhilygepgvYGVVsKP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 233 Y---VG-NYdfwYQSSQLaqkmaQEQNKkkeekikelqdfiaRFsanaskskqatsRKKQLEkIELDDIQPSSRRYPYVK 308
Cdd:COG1245 299 KsvrVGiNQ---YLDGYL-----PEENV--------------RI------------RDEPIE-FEVHAPRREKEEETLVE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 309 FTP-EREIGNDLLTVQGlsKTIDGEKVLdnisftmnpndkAILiGDSEIAKTTLLKILAGEMEPDEGTFKWGVTtsLSYF 387
Cdd:COG1245 344 YPDlTKSYGGFSLEVEG--GEIREGEVL------------GIV-GPNGIGKTTFAKILAGVLKPDEGEVDEDLK--ISYK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PkdnseffegvdmnlvdwlrQY--APEDEQTETFLRGFLGRMLFSG---EEV----------KKKASVLSGGEKVRCMLS 452
Cdd:COG1245 407 P-------------------QYisPDYDGTVEEFLRSANTDDFGSSyykTEIikplglekllDKNVKDLSGGELQRVAIA 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 453 KMMLSSANVLLLDEPTNHLDLESITAVNDGLASF----KGSIIFTSYDFEFINTIANRVI 508
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
8.93e-17 |
|
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: 79.64 E-value: 8.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHV--------SMGKDERLAVLKQ- 71
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditGLSEKELYELRRRi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 ----------DH--------FAYEEervldvvikgHERLYEvmKEKDEI-YMKpdfsdedgIRAAELEGefaemngwnae 132
Cdd:COG1127 85 gmlfqggalfDSltvfenvaFPLRE----------HTDLSE--AEIRELvLEK--------LELVGLPG----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 133 adAASL----LSGlGisadlhdkqMselennQKvKVLLAQSLFGEPDVLLLDEPTNGLDiPAISWLEDFLIN-----FDN 203
Cdd:COG1127 134 --AADKmpseLSG-G---------M------RK-RVALARALALDPEILLYDEPTAGLD-PITSAVIDELIRelrdeLGL 193
|
250 260
....*....|....*....|....*..
gi 499595078 204 TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:COG1127 194 TSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-508 |
9.13e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 79.72 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKwgvttslsyfpkdnsefFEGVD 399
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR-----------------VLGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 M--NLVDWLRQ--YAPEDEQTETFLRG-----FLGRM-----------------LFSGEEV-KKKASVLSGGEKVRCMLS 452
Cdd:COG1131 64 VarDPAEVRRRigYVPQEPALYPDLTVrenlrFFARLyglprkeareridelleLFGLTDAaDRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 453 KMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVI 508
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVA 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
1.38e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKD-----------ERLAVL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQDHFAYEEERVLDVVIKG---HERLYEVMkekdeiymkpdfsDEDGIRAAElegefAEMNGWNAEADAasllsglgisa 146
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrtpHRSRFDTW-------------TETDRAAVE-----RAMERTGVAQFA----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 147 dlhDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIP-AISWLEDF--LINFDNTVIVVSHDRHFLNNVCTHIA 223
Cdd:PRK09536 134 ---DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELV 210
|
....*..
gi 499595078 224 DLDFGKI 230
Cdd:PRK09536 211 LLADGRV 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
321-523 |
2.09e-16 |
|
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: 81.91 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 321 TVQGLSKTIDGEK-VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKD-----NSEF 394
Cdd:TIGR03719 6 TMNRVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpqldpTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 395 FEGVDMNLVDWLR----------QYAPEDEQTETFLR--GFL--------GRMLFSGEEVKKKA----------SVLSGG 444
Cdd:TIGR03719 86 RENVEEGVAEIKDaldrfneisaKYAEPDADFDKLAAeqAELqeiidaadAWDLDSQLEIAMDAlrcppwdadvTKLSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 445 EKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSGGlskeVPYE 523
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRG----IPWE 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
330-512 |
2.41e-16 |
|
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: 76.65 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvttslsyfpkdnseffeGVDMNLVD--WLR 407
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-----------------GVDLRDLDleSLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 408 Q---YAPEDEQtetflrgflgrmLFSGeevkkkaSV----LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVN 480
Cdd:cd03228 76 KniaYVPQDPF------------LFSG-------TIreniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....
gi 499595078 481 DGLASFKG--SIIFTSYDFEFINtIANRVIDLNQ 512
Cdd:cd03228 137 EALRALAKgkTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
3.33e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFG--DRKLFEDV-NIKFT--EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM------------GKD 63
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKAVdNVSLEvkEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 64 ER------LAVLKQDHFAYEEERVLDvvikgherlyevmkekdeiymkpDFSDEDGIraaELEGEFAEMNgwnaeadAAS 137
Cdd:TIGR03269 359 GRgrakryIGILHQEYDLYPHRTVLD-----------------------NLTEAIGL---ELPDELARMK-------AVI 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 138 LLSGLGISAD----LHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD-IPAISWLEDFL---INFDNTVIVVS 209
Cdd:TIGR03269 406 TLKMVGFDEEkaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILkarEEMEQTFIIVS 485
|
250 260
....*....|....*....|.
gi 499595078 210 HDRHFLNNVCTHIADLDFGKI 230
Cdd:TIGR03269 486 HDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-512 |
6.62e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 77.22 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTI-DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFFEGV 398
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 DM-----NLVDwlRQYApedeqTETFLRGFLGRM--------LFSGEEVK----------------KKASVLSGGEKVRC 449
Cdd:cd03256 81 GMifqqfNLIE--RLSV-----LENVLSGRLGRRstwrslfgLFPKEEKQralaalervglldkayQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 450 MLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASF---KG-SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGiTVIVSLHQVDLAREYADRIVGLKD 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-231 |
9.20e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.32 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILS-------GEI--DSQTGHVSMGKDERLAVLKQD 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpseGSIvvNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAYEEERvLDVVIKgHERLYEVMKEKDEIYMKPdfSDEDGIRAAElegefaemngwnAEADAASLLSGLGISADLHDKQ 152
Cdd:PRK10619 86 QLRLLRTR-LTMVFQ-HFNLWSHMTVLENVMEAP--IQVLGLSKQE------------ARERAVKYLAKVGIDERAQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 153 MSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD---IPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGK 229
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
..
gi 499595078 230 IK 231
Cdd:PRK10619 230 IE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-230 |
1.09e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 76.25 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGhvsmgkderlavlkqdhfayeeerv 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 lDVVIKGHErlyeVMKEKDEI-----YMKPDFSDEDGIRAAELEGEFAEMNGW-NAEAD--AASLLSGLGIsADLHDKQM 153
Cdd:cd03265 56 -RATVAGHD----VVREPREVrrrigIVFQDLSVDDELTGWENLYIHARLYGVpGAERRerIDELLDFVGL-LEAADRLV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAIS--W--LEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGK 229
Cdd:cd03265 130 KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
.
gi 499595078 230 I 230
Cdd:cd03265 210 I 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-484 |
1.54e-15 |
|
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: 79.33 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDG-EKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTfkwgVTTS--------------- 383
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE----VTLDgvpvssldqdevrrr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 384 LSYFPKDNSEFfegvDMNLVDWLRQYAPE--DEQTETFLRGF-LGRMLFSGEE-----VKKKASVLSGGEKVRCMLSKMM 455
Cdd:TIGR02868 411 VSVCAQDAHLF----DTTVRENLRLARPDatDEELWAALERVgLADWLRALPDgldtvLGEGGARLSGGERQRLALARAL 486
|
170 180 190
....*....|....*....|....*....|....*.
gi 499595078 456 LSSANVLLLDEPTNHLD-------LESITAVNDGLA 484
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDaetadelLEDLLAALSGRT 522
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
2.58e-15 |
|
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: 75.16 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF-----GDRKL--FEDVNIKFTEGNCYGLIGANGAGKSTFLKIL-------SGEI--DSQTGHVSMGK-D 63
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSIlvRHDGGWVDLAQaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 64 ER--LAVLKQD-----HFAYEEERV--LDVVIkghERLYevmkekdeiymkpdfsdEDGIRAAElegefaemngwnAEAD 134
Cdd:COG4778 84 PReiLALRRRTigyvsQFLRVIPRVsaLDVVA---EPLL-----------------ERGVDREE------------ARAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 135 AASLLSGLGISADLHD----------KQmselennqkvKVLLAQSLFGEPDVLLLDEPTNGLDiPA-----ISWLEDFLI 199
Cdd:COG4778 132 ARELLARLNLPERLWDlppatfsggeQQ----------RVNIARGFIADPPLLLLDEPTASLD-AAnravvVELIEEAKA 200
|
250 260
....*....|....*....|....*..
gi 499595078 200 NfDNTVIVVSHDRHFLNNVCTHIADLD 226
Cdd:COG4778 201 R-GTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-230 |
2.97e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.09 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF-GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQDHFAY--- 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 ------EEERVLDvvikgHERLYE-VM-------KEKDEIymkpdfsdedgiraaelegefaemngwnaEADAASLLSGL 142
Cdd:COG2884 80 rigvvfQDFRLLP-----DRTVYEnVAlplrvtgKSRKEI-----------------------------RRRVREVLDLV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 143 GISaDLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISW-----LEDFlinfdN----TVIVVSHDRH 213
Cdd:COG2884 126 GLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD-PETSWeimelLEEI-----NrrgtTVLIATHDLE 198
|
250
....*....|....*..
gi 499595078 214 FLNNVCTHIADLDFGKI 230
Cdd:COG2884 199 LVDRMPKRVLELEDGRL 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
311-531 |
3.13e-15 |
|
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: 78.72 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 311 PEREIGNDLLTVQGLSKTI-----------DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTfkwg 379
Cdd:COG2274 456 PEREEGRSKLSLPRLKGDIelenvsfrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR---- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 380 VttslsyfpkdnseFFEGVDMNLVD--WLRQ---YAPEDEQtetflrgflgrmLFSG---------------EEVKKKA- 438
Cdd:COG2274 532 I-------------LIDGIDLRQIDpaSLRRqigVVLQDVF------------LFSGtirenitlgdpdatdEEIIEAAr 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 439 -----------------------SVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG--SIIFT 493
Cdd:COG2274 587 laglhdfiealpmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIII 666
|
250 260 270
....*....|....*....|....*....|....*...
gi 499595078 494 SYDFEFINtIANRVIDLNQsGGLSKEVPYEEYLQEIGV 531
Cdd:COG2274 667 AHRLSTIR-LADRIIVLDK-GRIVEDGTHEELLARKGL 702
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
332-512 |
5.04e-15 |
|
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: 74.04 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 332 EKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG--VTTSLSYFPK--------DNSE---FFEGV 398
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkDLTKLSLKELrrkvglvfQNPDdqfFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 DMNLVDWLRQYA-PEDEQTE--------TFLRGFLGRMLFSgeevkkkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:cd03225 94 EEEVAFGLENLGlPEEEIEErveealelVGLEGLRDRSPFT----------LSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499595078 470 HLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
7.15e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.35 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAVL 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDvattpsrelaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQD-HFAyeeER--VLDVVI-------KGheRLyevmKEKDEIYMkpdfsdEDGIRAAELEgefaemngwnaeadaasll 139
Cdd:COG4604 81 RQEnHIN---SRltVRELVAfgrfpysKG--RL----TAEDREII------DEAIAYLDLE------------------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 140 sglgisaDLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD------IPAIswLEDFLINFDNTVIVVSHD 211
Cdd:COG4604 127 -------DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsvqMMKL--LRRLADELGKTVVIVLHD 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
8.28e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDerlAVLKQDHFAyeEERV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE---PVPSRARHA--RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvvikgherlyEVMKEKDEiyMKPDFSDEDGIRAaelegeFAEMNGWNAeADAASLLSGLGISADLHDK---QMSELEN 158
Cdd:PRK13537 83 ------------GVVPQFDN--LDPDFTVRENLLV------FGRYFGLSA-AAARALVPPLLEFAKLENKadaKVGELSG 141
|
170 180
....*....|....*....|....*....
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
322-512 |
8.36e-15 |
|
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: 73.34 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 322 VQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKwgvttslsYFPKDNSEffegvdmn 401
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR--------VFGKPLEK-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 402 lvDWLR-QYAPedeQTETFLRGF---------LGRMLFSG------EEVKKKA-----------------SVLSGGEKVR 448
Cdd:cd03235 66 --ERKRiGYVP---QRRSIDRDFpisvrdvvlMGLYGHKGlfrrlsKADKAKVdealervglseladrqiGELSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 449 CMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
9.56e-15 |
|
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: 76.87 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF-----GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD------ERLAV 68
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDltklsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 69 LK-------QDHFAYeeervldvvikgherLYEVMKEKDEIymkpdfsdEDGIRAaelegeFAEMNGWNAEADAASLLSG 141
Cdd:COG1123 340 LRrrvqmvfQDPYSS---------------LNPRMTVGDII--------AEPLRL------HGLLSRAERRERVAELLER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 142 LGISADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISW-----LEDFLINFDNTVIVVSHDRHFLN 216
Cdd:COG1123 391 VGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQAqilnlLRDLQRELGLTYLFISHDLAVVR 469
|
250
....*....|....
gi 499595078 217 NVCTHIADLDFGKI 230
Cdd:COG1123 470 YIADRVAVMYDGRI 483
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-230 |
1.01e-14 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 73.69 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLF----EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKD------------ 63
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 64 -ERLAVLKQDHFAyeeerVLDVVIKGHERLYEVMKEKdeiymKPDFSDEDgIRAAELEgefaemngwnaeadaasLLSGL 142
Cdd:cd03257 81 rKEIQMVFQDPMS-----SLNPRMTIGEQIAEPLRIH-----GKLSKKEA-RKEAVLL-----------------LLVGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 143 GISADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPaiswLEDFLIN--------FDNTVIVVSHDRHF 214
Cdd:cd03257 133 GLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS----VQAQILDllkklqeeLGLTLLFITHDLGV 208
|
250
....*....|....*.
gi 499595078 215 LNNVCTHIADLDFGKI 230
Cdd:cd03257 209 VAKIADRVAVMYAGKI 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
320-510 |
1.40e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 76.17 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGE-KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTT----------SLSYF 387
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKdNSEFFEGVDMNLVDWLRQYAPEDEQTE--------TFLRGfLGRMLfsGEEVKKKASVLSGGEKVRCMLSKMMLSSA 459
Cdd:TIGR02857 402 PQ-HPFLFAGTIAENIRLARPDASDAEIREaleragldEFVAA-LPQGL--DTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499595078 460 NVLLLDEPTNHLDLESITAVNDGLASFKG--SIIFTSYDFEFInTIANRVIDL 510
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-512 |
1.60e-14 |
|
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: 72.63 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTfkwgvTTSLSYFPKDNSEFFE--G 397
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE-----ITFDGKSYQKNIEALRriG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 VdmnLVD--WLRQYAPEDEQTETFLRGFLGR---------MLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDE 466
Cdd:cd03268 76 A---LIEapGFYPNLTARENLRLLARLLGIRkkridevldVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499595078 467 PTNHLDLESITAVND---GLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03268 153 PTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
320-495 |
1.94e-14 |
|
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: 72.01 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTS--LSYFPKDNSEFFEG 397
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 VD---------MNLVDWLR-----QYAPEDEQTETFLRGFLGRMlfsgeevkkkASVLSGGEKVRCMLSKMMLSSANVLL 463
Cdd:TIGR01189 81 LPglkpelsalENLHFWAAihggaQRTIEDALAAVGLTGFEDLP----------AAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 499595078 464 LDEPTNHLDLESITAVNDGLASF---KGSIIFTSY 495
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-230 |
2.73e-14 |
|
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: 72.60 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGD-RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG--EIDSQTGHVS-------MGKDER-----L 66
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGSVLIDgtdinklKGKALRqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 AVLKQDHFAYEEERVLDVVikgherlyevmkekdeiymkpdfsdedgiraaeLEGEFAEMNGWNA------EAD---AAS 137
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV---------------------------------LSGRLGRRSTWRSlfglfpKEEkqrALA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 138 LLSGLGIsADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAIS-----WLEDFLINFDNTVIVVSHDR 212
Cdd:cd03256 128 ALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD-PASSrqvmdLLKRINREEGITVIVSLHQV 205
|
250
....*....|....*...
gi 499595078 213 HFLNNVCTHIADLDFGKI 230
Cdd:cd03256 206 DLAREYADRIVGLKDGRI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 |
2.95e-14 |
|
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: 75.19 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRF--GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAV 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDlrdldeddlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 69 LKQDHFayeeerVLDVVIKGHERLyevmkekdeiyMKPDFSDEDGIRA---AELEGEFAEM-NGWNAE-ADAASLLSGlG 143
Cdd:COG4987 414 VPQRPH------LFDTTLRENLRL-----------ARPDATDEELWAAlerVGLGDWLAALpDGLDTWlGEGGRRLSG-G 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 144 isadlhdkqmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDIP-AISWLEDFLINFDN-TVIVVSHDRHFLNNVcTH 221
Cdd:COG4987 476 ----------------ERRRLALARALLRDAPILLLDEPTEGLDAAtEQALLADLLEALAGrTVLLITHRLAGLERM-DR 538
|
....*....
gi 499595078 222 IADLDFGKI 230
Cdd:COG4987 539 ILVLEDGRI 547
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
4.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 11 FGDRKLFeDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEERVLDVVIKGHE 90
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 91 RLYEVMKEKDEIYMKPDFsdedGIRAAElegefaemngwnAEADAASLLSGLGISADLHDKQMSELENNQKVKVLLAQSL 170
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNF----GIPKEK------------AEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499595078 171 FGEPDVLLLDEPTNGLDIPA-ISWLEDF--LINFDNTVIVVSH 210
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTH 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-473 |
4.48e-14 |
|
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: 72.00 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGdseiA----KTTLLKILAGEMEPDEGTFKWG-----------VTTS 383
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLG----PngsgKSTLLRALAGLLKPSSGEVLLDgrdlaslsrreLARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 384 LSYFPKDNSeffegVDMNL-------------VDWLRQYAPEDEQ------TETFLRGFLGRMLFSgeevkkkasvLSGG 444
Cdd:COG1120 77 IAYVPQEPP-----APFGLtvrelvalgryphLGLFGRPSAEDREaveealERTGLEHLADRPVDE----------LSGG 141
|
170 180
....*....|....*....|....*....
gi 499595078 445 EKVRCMLSKMMLSSANVLLLDEPTNHLDL 473
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-473 |
4.85e-14 |
|
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: 70.54 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 321 TVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEffegvdm 400
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR------- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 401 nLVDWLRQYApedEQTEtfLRGFLGRMLFSgeevkkkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDL 473
Cdd:cd03214 74 -KIAYVPQAL---ELLG--LAHLADRPFNE----------LSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-225 |
5.03e-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: 74.63 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDR-KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQDHF----AY 76
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLADADADSWrdqiAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEER--VLDVVIKGHERLYevmkekdeiymKPDFSDEDGIRAAELegefaemngwnaeADAASLLSGLGISADLH-DKQM 153
Cdd:TIGR02857 401 VPQHpfLFAGTIAENIRLA-----------RPDASDAEIREALER-------------AGLDEFVAALPQGLDTPiGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN--TVIVVSHDRHFLNNvCTHIADL 225
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-213 |
5.48e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQD-HFayeeE 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYL----D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGHERLyevmkekdeiymKPdfsdedGIRAAELEGEFAEMNgwnaeadaasllsglgiSADLHDKQMSELENN 159
Cdd:PRK09544 80 TTLPLTVNRFLRL------------RP------GTKKEDILPALKRVQ-----------------AGHLIDAPMQKLSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDfLIN-----FDNTVIVVSHDRH 213
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD-LIDqlrreLDCAVLMVSHDLH 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
7.03e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSmgkderlavlkqdhfayeeerV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT---------------------V 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVVIKGHERLyevmkEKDEIYMKPDFSDED---GIRAAELE-GEFAEMNGWNAEADAASLLSglgiSADLHDK---QMS 154
Cdd:PRK13536 101 LGVPVPARARL-----ARARIGVVPQFDNLDlefTVRENLLVfGRYFGMSTREIEAVIPSLLE----FARLESKadaRVS 171
|
170 180 190
....*....|....*....|....*....|...
gi 499595078 155 ELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-230 |
7.51e-14 |
|
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: 70.70 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGD--RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDERL---AVLKQdHFA 75
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRQldpADLRR-NIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YEEERVldVVIKGHERlyevmkekDEIYM-KPDFSDEDGIRAAELegefaemngwnaeadaasllSGLGISADLH----D 150
Cdd:cd03245 82 YVPQDV--TLFYGTLR--------DNITLgAPLADDERILRAAEL--------------------AGVTDFVNKHpnglD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 151 KQMSE----LENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLInfDNTVIVVSHDRHFLnNVCTHI 222
Cdd:cd03245 132 LQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSeerlKERLRQLLG--DKTLIIITHRPSLL-DLVDRI 208
|
....*...
gi 499595078 223 ADLDFGKI 230
Cdd:cd03245 209 IVMDSGRI 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-230 |
9.08e-14 |
|
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: 70.24 E-value: 9.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD--------ERLAVLKQD 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDvtgvpperRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAYEEERVLDVVIKGherlyevmkekdeiyMKPDFSDEDGIRAAELEgefaemngwnaeadaasLLSGLGISADLHdKQ 152
Cdd:cd03259 81 YALFPHLTVAENIAFG---------------LKLRGVPKAEIRARVRE-----------------LLELVGLEGLLN-RY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 153 MSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISW-----LEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDF 227
Cdd:cd03259 128 PHELSGGQQQRVALARALAREPSLLLLDEPLSALD-AKLREelreeLKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
...
gi 499595078 228 GKI 230
Cdd:cd03259 207 GRI 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-187 |
9.76e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.97 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGDRKLFE-----DVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEER 80
Cdd:PRK13634 7 KVEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VlDVVIKGHE-RLYEVMKEKDEIYMKPDF--SDEDgiraaelegefaemngwnAEADAASLLSGLGISADLHDKQMSELE 157
Cdd:PRK13634 87 V-GIVFQFPEhQLFEETVEKDICFGPMNFgvSEED------------------AKQKAREMIELVGLPEELLARSPFELS 147
|
170 180 190
....*....|....*....|....*....|
gi 499595078 158 NNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-229 |
1.70e-13 |
|
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: 68.56 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDR--KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG----KDERLAVLkQDHFA 75
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgvdlRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YeeerVL-DVVIkgherlyevmkekdeiymkpdFSDEdgIRAaelegefaemNgwnaeadaasLLSGlGisadlhdkqms 154
Cdd:cd03228 80 Y----VPqDPFL---------------------FSGT--IRE----------N----------ILSG-G----------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 155 elennQKVKVLLAQSLFGEPDVLLLDEPTNGLDIP-AISWLEDFLINFDN-TVIVVSHDRHFLNNvCTHIADLDFGK 229
Cdd:cd03228 101 -----QRQRIAIARALLRDPPILILDEATSALDPEtEALILEALRALAKGkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-512 |
1.88e-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: 69.53 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMnPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTS---------LSYFPK 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 390 DNSEF--FEGVDM-NLVDWLRQYAPEDEQTEtfLRGFLGRM-LfsGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLD 465
Cdd:cd03264 80 EFGVYpnFTVREFlDYIAWLKGIPSKEVKAR--VDEVLELVnL--GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499595078 466 EPTNHLDLESITAVND---GLASFKgSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03264 156 EPTAGLDPEERIRFRNllsELGEDR-IVILSTHIVEDVESLCNQVAVLNK 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
1.96e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.96 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 19 DVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEERVLDVVIKGHERLYEVMKE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFEDTVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 99 KDEIYMKPDFSdedgiraaelegefaeMNGWNAEADAASLLSGLGISADLHDKQMSELENNQKVKVLLAQSLFGEPDVLL 178
Cdd:PRK13646 105 REIIFGPKNFK----------------MNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 499595078 179 LDEPTNGLD----IPAISWLEDFLINFDNTVIVVSHD 211
Cdd:PRK13646 169 LDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
321-523 |
5.77e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 321 TVQGLSKTIDGEK-VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFP----------- 388
Cdd:PRK11819 8 TMNRVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPqepqldpektv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 KDNSEffEGVD--MNLVDWLRQ----YAPEDEQTETFLRgflgRM--------------LFSGEEVKKKA---------- 438
Cdd:PRK11819 88 RENVE--EGVAevKAALDRFNEiyaaYAEPDADFDALAA----EQgelqeiidaadawdLDSQLEIAMDAlrcppwdakv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 439 SVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSGGlsk 518
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRG--- 238
|
....*
gi 499595078 519 eVPYE 523
Cdd:PRK11819 239 -IPWE 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-230 |
6.43e-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: 67.94 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG--EIDSQT----GHVSMGKDERLAVLKQD--- 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPDSGTiiidGLKLTDDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 ---HFA-YEEERVLDVVIKGherLYEVMKE-KDEiymkpdfsdedgiraaelegefaemngwnAEADAASLLSGLGIsAD 147
Cdd:cd03262 81 vfqQFNlFPHLTVLENITLA---PIKVKGMsKAE-----------------------------AEERALELLEKVGL-AD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 148 LHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHIAD 224
Cdd:cd03262 128 KADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIF 207
|
....*.
gi 499595078 225 LDFGKI 230
Cdd:cd03262 208 MDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
6.51e-13 |
|
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: 68.38 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDR----KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKDerlaVLKQDHFA 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvDGTD----LTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YEEERVLDVVIKGHERLyevmkekdeiymkpdFSDEDGIRAAELEGEFAEMNGWNAEADAASLLSGLGISaDLHDKQMSE 155
Cdd:cd03258 77 LRKARRRIGMIFQHFNL---------------LSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLE-DKADAYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 156 LENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPA-----ISWLEDflIN--FDNTVIVVSHDRHFLNNVCTHIADLDFG 228
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALD-PEttqsiLALLRD--INreLGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
..
gi 499595078 229 KI 230
Cdd:cd03258 218 EV 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-507 |
6.64e-13 |
|
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: 67.92 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKT--IDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTT-------SLSYF 387
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysIRTdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKDNSeFFEGvdMNLVDWLRQYA--------PEDEQTETFLRGFLgrmlfSGEEVKKKASVLSGGEKVRCMLSKMMLSSA 459
Cdd:cd03263 81 PQFDA-LFDE--LTVREHLRFYArlkglpksEIKEEVELLLRVLG-----LTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499595078 460 NVLLLDEPTNHLDLESITAVNDGLASFKG--SIIFTSYDFEFINTIANRV 507
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
319-485 |
7.46e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTS--------LSYF 387
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgktATRGdrsrfmayLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKDNSEFFEGVDMNLVDWLRQYAPEdeQTETFLRGFLGRMLFSGEEVKKkasvLSGGEKVRCMLSKMMLSSANVLLLDEP 467
Cdd:PRK13543 91 PGLKADLSTLENLHFLCGLHGRRAK--QMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170
....*....|....*...
gi 499595078 468 TNHLDLESITAVNDGLAS 485
Cdd:PRK13543 165 YANLDLEGITLVNRMISA 182
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-230 |
7.87e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAVL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgDKPismlssrqlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQDHFAYEEERVLDVVIKG---HERLYEVMKEKDeiymkpdfsdedgiraaelegefaemngwnaEADAASLLSGLGISA 146
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLWGRLSAED-------------------------------NARVNQAMEQTRINH 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 147 dLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDrhfLNNV---CT 220
Cdd:PRK11231 131 -LADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD---LNQAsryCD 206
|
250
....*....|
gi 499595078 221 HIADLDFGKI 230
Cdd:PRK11231 207 HLVVLANGHV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
292-512 |
8.23e-13 |
|
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: 68.13 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 292 IELDDIQPSSRRYpyvkftpEREIGNdLLTVQGLSKTIDGEKV-LDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEME 370
Cdd:cd03267 1 IEVSNLSKSYRVY-------SKEPGL-IGSLKSLFKRKYREVEaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 371 PDEGTFKwgvttSLSYFPKDNSEFFE---GV----------DMNLVDWLRQ----YAPEDEQTETFLRGfLGRMLFSGEE 433
Cdd:cd03267 73 PTSGEVR-----VAGLVPWKRRKKFLrriGVvfgqktqlwwDLPVIDSFYLlaaiYDLPPARFKKRLDE-LSELLDLEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 434 VKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGL----ASFKGSIIFTSYDFEFINTIANRVID 509
Cdd:cd03267 147 LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeynRERGTTVLLTSHYMKDIEALARRVLV 226
|
...
gi 499595078 510 LNQ 512
Cdd:cd03267 227 IDK 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-524 |
1.07e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.05 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD---------ERLAVlk 70
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPvrfrsprdaQAAGI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 71 qdHFAYEEervLDVVikgherlyevmkekdeiymkPDFSdedgirAAE---LEGE--------FAEMNgwnaeADAASLL 139
Cdd:COG1129 82 --AIIHQE---LNLV--------------------PNLS------VAEnifLGREprrgglidWRAMR-----RRARELL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 140 SGLGISADLhDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLedflinFDN---------TVIVVSh 210
Cdd:COG1129 126 ARLGLDIDP-DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL------FRIirrlkaqgvAIIYIS- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 211 drHFLN---NVCTHIADL-DfGKiklYVGNYDFwyqSS----QLAQKMaqeqnkkkeekikelqdfIARfsanaskskqa 282
Cdd:COG1129 198 --HRLDevfEIADRVTVLrD-GR---LVGTGPV---AEltedELVRLM------------------VGR----------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 283 tsrkkqlekiELDDIQPssrrypyvkfTPEREIGNDLLTVQGLSktidGEKVLDNISFTMNPNDkaILiGdseIA----- 357
Cdd:COG1129 240 ----------ELEDLFP----------KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGE--IL-G---IAglvga 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 358 -KTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFFEGVDMNL---VDWLRQ---YAPEDEQTE------------- 417
Cdd:COG1129 290 gRTELARALFGADPADSGEI-----------------RLDGKPVRIrspRDAIRAgiaYVPEDRKGEglvldlsirenit 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 418 -TFLRGFLGRMLFSGEEVKKKA------------------SVLSGG--EKVrcMLSKMMLSSANVLLLDEPTNHLDL--- 473
Cdd:COG1129 353 lASLDRLSRGGLLDRRRERALAeeyikrlriktpspeqpvGNLSGGnqQKV--VLAKWLATDPKVLILDEPTRGIDVgak 430
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 499595078 474 -ESITAVNDgLASfKG-SIIFTSYDFEFINTIANRVIDLNQsGGLSKEVPYEE 524
Cdd:COG1129 431 aEIYRLIRE-LAA-EGkAVIVISSELPELLGLSDRILVMRE-GRIVGELDREE 480
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-210 |
1.18e-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: 66.09 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRK--LFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDERLAVLKQ--DHFAY 76
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 eeervldvvikgherlyeVMKEkDEIymkpdfsdedgiraaeLEGEFAEmngwnaeadaaSLLSGlgisadlhdkqmsel 156
Cdd:cd03246 81 ------------------LPQD-DEL----------------FSGSIAE-----------NILSG--------------- 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 157 enNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFD---NTVIVVSH 210
Cdd:cd03246 100 --GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-211 |
1.56e-12 |
|
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: 66.93 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGDRKLFEDVNIKFT-EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEERV--- 81
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ---------LDVvikgherlyevmKEKDEIYMKPDFSDEDGIRAAELegefaemngwnaeadaaslLSGLGISaDLHDKQ 152
Cdd:cd03297 81 fqqyalfphLNV------------RENLAFGLKRKRNREDRISVDEL-------------------LDLLGLD-HLLNRY 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 153 MSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSHD 211
Cdd:cd03297 129 PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-230 |
1.83e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDE-----------RLAVLK 70
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 71 QDHFAYEEERVLDVVIKG---HERLYEVMKEKdeiymkpdfsDEDGIRAAelegefaemngwnaeadaaslLSGLGISaD 147
Cdd:PRK10253 88 QNATTPGDITVQELVARGrypHQPLFTRWRKE----------DEEAVTKA---------------------MQATGIT-H 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 148 LHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN----TVIVVSHDrhfLNNVC---T 220
Cdd:PRK10253 136 LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQACryaS 212
|
250
....*....|
gi 499595078 221 HIADLDFGKI 230
Cdd:PRK10253 213 HLIALREGKI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-519 |
1.88e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQdhfayeeer 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-GNPCARLTP--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 vldvvIKGHER-LYEVMKEKdeiYMKPDFSDEDGIRaaelegeFAEMNGWNAEADAASLLSGLGISADLHDKQMS-ELEN 158
Cdd:PRK15439 81 -----AKAHQLgIYLVPQEP---LLFPNLSVKENIL-------FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSlEVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 159 NQKVKVLlaQSLFGEPDVLLLDEPTNGLDIPAISWLedF-----LINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKly 233
Cdd:PRK15439 146 RQIVEIL--RGLMRDSRILILDEPTASLTPAETERL--FsrireLLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 234 vgnydfwyqssqLAQKMAQEQNKkkeekikelqDFIArfsANASKSKQATSRKKQLEKIELddiqPSSRRypyvkftpER 313
Cdd:PRK15439 220 ------------LSGKTADLSTD----------DIIQ---AITPAAREKSLSASQKLWLEL----PGNRR--------QQ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 314 EIGNDLLTVQGLSktidGEKVLDnISFTMNPNDkaIL-------IGDSEIAKTT--LLKILAGEMEPDEGTFKWGVT--- 381
Cdd:PRK15439 263 AAGAPVLTVEDLT----GEGFRN-ISLEVRAGE--ILglagvvgAGRTELAETLygLRPARGGRIMLNGKEINALSTaqr 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 382 --TSLSYFPKDNSE---FFE--------GVDMNLVDWLRQYAPEDEQTETFLRGfLGrMLFSGEEvkKKASVLSGGEKVR 448
Cdd:PRK15439 336 laRGLVYLPEDRQSsglYLDaplawnvcALTHNRRGFWIKPARENAVLERYRRA-LN-IKFNHAE--QAARTLSGGNQQK 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 449 CMLSKMMLSSANVLLLDEPTNHLDlesITAVND------GLASFKGSIIFTSYDFEFINTIANRVIDLNQ---SGGLSKE 519
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVD---VSARNDiyqlirSIAAQNVAVLFISSDLEEIEQMADRVLVMHQgeiSGALTGA 488
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-230 |
2.02e-12 |
|
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: 65.14 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGhvsmgkderlavlkqdhfayeeerv 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 lDVVIKGHERLYEvmkekdeiymkpdfSDEDGIRAaelegefaemngwnaeadaasllsglGISA----DLHDKQMsele 157
Cdd:cd03216 56 -EILVDGKEVSFA--------------SPRDARRA--------------------------GIAMvyqlSVGERQM---- 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 158 nnqkvkVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03216 91 ------VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-233 |
2.06e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 66.79 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 9 LRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKDE---RLAVLKQDHFAYEEERVLDV 84
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvRGRVSsllGLGGGFNPELTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 85 VIKGHERlyEVMKEK-DEIYmkpdfsdedgiraaelegEFAEmngwnaeadaasllsgLGisaDLHDKQMSELENNQKVK 163
Cdd:cd03220 110 RLLGLSR--KEIDEKiDEII------------------EFSE----------------LG---DFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 164 VLLAQSLFGEPDVLLLDEPTNGLD----IPAISWLEDFLINfDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLY 233
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDaafqEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
2.17e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 69.31 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRF-GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQDHFAY---- 76
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRrvsv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 --EEERVLDVVIKGHERLyevmkekdeiyMKPDFSDEDGIRAAELEGefaemngwnAEADAASLLSGLGISADLHDKQMS 154
Cdd:TIGR02868 414 caQDAHLFDTTVRENLRL-----------ARPDATDEELWAALERVG---------LADWLRALPDGLDTVLGEGGARLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 155 eleNNQKVKVLLAQSLFGEPDVLLLDEPTNGLDI-PAISWLEDFLINFDN-TVIVVSHD 211
Cdd:TIGR02868 474 ---GGERQRLALARALLADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHH 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-233 |
2.19e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF-----GDRKLFE-----------------DVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhePSRSLKElllrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 59 SMgkDERLAVLkqdhfayeeervLDVvikGHErlyevmkekdeiyMKPDFSDEDGIRaaelegefaeMNGwnaeadaasL 138
Cdd:COG1134 84 EV--NGRVSAL------------LEL---GAG-------------FHPELTGRENIY----------LNG---------R 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 139 LsgLGISADLHDKQM------SELEN--NQKVK-------VLLAqslFG-----EPDVLLLDEPTNGLDIP----AISWL 194
Cdd:COG1134 115 L--LGLSRKEIDEKFdeivefAELGDfiDQPVKtyssgmrARLA---FAvatavDPDILLVDEVLAVGDAAfqkkCLARI 189
|
250 260 270
....*....|....*....|....*....|....*....
gi 499595078 195 EDFLINfDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLY 233
Cdd:COG1134 190 RELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
2.22e-12 |
|
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: 66.34 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDR----KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM------GKDERLAVLKQ 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 DHFAYEEERVLDVVIKGHERlyevmkekdeiymkpdfsdeDGIRAAELEgefaemngwnAEADAASLLSGLGISADLHDK 151
Cdd:cd03293 81 QDALLPWLTVLDNVALGLEL--------------------QGVPKAEAR----------ERAEELLELVGLSGFENAYPH 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 152 QMSeleNNQKVKVLLAQSLFGEPDVLLLDEPTNGLDipAIS------WLEDFLINFDNTVIVVSHD 211
Cdd:cd03293 131 QLS---GGMRQRVALARALAVDPDVLLLDEPFSALD--ALTreqlqeELLDIWRETGKTVLLVTHD 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-512 |
3.11e-12 |
|
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: 65.59 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFF---- 395
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 -EGVDMNL--VDWLRQYAP--EDEQTETflrgFLGRMLFSGEEVKKKASvLSGGEKVRCMLSKMMLSSANVLLLDEPTNH 470
Cdd:cd03231 81 aPGIKTTLsvLENLRFWHAdhSDEQVEE----ALARVGLNGFEDRPVAQ-LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499595078 471 LDLESITAVNDGLASF---KGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03231 156 LDKAGVARFAEAMAGHcarGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-473 |
3.20e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.72 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFK--------W---------GV- 380
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWspaelarrrAVl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 381 --TTSLSyFPkdnsefF---EGVDMNLVDWLRQYAPEDEQTETFLR-----GFLGRMLFSgeevkkkasvLSGGEKVRCM 450
Cdd:PRK13548 82 pqHSSLS-FP------FtveEVVAMGRAPHGLSRAEDDALVAAALAqvdlaHLAGRDYPQ----------LSGGEQQRVQ 144
|
170 180
....*....|....*....|....*....
gi 499595078 451 LSKMM--LSSAN----VLLLDEPTNHLDL 473
Cdd:PRK13548 145 LARVLaqLWEPDgpprWLLLDEPTSALDL 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-479 |
3.29e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW--------GVTTSLSYF-PKD 390
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdiddpDVAEACHYLgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 NSEFFEGVDMNLVDWLRQYAPEDEQTETFLRGF-LGRMLfsgeevKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:PRK13539 83 AMKPALTVAENLEFWAAFLGGEELDIAAALEAVgLAPLA------HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|
gi 499595078 470 HLDLESITAV 479
Cdd:PRK13539 157 ALDAAAVALF 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-198 |
5.53e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.12 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTF-------LKILSGEIDSQTGHVSmgkdeRLAVLKQDH 73
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALaralageLPLLSGERQSQFSHIT-----RLSFEQLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 74 FAYEEervldvvikgHERLYEVMKEKDEiymkpdfsDEDGIRAAELEgefaeMNGWNAEADAASLLSGLGISaDLHDKQM 153
Cdd:PRK10938 78 LVSDE----------WQRNNTDMLSPGE--------DDTGRTTAEII-----QDEVKDPARCEQLAQQFGIT-ALLDRRF 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFL 198
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-525 |
5.63e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 65.72 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT-------------FKWGVTT---S 383
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEilldgkditnlppHKRPVNTvfqN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 384 LSYFPKDNseFFEGVDMNLVdwlRQYAPEDEQTETFLRGFlgRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLL 463
Cdd:cd03300 81 YALFPHLT--VFENIAFGLR---LKKLPKAEIKERVAEAL--DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 464 LDEPTNHLDL-------ESITAVNDGLASfkgSIIFTSYDFEFINTIANRVIDLNQSGGLSKEVPYEEY 525
Cdd:cd03300 154 LDEPLGALDLklrkdmqLELKRLQKELGI---TFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-511 |
6.52e-12 |
|
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: 64.85 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTT------SLSYFPKD 390
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdVTGvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 NSEF-----FEGVDMNLVdwlRQYAPEDEQTETFLRgfLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLD 465
Cdd:cd03259 81 YALFphltvAENIAFGLK---LRGVPKAEIRARVRE--LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499595078 466 EPTNHLDLES----ITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLN 511
Cdd:cd03259 156 EPLSALDAKLreelREELKELQRELGITTIYVTHDQEEALALADRIAVMN 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
7.03e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.92 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 11 FGDRKLFeDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEERVLDVVIKGHE 90
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 91 RLYEVMKEKDEIYMKPDFsdedGIRAAElegefaemngwnAEADAASLLSGLGISADLHDKQMSELENNQKVKVLLAQSL 170
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNF----GVSQEE------------AEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170
....*....|....*..
gi 499595078 171 FGEPDVLLLDEPTNGLD 187
Cdd:PRK13649 161 AMEPKILVLDEPTAGLD 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-508 |
7.05e-12 |
|
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: 63.60 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEgtfkwgvttslsyfpkdnseffegvd 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 mnlvdwlrqyapedeqtetflrgflGRMLFSGEEVK-------KKASV-----LSGGEKVRCMLSKMMLSSANVLLLDEP 467
Cdd:cd03216 55 -------------------------GEILVDGKEVSfasprdaRRAGIamvyqLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499595078 468 TNHLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVI 508
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-211 |
7.56e-12 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 65.05 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLfEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD--------ERLAVLKQD 72
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDitnlppekRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAYEEERVLDVVIKGHeRLYEVMKEKDEIYMKpdfsdedgiraaelegEFAEMngwnaeadaasllsgLGISADLHDKQ 152
Cdd:cd03299 80 YALFPHMTVYKNIAYGL-KKRKVDKKEIERKVL----------------EIAEM---------------LGIDHLLNRKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 153 MSeLENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDI----PAISWLEDFLINFDNTVIVVSHD 211
Cdd:cd03299 128 ET-LSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-230 |
1.24e-11 |
|
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: 64.67 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQdhfayeeERV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-------ERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVVIKgHERLYEVMKEKDEI----YMKPDFS--DEDGIRAAelegefaemngwnaeadAASLLSGLGISAdLHDKQMSE 155
Cdd:cd03296 76 VGFVFQ-HYALFRHMTVFDNVafglRVKPRSErpPEAEIRAK-----------------VHELLKLVQLDW-LADRYPAQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 156 LENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
332-472 |
1.30e-11 |
|
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: 63.49 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 332 EKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTfkwgVTtslsyfpkdnsefFEGVDM-NLVDWLRQYA 410
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE----IT-------------LDGVPVsDLEKALSSLI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 411 PEDEQT----ETFLRGFLGRMLfsgeevkkkasvlSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:cd03247 78 SVLNQRpylfDTTLRNNLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-512 |
1.44e-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: 64.38 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEG------------------------T 375
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgeditglppheiarlgigrT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 376 FKwgvTTSLsyFPK----DN----SEFFEGVDMNLVDWLRQYAPEDEQTETFLRgFLGrmLfsGEEVKKKASVLSGGEKV 447
Cdd:cd03219 81 FQ---IPRL--FPEltvlENvmvaAQARTGSGLLLARARREEREARERAEELLE-RVG--L--ADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 448 RCMLSKMMLSSANVLLLDEPT---NHLDLESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
1.64e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGhvsmgkderlAVLKQDhfayeeeR 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKG----------AVLWQG-------K 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGherLYEVMKEKDEIYMKPD----FSDEDGIRAaelegeFAEMNGWNAEADAASLL-SGLGISADLHDKQ--M 153
Cdd:PRK13638 64 PLDYSKRG---LLALRQQVATVFQDPEqqifYTDIDSDIA------FSLRNLGVPEAEITRRVdEALTLVDAQHFRHqpI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPA-----ISWLEDfLINFDNTVIVVSHD 211
Cdd:PRK13638 135 QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD-PAgrtqmIAIIRR-IVAQGNHVIISSHD 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
350-512 |
1.87e-11 |
|
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: 63.67 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 350 LIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTS------LSYFPKDNSEF-----FEGVDMNLVDWLRqYAPEDEQ 415
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdVTAAppadrpVSMLFQENNLFahltvEQNVGLGLSPGLK-LTAEDRQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 416 TetfLRGFLGRMLFSGEEvKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD----LESITAVNDGLASFKGSII 491
Cdd:cd03298 108 A---IEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVL 183
|
170 180
....*....|....*....|.
gi 499595078 492 FTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03298 184 MVTHQPEDAKRLAQRVVFLDN 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-223 |
2.26e-11 |
|
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: 66.96 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 27 GNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDH--FAY-EEERVLDVVIKGHERLYEVMKEKdeiy 103
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHqnMGYcPQFDAIDDLLTGREHLYLYARLR---- 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 104 mkpdfsdedGIRAAELEgefaEMNGWNAEADAASLLSglgisadlhDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPT 183
Cdd:TIGR01257 2041 ---------GVPAEEIE----KVANWSIQSLGLSLYA---------DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499595078 184 NGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIA 223
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRLA 2141
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-534 |
2.68e-11 |
|
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: 63.51 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTI-DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTSlsyfpkdnseffeg 397
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDIT-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 vDMNLVDWLR------QYaPEDeqtetflrgflgrMLF-----------------SGEEVKKKA---------------- 438
Cdd:COG1122 67 -KKNLRELRRkvglvfQN-PDD-------------QLFaptveedvafgpenlglPREEIRERVeealelvglehladrp 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 439 -SVLSGGEKVR-CMLSKMMLSSAnVLLLDEPTNHLDLESITAVND---GLASFKGSIIFTSYDFEFINTIANRVIDLNQs 513
Cdd:COG1122 132 pHELSGGQKQRvAIAGVLAMEPE-VLVLDEPTAGLDPRGRRELLEllkRLNKEGKTVIIVTHDLDLVAELADRVIVLDD- 209
|
250 260
....*....|....*....|.
gi 499595078 514 GGLSKEVPYEEYLQEIGVLQK 534
Cdd:COG1122 210 GRIVADGTPREVFSDYELLEE 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-230 |
2.72e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLK-------ILSGEIDSQTGHVSMGK-DERL------ 66
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKVNDPKvDERLirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 AVLKQDHFaYEEERVLDVVIKGHERlyevmkekdeiymkpdfsdedgIRAAELEgefaemngwNAEADAASLLSGLGISA 146
Cdd:PRK09493 81 MVFQQFYL-FPHLTALENVMFGPLR----------------------VRGASKE---------EAEKQARELLAKVGLAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 147 DLHDKQmSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiP-----AISWLEDfLINFDNTVIVVSHDRHFLNNVCTH 221
Cdd:PRK09493 129 RAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALD-PelrheVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASR 205
|
....*....
gi 499595078 222 IADLDFGKI 230
Cdd:PRK09493 206 LIFIDKGRI 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-213 |
3.23e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.90 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSgEIDSQTGHVSMgkDERLAVLKQDHFayeEERV 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRV--EGRVEFFNQNIY---ERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvvikgheRLYEVMKEKDEIYMKPDF---SDEDGIRAAelegefAEMNGWNAEADAASLLSGLGISADLHD-------K 151
Cdd:PRK14258 82 ---------NLNRLRRQVSMVHPKPNLfpmSVYDNVAYG------VKIVGWRPKLEIDDIVESALKDADLWDeikhkihK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF----DNTVIVVSHDRH 213
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLH 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-211 |
3.58e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.34 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 21 NIKFT--EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKD---ERLAVLKQ-------------DHFAYEEerv 81
Cdd:COG4586 40 DISFTiePGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVpfkRRKEFARRigvvfgqrsqlwwDLPAIDS--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvvikgherlYEVMKekdEIYmkpdfsdedGIRAAELE---GEFAEMngwnaeadaasllsgLGISaDLHDKQMSELEN 158
Cdd:COG4586 117 -----------FRLLK---AIY---------RIPDAEYKkrlDELVEL---------------LDLG-ELLDTPVRQLSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFL--IN--FDNTVIVVSHD 211
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeYNreRGTTILLTSHD 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
5.12e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLK------------ILSGEID--------SQTGHVSM 60
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVynghniysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 61 GKdERLAVLKQDH---FAYEEERVLDVVIKGherlyevMKEKDEIymkpDFSDEDGIRAAELegefaemngWNAEADAas 137
Cdd:PRK14239 85 RK-EIGMVFQQPNpfpMSIYENVVYGLRLKG-------IKDKQVL----DEAVEKSLKGASI---------WDEVKDR-- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 138 llsglgisadLHDKQMSeLENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF--DNTVIVVSH 210
Cdd:PRK14239 142 ----------LHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTR 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-507 |
5.17e-11 |
|
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: 62.74 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIdGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTT------SLSYFPKD 390
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkdITNlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 NSEF-FEGVDMNLVDWLRQYAPEDEQTETFLRGfLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:cd03299 80 YALFpHMTVYKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499595078 470 HLDLES----ITAVNDGLASFKGSIIFTSYDFEFINTIANRV 507
Cdd:cd03299 159 ALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
294-512 |
5.55e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.47 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 294 LDDIQPSSRRYPYVKFTPEREIGNdlltvqgLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDE 373
Cdd:PRK11607 1 MNDAIPRPQAKTRKALTPLLEIRN-------LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 374 GTFKW-GVTTSL-------------SY--FPKDNseffegVDMNLVDWLRQyapeDEQTETFLRGFLGRML---FSGEEV 434
Cdd:PRK11607 74 GQIMLdGVDLSHvppyqrpinmmfqSYalFPHMT------VEQNIAFGLKQ----DKLPKAEIASRVNEMLglvHMQEFA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 435 KKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD--------LEsitaVNDGLASFKGSIIFTSYDFEFINTIANR 506
Cdd:PRK11607 144 KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLE----VVDILERVGVTCVMVTHDQEEAMTMAGR 219
|
....*.
gi 499595078 507 VIDLNQ 512
Cdd:PRK11607 220 IAIMNR 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-230 |
6.18e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 62.27 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG---------KDERLAVLKQD 72
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlppKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAYEEERVLDVVIKGherlYEVMKE-KDEIymkpdfsDEDGIRAAELegefaemngwnaeadaasllsgLGISADLhDK 151
Cdd:cd03301 81 YALYPHMTVYDNIAFG----LKLRKVpKDEI-------DERVREVAEL----------------------LQIEHLL-DR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD----IPAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDF 227
Cdd:cd03301 127 KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
...
gi 499595078 228 GKI 230
Cdd:cd03301 207 GQI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
320-534 |
8.00e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 64.40 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEK--VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG-----------VTTSLSY 386
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeddLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 387 FPkDNSEFFegvDMNLVDWLR---QYAPEDE--------QTETFLRGF---LGRMLfsGEevkkKASVLSGGEKVRCMLS 452
Cdd:COG4987 414 VP-QRPHLF---DTTLRENLRlarPDATDEElwaalervGLGDWLAALpdgLDTWL--GE----GGRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 453 KMMLSSANVLLLDEPTNHLDLESITAV-NDGLASFKG-SIIFTSYDFEFINtIANRVIDLNQsGGLSKEVPYEEYLQEIG 530
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGrTVLLITHRLAGLE-RMDRILVLED-GRIVEQGTHEELLAQNG 561
|
....
gi 499595078 531 VLQK 534
Cdd:COG4987 562 RYRQ 565
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
8.00e-11 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 62.18 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTT---------SLSYF 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdITKlpmhkrarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKDNSEFFE-GVDMNLVDWLRQYAPEDEQTETFLRGFLGrmLFSGEEV-KKKASVLSGGEKVRCMLSKMMLSSANVLLLD 465
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELLE--EFHITHLrKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 499595078 466 EP 467
Cdd:cd03218 159 EP 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
330-512 |
8.23e-11 |
|
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: 61.66 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTS----------LSYFPKDNSEFFEGV 398
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDIStipledlrssLTIIPQDPTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 DMNLvdwlrqyAPEDEQTETFLRGFLgrmlfsgeEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESita 478
Cdd:cd03369 99 RSNL-------DPFDEYSDEEIYGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT--- 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 499595078 479 vnDGLASfkgSIIFTSYDFEFINTIANR---VIDLNQ 512
Cdd:cd03369 161 --DALIQ---KTIREEFTNSTILTIAHRlrtIIDYDK 192
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-230 |
9.23e-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: 61.65 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRF-GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG-------KDERLAVLKQD-HFAY 76
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKiGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEERVLDvvikgHERLYE-VMKEKDEIYMKPdfsdedgiraaelegefaemNGWNAEADAASLLSGLgisADLHDKQMSE 155
Cdd:cd03292 85 QDFRLLP-----DRNVYEnVAFALEVTGVPP--------------------REIRKRVPAALELVGL---SHKHRALPAE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 156 LENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISWLEDFLINFDN----TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLD-PDTTWEIMNLLKKINkagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-512 |
9.79e-11 |
|
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: 64.15 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDG--EKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGeMEPDEGTfkwgVTTSLSYFPKD---NSE 393
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGR----ISGEVLLDGRDlleLSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 394 FFEGVDMNLV--DWLRQYAP---EDEQTETFLRGFLGRmlfsgEEVKKKA-----------------SVLSGGEKVRCML 451
Cdd:COG1123 79 ALRGRRIGMVfqDPMTQLNPvtvGDQIAEALENLGLSR-----AEARARVlelleavglerrldrypHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 452 SKMMLSSANVLLLDEPTNHLDLES---ITAVNDGLASFKG-SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDD 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-472 |
1.05e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttSLSYFPKDNSEFFEGV 398
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI------TLDGKPVEGPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 ---DMNLVDW----------LRQYAPEDEQTETFLRGFLGRMLFSGEEvKKKASVLSGGEKVRCMLSKMMLSSANVLLLD 465
Cdd:PRK11248 75 vfqNEGLLPWrnvqdnvafgLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
....*..
gi 499595078 466 EPTNHLD 472
Cdd:PRK11248 154 EPFGALD 160
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-187 |
1.11e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 7 VSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIdsqtghvSMGKDERLAVLKQDHFaYEEERVLdvvi 86
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------KGTPVAGCVDVPDNQF-GREASLI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 87 kgherlyevmkekDEIYMKPDFsdedgiraaelegefaemngwnaeADAASLLSGLGIS-ADLHDKQMSELENNQKVKVL 165
Cdd:COG2401 104 -------------DAIGRKGDF------------------------KDAVELLNAVGLSdAVLWLRRFKELSTGQKFRFR 146
|
170 180
....*....|....*....|..
gi 499595078 166 LAQSLFGEPDVLLLDEPTNGLD 187
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-512 |
1.25e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 61.12 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFFEGVD 399
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-----------------YIGGRD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 MNLVD--------WLRQYA--------------------PEDEQTETFLRgfLGRMLFSGEEVKKKASVLSGGEKVRCML 451
Cdd:cd03301 64 VTDLPpkdrdiamVFQNYAlyphmtvydniafglklrkvPKDEIDERVRE--VAELLQIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 452 SKMMLSSANVLLLDEPTNHLD----LESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-510 |
1.28e-10 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 61.35 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEK----VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFF 395
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-----------------RV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 EGVDMNlvdwlrqYAPEDEQTEtFLR---GF-------LGR----------MLFSG--------------EEV------K 435
Cdd:cd03255 64 DGTDIS-------KLSEKELAA-FRRrhiGFvfqsfnlLPDltalenvelpLLLAGvpkkerreraeellERVglgdrlN 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 436 KKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVND---GLASFKG-SIIFTSYDFEFINtIANRVIDL 510
Cdd:cd03255 136 HYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMEllrELNKEAGtTIVVVTHDPELAE-YADRIIEL 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-235 |
1.48e-10 |
|
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: 61.13 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 13 DRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQ---TGHVSMGKDERLAVLKQDHFAYEEErvLDVVIKG- 88
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCVAYVRQ--DDILLPGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 89 --HERLYevmkekdeiYMKPdfsdedgIRAAELEGEFAEmngwnAEADAASLLSGLGISaDLHDKQMSELENNQKVKVLL 166
Cdd:cd03234 97 tvRETLT---------YTAI-------LRLPRKSSDAIR-----KKRVEDVLLRDLALT-RIGGNLVKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 167 AQSLFGEPDVLLLDEPTNGLDipaiSWLEDFLINF-------DNTVIVVSHD-RHFLNNVCTHIADLDFGKIkLYVG 235
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLD----SFTALNLVSTlsqlarrNRIVILTIHQpRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
329-508 |
1.51e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 61.16 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 329 IDGEKVLD----NISFTMNPNDKAILiGDSEIAKTTLLKILAGEMEPDEGTFKWGVT----TSLSYF--PKD-------- 390
Cdd:cd03297 4 VDIEKRLPdftlKIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINlpPQQrkiglvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 NSEFFE--GVDMNLVDWLRQYAP-EDEQTETFLRGFLGrmlfSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEP 467
Cdd:cd03297 83 QYALFPhlNVRENLAFGLKRKRNrEDRISVDELLDLLG----LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499595078 468 TNHLD----LESITAVNDGLASFKGSIIFTSYDFEFINTIANRVI 508
Cdd:cd03297 159 FSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
320-512 |
1.63e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTSLSYfpkdnseffe 396
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditIDTARSL---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 397 GVDMNLVDWLRQY---------------APED-------------EQTETFLRGFLGRMLFSGEEvKKKASVLSGGEKVR 448
Cdd:PRK11264 74 SQQKGLIRQLRQHvgfvfqnfnlfphrtVLENiiegpvivkgepkEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 449 CMLSKMMLSSANVLLLDEPTNHLDLESITAVND---GLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNtirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
322-512 |
2.11e-10 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 60.98 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 322 VQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF--------------------KWGVT 381
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaelyrlrrRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 382 -------TSLSYFpkDNSEFfegvdmnlvdWLRQYA--PEDEQTEtFLRGFLGRMLFSGEEvKKKASVLSGGEKVRCMLS 452
Cdd:cd03261 83 fqsgalfDSLTVF--ENVAF----------PLREHTrlSEEEIRE-IVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 453 KMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKGS----IIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHDLDTAFAIADRIAVLYD 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-512 |
2.12e-10 |
|
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: 60.68 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 333 KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTS-----------LSYFPKDNSEFFEGVDMN 401
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpadlrrnIGYVPQDVTLFYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 402 LVdwLRQYAPEDEQ---------TETFLRGF---LGRMLfsGEevkkKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:cd03245 98 IT--LGAPLADDERilraaelagVTDFVNKHpngLDLQI--GE----RGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499595078 470 HLDLESITAVNDGLASFKG--SIIFTSYDFEFInTIANRVIDLNQ 512
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGdkTLIIITHRPSLL-DLVDRIIVMDS 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
325-508 |
2.26e-10 |
|
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: 60.88 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 325 LSKTiDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTsLSYFPKDNSEFFEGVdmnlVD 404
Cdd:cd03237 6 MKKT-LGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQYIKADYEGT----VR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 405 WLRQYAPEDEQTETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLA 484
Cdd:cd03237 80 DLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180
....*....|....*....|....*...
gi 499595078 485 SF----KGSIIFTSYDFEFINTIANRVI 508
Cdd:cd03237 160 RFaennEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-472 |
3.00e-10 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 60.18 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGE----KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF------KWGVTTSLSY--- 386
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYvfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 387 ----FP----KDNSEFfeGVDMNLVDWLRQYAPEDEQTETF-LRGFLGRmlFSGEevkkkasvLSGGEKVRCMLSKMMLS 457
Cdd:cd03293 81 qdalLPwltvLDNVAL--GLELQGVPKAEARERAEELLELVgLSGFENA--YPHQ--------LSGGMRQRVALARALAV 148
|
170
....*....|....*
gi 499595078 458 SANVLLLDEPTNHLD 472
Cdd:cd03293 149 DPDVLLLDEPFSALD 163
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
326-478 |
3.10e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 326 SKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEgtfkwGVTTSLSYFPKDNSEFFEGVDMNLVdw 405
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNV-----SVEGDIHYNGIPYKEFAEKYPGEII-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 406 lrqYAPED---------EQTETFLRGFLGRMLFSGeevkkkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDleSI 476
Cdd:cd03233 87 ---YVSEEdvhfptltvRETLDFALRCKGNEFVRG---------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SS 152
|
..
gi 499595078 477 TA 478
Cdd:cd03233 153 TA 154
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-218 |
3.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 15 KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKIL-------SGEI-----DSQTGHVSMGKDERLAVL-------KQDHFA 75
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdTGTIewifkDEKNKKKTKEKEKVLEKLviqktrfKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YEEERVLDVVIKGHE-RLYEVMKEKDEIYMKPDFsdedGIRAAElegefaemngwnAEADAASLLSGLGISADLHDKQMS 154
Cdd:PRK13651 101 KEIRRRVGVVFQFAEyQLFEQTIEKDIIFGPVSM----GVSKEE------------AKKRAAKYIELVGLDESYLQRSPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 155 ELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAISwlEDFLINFDN------TVIVVSHDrhfLNNV 218
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD-PQGV--KEILEIFDNlnkqgkTIILVTHD---LDNV 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
324-508 |
4.04e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 324 GLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEME--PDEGTFKwgvttslsyFPKDNSeffeGVDMN 401
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD---------VPDNQF----GREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 402 LVDWLRQYAPEDEQTEtflrgFLGRM-LFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLES--ITA 478
Cdd:COG2401 102 LIDAIGRKGDFKDAVE-----LLNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakRVA 176
|
170 180 190
....*....|....*....|....*....|...
gi 499595078 479 VNDGLAS--FKGSIIFTSYDFEFINTIA-NRVI 508
Cdd:COG2401 177 RNLQKLArrAGITLVVATHHYDVIDDLQpDLLI 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-482 |
4.34e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.78 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG-----------VTTSLSYFP 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 KDNSEFFE-----GVDMNLVDWLRQYAPEDEQTETFLRGFLGRM---LFSGEEVkkkaSVLSGGEKVRCMLSKMMLSSAN 460
Cdd:PRK09536 84 QDTSLSFEfdvrqVVEMGRTPHRSRFDTWTETDRAAVERAMERTgvaQFADRPV----TSLSGGERQRVLLARALAQATP 159
|
170 180 190
....*....|....*....|....*....|
gi 499595078 461 VLLLDEPTNHLD-------LESI-TAVNDG 482
Cdd:PRK09536 160 VLLLDEPTASLDinhqvrtLELVrRLVDDG 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-480 |
4.49e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 59.10 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDG------EKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAG--EMEPDEGTFkwgvttslsyfpkdn 391
Cdd:cd03213 4 LSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEV--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 392 seFFEGVDMNLVDWLRQ--YAPEDEQT-------ETflrgflgrMLFSGeevkkKASVLSGGEKVRCMLSKMMLSSANVL 462
Cdd:cd03213 69 --LINGRPLDKRSFRKIigYVPQDDILhptltvrET--------LMFAA-----KLRGLSGGERKRVSIALELVSNPSLL 133
|
170
....*....|....*...
gi 499595078 463 LLDEPTNHLDleSITAVN 480
Cdd:cd03213 134 FLDEPTSGLD--SSSALQ 149
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
330-484 |
4.67e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.10 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvttslsyfpkdnseffeGVD---MNLVDWL 406
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-----------------GVDirdLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 407 RQ--YAPEDeqteTFLrgF---------LGRMLFSGEEVK---KKASV---------------------LSGGEKVRCML 451
Cdd:COG1132 414 RQigVVPQD----TFL--FsgtirenirYGRPDATDEEVEeaaKAAQAhefiealpdgydtvvgergvnLSGGQRQRIAI 487
|
170 180 190
....*....|....*....|....*....|...
gi 499595078 452 SKMMLSSANVLLLDEPTNHLDLESITAVNDGLA 484
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALE 520
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-508 |
4.69e-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: 59.83 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGE----KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEF 394
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 395 FEGVDM---------N--------LVDWLRQYAPEDEQTETFLRGFLGRMLFSGEE--VKKKASVLSGGEKVRCMLSKMM 455
Cdd:cd03257 81 RKEIQMvfqdpmsslNprmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 456 LSSANVLLLDEPTNHLDLESITAVNDGL----ASFKGSIIFTSYDFEFINTIANRVI 508
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
331-530 |
4.81e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.06 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 331 GEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTT-----------SLSYFPKDNSEFF---- 395
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQEPYIFSgsil 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 --------EGVDMNLVDWLRQYAPEDEQTETFLRGFlgrmlfsGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEP 467
Cdd:TIGR01193 566 enlllgakENVSQDEIWAACEIAEIKDDIENMPLGY-------QTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 468 TNHLDLESITAVNDGLASFK-GSIIFTSYDFEfINTIANRVIDLnQSGGLSKEVPYEEYLQEIG 530
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQdKTIIFVAHRLS-VAKQSDKIIVL-DHGKIIEQGSHDELLDRNG 700
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
4.90e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGD-RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKderlavlkqdhfayeee 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGherLYEVMKEKDEIYMKPD---FSdedgirAAELEG-EFAEMNGWNAEAD----AASLLSGLGISaDLHDK 151
Cdd:PRK13636 68 KPIDYSRKG---LMKLRESVGMVFQDPDnqlFS------ASVYQDvSFGAVNLKLPEDEvrkrVDNALKRTGIE-HLKDK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLIN----FDNTVIVVSHDRHFLNNVCTHIADLDF 227
Cdd:PRK13636 138 PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqkeLGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
....*
gi 499595078 228 GKIKL 232
Cdd:PRK13636 218 GRVIL 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-484 |
4.97e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.17 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSE-------FFEGVDMNL 402
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVpdslpltVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 403 ---VDWLRQYAPEDEQ------TETFLRGFLGRMLfsgeevkkkaSVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDL 473
Cdd:NF040873 83 warRGLWRRLTRDDRAavddalERVGLADLAGRQL----------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170
....*....|.
gi 499595078 474 ESITAVNDGLA 484
Cdd:NF040873 153 ESRERIIALLA 163
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
7.28e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.38 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKftEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD-------ER-LAVLKQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDltalppaERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 DH--FAYeeervLDVvikgherlyevmkeKDEIY--MKPD--FSDEDgiraaelegefaemngwnaEADAASLLSGLGIs 145
Cdd:COG3840 79 ENnlFPH-----LTV--------------AQNIGlgLRPGlkLTAEQ-------------------RAQVEQALERVGL- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595078 146 ADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPA-----ISWLEDFLINFDNTVIVVSHD 211
Cdd:COG3840 120 AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PAlrqemLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
7.40e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgkDERLAVLKQDHFAYEeer 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV--DGKVLYFGKDIFQID--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 vldvVIKGHERLYEVMKEKDEIymkPDFSDEDGIrAAELEG----EFAEMNGWNAEAdaaslLSGLGISADLHDK---QM 153
Cdd:PRK14246 85 ----AIKLRKEVGMVFQQPNPF---PHLSIYDNI-AYPLKShgikEKREIKKIVEEC-----LRKVGLWKEVYDRlnsPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN--TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-187 |
9.74e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDV--NIKFT--EGNCYGLIGANGAGKSTFLKILSGeIDSQTGHVSMGKDERLAVLKQDHFAY 76
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVlhNVSFSigEGEMMAIVGSSGSGKSTLLHLLGG-LDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 EEERVLDVVIKGHERLyevmkekdeiymkPDFSDEDGIRAAELEGEfaeMNGWNAEADAASLLSGLGISADLHDKQmSEL 156
Cdd:PRK11629 84 LRNQKLGFIYQFHHLL-------------PDFTALENVAMPLLIGK---KKPAEINSRALEMLAAVGLEHRANHRP-SEL 146
|
170 180 190
....*....|....*....|....*....|.
gi 499595078 157 ENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK11629 147 SGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
319-508 |
1.04e-09 |
|
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: 58.53 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEK----VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTSLSYFP-KDNS 392
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 393 EFFEGvDMNLVDWL----------RQYAPEDEQTETFLRGFLGRMLFsGEEVKKKASVLSGGEKVRCMLSKMMLSSANVL 462
Cdd:cd03266 81 GFVSD-STGLYDRLtarenleyfaGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499595078 463 LLDEPTNHLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVI 508
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVV 207
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-515 |
1.14e-09 |
|
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: 59.06 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTT--------SLSYFP 388
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgvdLHGlsrrararRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 KDNSE-----FFEGVDMNLVDWLRQYAPEDEQTETFLRGFLGRMLFSgEEVKKKASVLSGGEKVRCMLSKMMLSSANVLL 463
Cdd:TIGR03873 82 QDSDTavpltVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 464 LDEPTNHLD----LESITAVNDgLASFKGSIIFTSYDFEFINTIANRVIDLnqSGG 515
Cdd:TIGR03873 161 LDEPTNHLDvraqLETLALVRE-LAATGVTVVAALHDLNLAASYCDHVVVL--DGG 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.71e-09 |
|
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: 57.54 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGeidsqtghvsmgkderlavlkqdHFAYEeerv 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-----------------------HPKYE---- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvVIKGHERLyevmKEKDEIYMKPDFSDEDGI-----RAAELEGefaemngwnaeADAASLLSGLGISADLHDKQMSEl 156
Cdd:cd03217 54 ---VTEGEILF----KGEDITDLPPEERARLGIflafqYPPEIPG-----------VKNADFLRYVNEGFSGGEKKRNE- 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 157 ennqkvkvlLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDF---LINFDNTVIVVSHDRHFLNNV 218
Cdd:cd03217 115 ---------ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-495 |
2.06e-09 |
|
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: 57.54 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEM--EPDEG--TFKWGVTTSLSyfPKDNSEff 395
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGeiLFKGEDITDLP--PEERAR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 EGVDMNLvdwlrQYAPEDE--QTETFLR----GFlgrmlfsgeevkkkasvlSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:cd03217 77 LGIFLAF-----QYPPEIPgvKNADFLRyvneGF------------------SGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|
gi 499595078 470 HLDLESITAVNDGLASF----KGSIIFTSY 495
Cdd:cd03217 134 GLDIDALRLVAEVINKLreegKSVLIITHY 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-210 |
2.12e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.79 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRF-GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG----KDERLAVLkQDHFAYeeer 80
Cdd:COG1132 344 NVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLESL-RRQIGV---- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VL-DVVikgherLYEvmkekDEI-----YMKPDFSDEDGIRAAELEG--EFAEM--NGWNAE-ADAASLLSGlGisadlh 149
Cdd:COG1132 419 VPqDTF------LFS-----GTIrenirYGRPDATDEEVEEAAKAAQahEFIEAlpDGYDTVvGERGVNLSG-G------ 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 150 dkqmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDipAISwleDFLI--NFDN-----TVIVVSH 210
Cdd:COG1132 481 ----------QRQRIAIARALLKDPPILILDEATSALD--TET---EALIqeALERlmkgrTTIVIAH 533
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
2.43e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 32 LIGANGAGKSTFLKILSGEIDSQTGHVSMgkderlavLKQDHFAYEEERvldvviKGHERLYEVMKEKDEIYMKPDFSDE 111
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSL--------VGQPLHQMDEEA------RAKLRAKHVGFVFQSFMLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 112 DGIR-AAELEGEfaemNGWNAEADAASLLSGLGISADLHDKQmSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA 190
Cdd:PRK10584 107 ENVElPALLRGE----SSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*
gi 499595078 191 ISWLEDFLI----NFDNTVIVVSHD 211
Cdd:PRK10584 182 GDKIADLLFslnrEHGTTLILVTHD 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
2.70e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVsmgkderlavlkqdHFAYEEER 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------------HYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHERLYEVMK-EKDEIYMKPdfsdEDGIR----AAELEGEFAEMNGW----NAEADAASLLSGLGISADLHDK 151
Cdd:PRK11701 72 LRDLYALSEAERRRLLRtEWGFVHQHP----RDGLRmqvsAGGNIGERLMAVGArhygDIRATAGDWLERVEIDAARIDD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFL----INFDNTVIVVSHD 211
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrglvRELGLAVVIVTHD 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-230 |
2.86e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 12 GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGhvsmgkderlavlkqdhfayeeervlDVVIKGH-- 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSG--------------------------SVLIRGEpi 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 90 --ERLYEVMKEKDEIYMKPDfsdeDGIRAAELEGE--FAEMN-GWNAEADA---ASLLSGLGISaDLHDKQMSELENNQK 161
Cdd:PRK13652 69 tkENIREVRKFVGLVFQNPD----DQIFSPTVEQDiaFGPINlGLDEETVAhrvSSALHMLGLE-ELRDRVPHHLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
2.94e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDERL-AVLKQDHFAyee 78
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDpDVAEACHYL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ervldvvikGHerlyevmkeKDeiYMKPDFSDEDGIraaelegEF-AEMNGwNAEADAASLLSGLGIsADLHDKQMSELE 157
Cdd:PRK13539 79 ---------GH---------RN--AMKPALTVAENL-------EFwAAFLG-GEELDIAAALEAVGL-APLAHLPFGYLS 129
|
170 180 190
....*....|....*....|....*....|....*
gi 499595078 158 NNQKVKVLLAQSL-FGEPdVLLLDEPTNGLDIPAI 191
Cdd:PRK13539 130 AGQKRRVALARLLvSNRP-IWILDEPTAALDAAAV 163
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-512 |
3.07e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG--EIDSQTGHVSMGKDErlavLKQDHFAyEE 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSP----LKASNIR-DT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ERVLDVVIKGHERLYEVMKEKDEIYMKPDFSDEDGIRAaelegeFAEMNgwnaeADAASLLSGLGISADLHDKQMSELEN 158
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMA------YNAMY-----LRAKNLLRELQLDADNVTRPVGDYGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHIADLDFGKiklYVG 235
Cdd:TIGR02633 145 GQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQ---HVA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 236 NYDFWYQSSQ--LAQKMAQEQNKKKEEKIKELQDFIARFSANASKSKQATSRKKqlekieLDDIQPSSRRypyvkftper 313
Cdd:TIGR02633 222 TKDMSTMSEDdiITMMVGREITSLYPHEPHEIGDVILEARNLTCWDVINPHRKR------VDDVSFSLRR---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 314 eigNDLLTVQGLSKTidGEKVLDNISFTMNPN--DKAILIGDSEIA-KTTLLKILAGEMEPDEGTFKWGVTTSLsyfpkd 390
Cdd:TIGR02633 286 ---GEILGVAGLVGA--GRTELVQALFGAYPGkfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKRHGIVPIL------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 nseffeGVDMNL-VDWLRQYAPE---DEQTEtflrgfLGRMLFSGEEVKKKASV-------LSGGEKVRCMLSKMMLSSA 459
Cdd:TIGR02633 355 ------GVGKNItLSVLKSFCFKmriDAAAE------LQIIGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNP 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 460 NVLLLDEPTNHLDLES---ITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-512 |
3.97e-09 |
|
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: 56.77 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFFEGVD 399
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-----------------IIDGLK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 MNL----VDWLRQYA-----------------------------PEDEQTETFLRgFLGRMLFSgEEVKKKASVLSGGEK 446
Cdd:cd03262 64 LTDdkknINELRQKVgmvfqqfnlfphltvlenitlapikvkgmSKAEAEERALE-LLEKVGLA-DKADAYPAQLSGGQQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 447 VRCMLSKMMLSSANVLLLDEPTNHLDLESITAVND---GLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDvmkDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
424-510 |
4.46e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 424 LGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDFEFINTI 503
Cdd:PLN03073 328 LAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
....*..
gi 499595078 504 ANRVIDL 510
Cdd:PLN03073 408 VTDILHL 414
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
4.76e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG--------KDERLavLKQDH 73
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGtaplaearEDTRL--MFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 74 FAYEEERVLDVV---IKGHERlyevmkekdeiymkpdfsdEDGIRAAELEGEFAEMNGWNAEadaaslLSGlgisadlhd 150
Cdd:PRK11247 91 RLLPWKKVIDNVglgLKGQWR-------------------DAALQALAAVGLADRANEWPAA------LSG--------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 151 kqmselenNQKVKVLLAQSLFGEPDVLLLDEPTNGLDipAISWLE-DFLI-------NFdnTVIVVSHD 211
Cdd:PRK11247 137 --------GQKQRVALARALIHRPGLLLLDEPLGALD--ALTRIEmQDLIeslwqqhGF--TVLLVTHD 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-230 |
5.22e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.94 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 15 KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKderlaVLKQDHFAYEEERVLDVV--IKGHERL 92
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD-----IYIGDKKNNHELITNPYSkkIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 93 ------------YEVMK---EKDeIYMKPDFSDEDGIRAAELegefaemngwnaeadAASLLSGLGISADLHDKQMSELE 157
Cdd:PRK13631 115 rrrvsmvfqfpeYQLFKdtiEKD-IMFGPVALGVKKSEAKKL---------------AKFYLNKMGLDDSYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 158 NNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-512 |
5.64e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 318 DLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSeffeg 397
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 VDMNL---VDWLRQYAPEDEQTEtfLRGFLGRMLfSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLE 474
Cdd:PRK09544 78 LDTTLpltVNRFLRLRPGTKKED--ILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499595078 475 SITAVNDGLASFKG----SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:PRK09544 155 GQVALYDLIDQLRReldcAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
7.68e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.92 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLF--EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSmgkderlavlkqdhfayee 78
Cdd:PRK13632 7 MIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ervLDVVIKGHERLYEVMKEKDEIYMKPD-----FSDEDGIrAAELEGEFAEMNGWNAEADAASLLSGLGisaDLHDKQM 153
Cdd:PRK13632 68 ---IDGITISKENLKEIRKKIGIIFQNPDnqfigATVEDDI-AFGLENKKVPPKKMKDIIDDLAKKVGME---DYLDKEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF----DNTVIVVSHD 211
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
331-510 |
7.72e-09 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 55.88 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 331 GEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTS------LSYFPKD------------N 391
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVSdlrgraIPYLRRKigvvfqdfrllpD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 392 SEFFEGVDMNLVdwLRQYAPEDEQTEtfLRGFLGRMLFSGEEvKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHL 471
Cdd:cd03292 93 RNVYENVAFALE--VTGVPPREIRKR--VPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499595078 472 DLESITAVNDGLASFK---GSIIFTSYDFEFINTIANRVIDL 510
Cdd:cd03292 168 DPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIAL 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-211 |
9.66e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKD--------------ERL 66
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvrKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 AVLKQDHFAYEEERVLDVV---IKGHERLYEVMKeKDEIYMKpdfsdedgIRAAELEGefaemngwnaeadAASLLSglg 143
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVaypLREHTQLPAPLL-HSTVMMK--------LEAVGLRG-------------AAKLMP--- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 144 isadlhdkqmSELENNQKVKVLLAQSLFGEPDVLLLDEP-------TNGLDIPAISWLEDFLinfDNTVIVVSHD 211
Cdd:PRK11831 142 ----------SELSGGMARRAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSAL---GVTCVVVSHD 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-211 |
1.05e-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: 56.26 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 24 FTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGhvsmgkDERLAVlkqDHFAYEEErvldvvikgherlyevmkekdeiY 103
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG------DIEIEL---DTVSYKPQ-----------------------Y 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 104 MKPDFsdEDGIRA--AELEGEFAEMNGWNAEadaasLLSGLGISaDLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDE 181
Cdd:cd03237 70 IKADY--EGTVRDllSSITKDFYTHPYFKTE-----IAKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190
....*....|....*....|....*....|....
gi 499595078 182 PTNGLD----IPAISWLEDFLINFDNTVIVVSHD 211
Cdd:cd03237 142 PSAYLDveqrLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
319-512 |
1.17e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSkTIDGEKVL-DNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTSlsyfpKDNSEFFE 396
Cdd:PRK13538 1 MLEARNLA-CERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-----RQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 397 ---------GVDMNLVDW--LRQYAP-----EDEQTETFLR--GFLGRmlfsgEEVkkKASVLSGGEKVRCMLSKMMLSS 458
Cdd:PRK13538 75 dllylghqpGIKTELTALenLRFYQRlhgpgDDEALWEALAqvGLAGF-----EDV--PVRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 459 ANVLLLDEPTNHLD---LESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:PRK13538 148 APLWILDEPFTAIDkqgVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
331-524 |
1.24e-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: 57.04 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 331 GEKVLDnISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF----------KWGVTTS-----LSYFPKDNSEFF 395
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsRKGIFLPpekrrIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 E-GVDMNLVDWLRQYAPEDEQTeTFLRgfLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD-- 472
Cdd:TIGR02142 89 HlSVRGNLRYGMKRARPSERRI-SFER--VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 473 --------LESITavndglASFKGSIIFTSYDFEFINTIANRVIDLNQsGGLSKEVPYEE 524
Cdd:TIGR02142 166 rkyeilpyLERLH------AEFGIPILYVSHSLQEVLRLADRVVVLED-GRVAAAGPIAE 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-229 |
1.28e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.17 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRK-----LFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKderlavlkqdHFAY 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------SIAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 77 -------EEERVLDVVIKG----HERLYEVmkekdeiymkpdfsdedgIRAAELEGEFAEM----------NGWNaeada 135
Cdd:cd03250 71 vsqepwiQNGTIRENILFGkpfdEERYEKV------------------IKACALEPDLEILpdgdlteigeKGIN----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 136 aslLSGlGisadlhdkqmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLIN----FDNTVIVVSHD 211
Cdd:cd03250 128 ---LSG-G----------------QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILglllNNKTRILVTHQ 187
|
250
....*....|....*...
gi 499595078 212 RHFLNNvCTHIADLDFGK 229
Cdd:cd03250 188 LQLLPH-ADQIVVLDNGR 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-187 |
1.29e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 14 RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVsmgkderlavLKQDHFAY--EEERVLDVVIKGHER 91
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------WAERSIAYvpQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 92 LYEvmkEKDEIYMkpdfsdEDGIRAAELEgefaemngwnaeADAASLLSGLgiSADLHDKQMSeLENNQKVKVLLAQSLF 171
Cdd:PTZ00243 743 FFD---EEDAARL------ADAVRVSQLE------------ADLAQLGGGL--ETEIGEKGVN-LSGGQKARVSLARAVY 798
|
170
....*....|....*.
gi 499595078 172 GEPDVLLLDEPTNGLD 187
Cdd:PTZ00243 799 ANRDVYLLDDPLSALD 814
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
1.46e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGeIDSQT-GHVSM-GKD-ERLavlkqdhfaYEE 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQTsGHIRFhGTDvSRL---------HAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ERVLDVVIKgHERLYEVMKEKDEIYMkpdfsdedGIR---------AAELEgefaemngwnaeADAASLLSGLGISaDLH 149
Cdd:PRK10851 73 DRKVGFVFQ-HYALFRHMTVFDNIAF--------GLTvlprrerpnAAAIK------------AKVTQLLEMVQLA-HLA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 150 DKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA----ISWLEDFLINFDNTVIVVSHDR 212
Cdd:PRK10851 131 DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-210 |
1.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.82 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 13 DRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM------GKDERLAVLKQDH---FAYEEERVLD 83
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDIRKKVglvFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 84 VVIK-----GHERLYEvmkEKDEIYMKpdfsdedgIRAAelegefaeMNgwnaeadaaslLSGLGISaDLHDKQMSELEN 158
Cdd:PRK13637 99 ETIEkdiafGPINLGL---SEEEIENR--------VKRA--------MN-----------IVGLDYE-DYKDKSPFELSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLD-------IPAISWLEDfliNFDNTVIVVSH 210
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSH 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
320-530 |
1.79e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW----------------GVTTS 383
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsrarharqrvGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 384 LSYFPKDNSeffegVDMNLVDWLRQYAPEDEQTETFLRGFLGrmlFSGEEVKKKASV--LSGGEKVRCMLSKMMLSSANV 461
Cdd:PRK13537 88 FDNLDPDFT-----VRENLLVFGRYFGLSAAAARALVPPLLE---FAKLENKADAKVgeLSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595078 462 LLLDEPTNHLDLESITAVNDGLASFKGS---IIFTSYDFEFINTIANRVIDLNQSGGLSKEVPYEEYLQEIG 530
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIG 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
2.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKderLAVLKQDHFAYEEerv 81
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGD---VLLGGRSIFNYRD--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 ldvVIKGHERLYEVMKEKDEIYMKPDFSDEDGIRAAEL----------EGEFAEMNGWNAEADAasllsglgisadLHDK 151
Cdd:PRK14271 96 ---VLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLvprkefrgvaQARLTEVGLWDAVKDR------------LSDS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595078 152 QMsELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN--TVIVVSHD 211
Cdd:PRK14271 161 PF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-472 |
2.07e-08 |
|
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: 57.23 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSK--TIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLL----KILAGEMEPDEGTFKWGVTT------SLSYF 387
Cdd:TIGR01271 1218 MDVQGLTAkyTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIQIDGVSWNSVTlqtwrkAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKDNSEFFEGVDMNLvDWLRQYAPED-----EQT--ETFLRGFLGRMLFSGEEvkkKASVLSGGEKVRCMLSKMMLSSAN 460
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNL-DPYEQWSDEEiwkvaEEVglKSVIEQFPDKLDFVLVD---GGYVLSNGHKQLMCLARSILSKAK 1373
|
170
....*....|..
gi 499595078 461 VLLLDEPTNHLD 472
Cdd:TIGR01271 1374 ILLLDEPSAHLD 1385
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
319-507 |
2.38e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFFEGV 398
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 ---DMNLVDWLrqyapeDEQTETFL-----RGFLGRMLFSGEEVKKKASV-----------------LSGGEKVRCMLSK 453
Cdd:PRK09700 85 iyqELSVIDEL------TVLENLYIgrhltKKVCGVNIIDWREMRVRAAMmllrvglkvdldekvanLSISHKQMLEIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 454 MMLSSANVLLLDEPTNHL---DLESITAVNDGLASFKGSIIFTSYDFEFINTIANRV 507
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-210 |
2.57e-08 |
|
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: 54.85 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGDR---KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDERLAVLKQ--DHFAY-EE 78
Cdd:cd03249 5 NVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWlrSQIGLvSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ERVL-DVVIkgherlyevmkeKDEI-YMKPDFSDEDGIRAAELEG--EFAEM--NGWNAEA-DAASLLSGlgisadlhdk 151
Cdd:cd03249 85 EPVLfDGTI------------AENIrYGKPDATDEEVEEAAKKANihDFIMSlpDGYDTLVgERGSQLSG---------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 152 qmselenNQKVKVLLAQSLFGEPDVLLLDEPTNGLDipAIS------WLEDFLINFdnTVIVVSH 210
Cdd:cd03249 143 -------GQKQRIAIARALLRNPKILLLDEATSALD--AESeklvqeALDRAMKGR--TTIVIAH 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-513 |
2.60e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 54.21 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW---GVTTS----LSYFPKDNS 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkPLDIAarnrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 393 EFfegVDMNLVDWLRQYA------PEDEQTEtfLRGFLGRMLFSGEEvKKKASVLSGGEKVRCMLSKMMLSSANVLLLDE 466
Cdd:cd03269 81 LY---PKMKVIDQLVYLAqlkglkKEEARRR--IDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499595078 467 PTNHLD---LESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQS 513
Cdd:cd03269 155 PFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
320-512 |
2.99e-08 |
|
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: 54.65 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKD-NSEF---- 394
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErNVGFvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 395 ---------FEGVDMNL-VDWLRQYAPEDEQTETfLRGFLGRMLFSGEEvKKKASVLSGGEKVRCMLSKMMLSSANVLLL 464
Cdd:cd03296 83 yalfrhmtvFDNVAFGLrVKPRSERPPEAEIRAK-VHELLKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 465 DEPTNHLDlesiTAVNDGLASFKGSI--------IFTSYDFEFINTIANRVIDLNQ 512
Cdd:cd03296 161 DEPFGALD----AKVRKELRRWLRRLhdelhvttVFVTHDQEEALEVADRVVVMNK 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
3.08e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEID-----SQTGHVSM-GKDerlaVLKQDhfa 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLdGQD----IFKMD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 yeeervldvVIKGHERLYEVMKEKDEIymkPDFSDEDGI-------RAAELEGEFAEMNGWNAEadAASLLSGLgisADL 148
Cdd:PRK14247 77 ---------VIELRRRVQMVFQIPNPI---PNLSIFENValglklnRLVKSKKELQERVRWALE--KAQLWDEV---KDR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 149 HDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF--DNTVIVVSHDRHFLNNVCTHIADLD 226
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQQAARISDYVAFLY 219
|
....
gi 499595078 227 FGKI 230
Cdd:PRK14247 220 KGQI 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-211 |
3.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 13 DRKLFEDVNIKFTEGNCYGLIGANGAGKSTF-------LKILSGEID-------SQTGHVSMGKDERLAVLKqdhFAYEE 78
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLmqhfnalLKPSSGTITiagyhitPETGNKNLKKLRKKVSLV---FQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ERvldvvikgherLYEVMKEKDEIYMKPDFSdedgirAAELEgefaemngwnAEADAASLLSGLGISADLHDKQMSELEN 158
Cdd:PRK13641 96 AQ-----------LFENTVLKDVEFGPKNFG------FSEDE----------AKEKALKWLKKVGLSEDLISKSPFELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFD---NTVIVVSHD 211
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHN 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-473 |
3.49e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.63 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYFPKDNSEFF---- 395
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 ------EGV-----------------------DMNLVDWlrqyAPEDEQTETFlrgflgrmlfsgeeVKKKASVLSGGEK 446
Cdd:PRK11231 83 qhhltpEGItvrelvaygrspwlslwgrlsaeDNARVNQ----AMEQTRINHL--------------ADRRLTDLSGGQR 144
|
170 180
....*....|....*....|....*..
gi 499595078 447 VRCMLSKMMLSSANVLLLDEPTNHLDL 473
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-63 |
3.59e-08 |
|
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: 54.22 E-value: 3.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKD 63
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGED 66
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-472 |
3.71e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.34 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF-------------KWGVTT--- 382
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaeNRHVNTvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 383 SLSYFPK----DNSEFfeGVDMnlvdwlrQYAPEDEQTETFLRGFlgRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSS 458
Cdd:PRK09452 94 SYALFPHmtvfENVAF--GLRM-------QKTPAAEITPRVMEAL--RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|....
gi 499595078 459 ANVLLLDEPTNHLD 472
Cdd:PRK09452 163 PKVLLLDESLSALD 176
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-508 |
3.91e-08 |
|
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: 54.11 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAG-----EMEPDEGT--------FKWGVTTSL-- 384
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEvlldgkdiYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 385 ----------SYFPK---DNseffegvdMNLVDWLRQYAPEDEQTETFLRGFLGRMLFsgEEVKKKASV--LSGGEKVRC 449
Cdd:cd03260 81 rrvgmvfqkpNPFPGsiyDN--------VAYGLRLHGIKLKEELDERVEEALRKAALW--DEVKDRLHAlgLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595078 450 MLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG--SIIFTSYDFEFINTIANRVI 508
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADRTA 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-186 |
4.22e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 53.98 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------------- 63
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDitglppheraragigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 64 -------------ERLAV----LKQDHFAYEEERVLDVVikghERLYEVMKEKdeiymkpdfsdedgiraaelegefaem 126
Cdd:cd03224 81 pegrrifpeltveENLLLgayaRRRAKRKARLERVYELF----PRLKERRKQL--------------------------- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 127 ngwnaeadaASLLSGlGisadlhDKQMselennqkvkVLLAQSLFGEPDVLLLDEPTNGL 186
Cdd:cd03224 130 ---------AGTLSG-G------EQQM----------LAIARALMSRPKLLLLDEPSEGL 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-211 |
4.71e-08 |
|
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: 54.29 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 26 EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSmGKDERLAVLK-------QDHFAYEEERVLDVVIKGHE-------- 90
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDefrgselQNYFTKLLEGDVKVIVKPQYvdlipkav 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 91 --RLYEVMKEKDEIYMKpdfsdEDGIRAAELEGefaemngwnaeadaasllsglgisadLHDKQMSELENNQKVKVLLAQ 168
Cdd:cd03236 104 kgKVGELLKKKDERGKL-----DELVDQLELRH--------------------------VLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499595078 169 SLFGEPDVLLLDEPTNGLDI-----PAISWLEdfLINFDNTVIVVSHD 211
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIkqrlnAARLIRE--LAEDDNYVLVVEHD 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
319-487 |
4.72e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.01 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKIL--AGEMEPDegtfkwgVTTSLS--------YFP 388
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPE-------VTITGSivynghniYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 389 K-DNSEFFEGVDM--------------NLVDWLR-----QYAPEDEQTETFLRGflgrmLFSGEEVKKK----ASVLSGG 444
Cdd:PRK14239 78 RtDTVDLRKEIGMvfqqpnpfpmsiyeNVVYGLRlkgikDKQVLDEAVEKSLKG-----ASIWDEVKDRlhdsALGLSGG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499595078 445 EKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFK 487
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
305-472 |
5.00e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 305 PYVKFTPEREIGNDLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF-------- 376
Cdd:PRK13536 27 SEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 377 --------KWGVttsLSYFPKDNSEFfeGVDMNLVDWLRQYAPEDEQTETFLRGFLGrmlFSGEEVKKKASV--LSGGEK 446
Cdd:PRK13536 107 ararlaraRIGV---VPQFDNLDLEF--TVRENLLVFGRYFGMSTREIEAVIPSLLE---FARLESKADARVsdLSGGMK 178
|
170 180
....*....|....*....|....*.
gi 499595078 447 VRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-188 |
5.43e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTdVSLRFGDRKLfEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAY---EEE 79
Cdd:PRK15056 11 DVT-VTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpqSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 -------RVLDVVIKG---HERLYEVMKEKDEiymkpdfsdedgiraaelegefaemngwnAEADAAslLSGLGISaDLH 149
Cdd:PRK15056 89 vdwsfpvLVEDVVMMGrygHMGWLRRAKKRDR-----------------------------QIVTAA--LARVDMV-EFR 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 499595078 150 DKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDI 188
Cdd:PRK15056 137 HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
319-375 |
7.26e-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: 53.44 E-value: 7.26e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT 375
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE 61
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-186 |
8.43e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDerlavLKQDHFAYEEE 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdGKD-----ITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGhERLYEVMKEKDEIYMKPDFSDEDGI--RAAELEGEFAEMngWNAEADAASLLSGlgisadlHDKQMsele 157
Cdd:PRK11614 80 EAVAIVPEG-RRVFSRMTVEENLAMGGFFAERDQFqeRIKWVYELFPRL--HERRIQRAGTMSG-------GEQQM---- 145
|
170 180
....*....|....*....|....*....
gi 499595078 158 nnqkvkVLLAQSLFGEPDVLLLDEPTNGL 186
Cdd:PRK11614 146 ------LAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
319-511 |
8.72e-08 |
|
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: 53.21 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKT-----IDGEK--VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGtfkwgvttSLSYfpkdN 391
Cdd:COG4778 4 LLEVENLSKTftlhlQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG--------SILV----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 392 SEFfEGVDmnLVDwlrqyAPEDE-----QTE-----TFLRGF------------LGRMLFSGEEVKKKASVL-------- 441
Cdd:COG4778 72 HDG-GWVD--LAQ-----ASPREilalrRRTigyvsQFLRVIprvsaldvvaepLLERGVDREEARARARELlarlnlpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 442 ----------SGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG---SIIFTSYDFEFINTIANRVI 508
Cdd:COG4778 144 rlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKArgtAIIGIFHDEEVREAVADRVV 223
|
...
gi 499595078 509 DLN 511
Cdd:COG4778 224 DVT 226
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
320-495 |
9.60e-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: 53.03 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAG-------------------EMEPDEGTFKwGV 380
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyevtsgtilfkgqdllELEPDERARA-GL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 381 TTSLSY---FPKDNSEFFEGVDMNLVdwlRQYAPEDE----QTETFLRGFLGRMLFSGEEVKKKASV-LSGGEKVRCMLS 452
Cdd:TIGR01978 80 FLAFQYpeeIPGVSNLEFLRSALNAR---RSARGEEPldllDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEIL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499595078 453 KMMLSSANVLLLDEPTNHLDLESITAVNDGLASFK----GSIIFTSY 495
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRepdrSFLIITHY 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
333-530 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.51 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 333 KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFK------WGVTTSLSYFPK---------DNSEFFEG 397
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdiTDKKVKLSDIRKkvglvfqypEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 VDMNLVDWLRQYAPEDEQTETFLRGFLGRMLFSGEEVKKKASV-LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD---- 472
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgr 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 473 ---LESITAVNDglaSFKGSIIFTSYDFEFINTIANRVIDLNQSG----GLSKEVPYE-EYLQEIG 530
Cdd:PRK13637 181 deiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVMNKGKcelqGTPREVFKEvETLESIG 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-211 |
1.33e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.34 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 15 KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILsGEIDSQTG--------HVSMGKDERLAVLKQDHFAYEEERvldvvi 86
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTSgtyrvagqDVATLDADALAQLRREHFGFIFQR------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 87 kgherlYEVMkekdeiymkPDFSDEDGIraaELEGEFAEMNGWNAEADAASLLSGLGIsADLHDKQMSELENNQKVKVLL 166
Cdd:PRK10535 95 ------YHLL---------SHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499595078 167 AQSLFGEPDVLLLDEPTNGLD------IPAIswLEDfLINFDNTVIVVSHD 211
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDshsgeeVMAI--LHQ-LRDRGHTVIIVTHD 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-229 |
1.40e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG-EIDSQTGHVSMGKDERLAVLKQdhfayeee 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDGVDLSHVPPYQ-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGHERLYEVMKEKDEIY-MKpdfsdEDGIRAAELEGEFAEMngwnaeadaasllSGLGISADLHDKQMSELEN 158
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFgLK-----QDKLPKAEIASRVNEM-------------LGLVHMQEFAKRKPHQLSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLE----DFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGK 229
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
330-512 |
1.44e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 52.36 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVttSLSYFPKDNSEFFE---GV------- 398
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQ--DLSRLKRREIPYLRrriGVvfqdfrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 --DMN------LVdwLR-QYAPEDE---QTETFLR--GFLGRMlfsgeevKKKASVLSGGEKVRCMLSKMMLSSANVLLL 464
Cdd:COG2884 91 lpDRTvyenvaLP--LRvTGKSRKEirrRVREVLDlvGLSDKA-------KALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499595078 465 DEPTNHLDLESITAVNDGLASF--KG-SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLELED 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
313-475 |
1.60e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.04 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 313 REIGNDLLTVQGLS-KTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAG---------EMEPDE--------- 373
Cdd:COG4178 356 ETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgriARPAGArvlflpqrp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 374 ----GTFKwgvtTSLSYfPKDNSEFfegvdmnlvdwlrqyapEDEQTETFLR-----GFLGRMlfsgEEVKKKASVLSGG 444
Cdd:COG4178 436 ylplGTLR----EALLY-PATAEAF-----------------SDAELREALEavglgHLAERL----DEEADWDQVLSLG 489
|
170 180 190
....*....|....*....|....*....|.
gi 499595078 445 EKVRCMLSKMMLSSANVLLLDEPTNHLDLES 475
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-515 |
1.83e-07 |
|
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: 51.00 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLS-KTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAG---------EMEPDEGTF----KwgvttslS 385
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgsgriGMPEGEDLLflpqR-------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 386 YFPKDNseffegvdmnlvdwLRQ---YAPEDeqtetflrgflgrmlfsgeevkkkasVLSGGEKVRCMLSKMMLSSANVL 462
Cdd:cd03223 74 YLPLGT--------------LREqliYPWDD--------------------------VLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499595078 463 LLDEPTNHLDLESITAVNDGLASFKGSIIFTSYDfEFINTIANRVIDLNQSGG 515
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELGITVISVGHR-PSLWKFHDRVLDLDGEGG 165
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
330-483 |
2.11e-07 |
|
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: 53.57 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFFEGV---DMNLVDWL 406
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-----------------LLDGHdlaDYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 407 RQYA------------------------PEDEQTETFLRG-----FLGRM-LFSGEEVKKKASVLSGGEKVRCMLSKMML 456
Cdd:TIGR02203 406 RQVAlvsqdvvlfndtianniaygrteqADRAEIERALAAayaqdFVDKLpLGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180
....*....|....*....|....*..
gi 499595078 457 SSANVLLLDEPTNHLDLESITAVNDGL 483
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAAL 512
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-63 |
2.29e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.40 E-value: 2.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 1 MLQVTDVSLRFG-----DRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKD 63
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILiDGKD 69
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-230 |
2.74e-07 |
|
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: 51.47 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLkqdhfAYEeeRV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PHK--RP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVVIKgHERLYEVMKEKDEI----YMKpdfsdedGIRAAELEGEFAEMNGwnaeadaaslLSGLGisaDLHDKQMSELE 157
Cdd:cd03300 74 VNTVFQ-NYALFPHLTVFENIafglRLK-------KLPKAEIKERVAEALD----------LVQLE---GYANRKPSQLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 158 NNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN----TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
320-467 |
2.76e-07 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 51.89 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTS---------LSYF 387
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdITHLpmherarlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKDNSEFFE-GVDMNL--VDWLRQYAPEDEQ---TETFLRGF-LGRMLfsgeevKKKASVLSGGEKVRCMLSKMMLSSAN 460
Cdd:TIGR04406 82 PQEASIFRKlTVEENImaVLEIRKDLDRAEReerLEALLEEFqISHLR------DNKAMSLSGGERRRVEIARALATNPK 155
|
....*..
gi 499595078 461 VLLLDEP 467
Cdd:TIGR04406 156 FILLDEP 162
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-230 |
2.88e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKIL-------SGEIDSQTGHVSMGK---DERLAVLKQ 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKtpsDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 72 D------------HFAyeeerVLDVVIKGHERLYEVMKEKdeiymkpdfsdedgiraaelegefaemngwnAEADAASLL 139
Cdd:PRK11124 83 NvgmvfqqynlwpHLT-----VQQNLIEAPCRVLGLSKDQ-------------------------------ALARAEKLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 140 SGLGIsADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD--IPA-----ISWLEDFLInfdnTVIVVSHDR 212
Cdd:PRK11124 127 ERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeITAqivsiIRELAETGI----TQVIVTHEV 201
|
250
....*....|....*...
gi 499595078 213 HFLNNVCTHIADLDFGKI 230
Cdd:PRK11124 202 EVARKTASRVVYMENGHI 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-491 |
2.99e-07 |
|
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: 51.46 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 331 GEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEG------------TFKWgVTTSLSYFPKDnSEFFEGV 398
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdiSRKS-LRSMIGVVLQD-TFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 DMNLVDWLRQYAPEDE----QTETFLRGFLgRMLFSG--EEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:cd03254 93 IMENIRLGRPNATDEEvieaAKEAGAHDFI-MKLPNGydTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180
....*....|....*....|..
gi 499595078 473 LESITAVNDGLAS-FKG--SII 491
Cdd:cd03254 172 TETEKLIQEALEKlMKGrtSII 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-198 |
3.29e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAvlKQDhfayeEER 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW-QGEPIR--RQR-----DEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHerlyevmkeKDEIymKPDFSDEDGIRAaelegeFAEMNGWNAEADAASLLSGLGIS--ADLHDKQMSElen 158
Cdd:PRK13538 73 HQDLLYLGH---------QPGI--KTELTALENLRF------YQRLHGPGDDEALWEALAQVGLAgfEDVPVRQLSA--- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFL 198
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-528 |
3.41e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILS---------GEI--DSQTGHVSMGKD-ER--L 66
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphgtyeGEIifEGEELQASNIRDtERagI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 AVLKQDHFAYEEERVLDVVIKGHErlyevmkekdeiymkpdfsdedgiraaelEGEFAEMNgWNA-EADAASLLSGLGIS 145
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNE-----------------------------ITPGGIMD-YDAmYLRAQKLLAQLKLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 146 ADLHDKQMsELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDrhfLNNV---C 219
Cdd:PRK13549 135 INPATPVG-NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHK---LNEVkaiS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 220 THIADLDFGKiklYVGNYDfwyqssqlAQKMAQEqnkkkeekikelqDFIArfsanaskskQATSRkkqlekiELddiqp 299
Cdd:PRK13549 211 DTICVIRDGR---HIGTRP--------AAGMTED-------------DIIT----------MMVGR-------EL----- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 300 sSRRYPYVkftpEREIGNDLLTVQGLS---KTIDGEKVLDNISFTMNPND---KAILIGDseiAKTTLLKILAGemepde 373
Cdd:PRK13549 245 -TALYPRE----PHTIGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEilgIAGLVGA---GRTELVQCLFG------ 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 374 gtfkwgvttslSYFPKDNSEFF-EG--VDM-NLVDWLRQ---YAPEDEQ--------------TETFLRGFLGRMLFS-- 430
Cdd:PRK13549 311 -----------AYPGRWEGEIFiDGkpVKIrNPQQAIAQgiaMVPEDRKrdgivpvmgvgkniTLAALDRFTGGSRIDda 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 431 ------GEEVK----KKASV------LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDL----ESITAVNDgLASFKGSI 490
Cdd:PRK13549 380 aelktiLESIQrlkvKTASPelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQ-LVQQGVAI 458
|
570 580 590
....*....|....*....|....*....|....*...
gi 499595078 491 IFTSYDFEFINTIANRVIDLNQsGGLSKEVPYEEYLQE 528
Cdd:PRK13549 459 IVISSELPEVLGLSDRVLVMHE-GKLKGDLINHNLTQE 495
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
3.90e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.58 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG---EIDSQ--TGHVSM------GKDERLAVLK 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGArvEGEILLdgediyDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 71 Q-----------------DHFAYeeervldvvikGHeRLYEVM--KEKDEIYmkpdfsdEDGIRAAELegefaemngWNA 131
Cdd:COG1117 92 RrvgmvfqkpnpfpksiyDNVAY-----------GL-RLHGIKskSELDEIV-------EESLRKAAL---------WDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 132 EAD----AASLLSGlGisadlhdkqmselennQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF--DNTV 205
Cdd:COG1117 144 VKDrlkkSALGLSG-G----------------QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELkkDYTI 206
|
....*
gi 499595078 206 IVVSH 210
Cdd:COG1117 207 VIVTH 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
319-375 |
4.02e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 4.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT 375
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE 62
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-187 |
4.41e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.24 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKD-------ERlAVLKQDH 73
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaER-GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 74 FAYEEERVLDVVIKGHErLYEVMKEKdeiymkpdfsdedgiraaelegefaemngwnAEADAASLLSGLGIsADLHDKQM 153
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQ-LAGVEKMQ-------------------------------RLEIAHQMLKKVGL-EGAEKRYI 126
|
170 180 190
....*....|....*....|....*....|....
gi 499595078 154 SELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK11248 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
337-512 |
4.51e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.91 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 337 NISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG---VTTSLSY-------FpKDNSEF-----FEGVDMN 401
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdLTALPPAerpvsmlF-QENNLFphltvAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 402 LVDWLRQYAPEDEQTETFLR-----GFLGRmlfsgeevkkKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD---- 472
Cdd:COG3840 96 LRPGLKLTAEQRAQVEQALErvglaGLLDR----------LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499595078 473 LESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
5.03e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILS-----GEIDSQTGHVSM-GKDerlaVLKQDHFA 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLfGRN----IYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YEEERVLDVVIK-----GHERLYE----------VMKEKDEIymkpDFSDEDGIRAAELegefaemngWNAEADAaslls 140
Cdd:PRK14267 81 IEVRREVGMVFQypnpfPHLTIYDnvaigvklngLVKSKKEL----DERVEWALKKAAL---------WDEVKDR----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 141 glgisadLHDKQmSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF--DNTVIVVSHDRHFLNNV 218
Cdd:PRK14267 143 -------LNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARV 214
|
250
....*....|..
gi 499595078 219 CTHIADLDFGKI 230
Cdd:PRK14267 215 SDYVAFLYLGKL 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-533 |
5.21e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.16 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvTTSLSYFPK--------- 389
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ-GKPLDYSKRgllalrqqv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 390 -------DNSEFFEGVDMNLVDWLRQYA-PEDEQTETFLRGFlgrMLFSGEEVKKKA-SVLSGGEKVRCMLSKMMLSSAN 460
Cdd:PRK13638 80 atvfqdpEQQIFYTDIDSDIAFSLRNLGvPEAEITRRVDEAL---TLVDAQHFRHQPiQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 461 VLLLDEPTNHLD---LESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSGGLSKEVPYE-----EYLQEIGVL 532
Cdd:PRK13638 157 YLLLDEPTAGLDpagRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEvfactEAMEQAGLT 236
|
.
gi 499595078 533 Q 533
Cdd:PRK13638 237 Q 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-508 |
5.73e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 49.74 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 316 GNDLLTVQGLSktidGEKVLDNISFTmnpndkailIGDSEIA---------KTTLLKILAGEMEPDEGTFkwgvttslsy 386
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFE---------VRAGEIVgiaglvgngQTELAEALFGLRPPASGEI---------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 387 fpkdnseFFEGVDMNLV---DWLRQ---YAPEDEQTEtflrgflGrmLFSGEEVKKKASV---LSGG--EKVrcMLSKMM 455
Cdd:cd03215 58 -------TLDGKPVTRRsprDAIRAgiaYVPEDRKRE-------G--LVLDLSVAENIALsslLSGGnqQKV--VLARWL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 456 LSSANVLLLDEPTNHLDLESITAVNDGLASFK---GSIIFTSYDFEFINTIANRVI 508
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRIL 175
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-210 |
5.83e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 9 LRF-GDRKLFEDV----NIKFT--EGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERlavlkqdHFAYEEERV 81
Cdd:PRK11288 5 LSFdGIGKTFPGVkaldDISFDcrAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-------RFASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 82 LDVVIKGHERLYEVmkekdeiymkPDFSDEDGIRAAELEGEFAEMNGWNAEADAASLLSGLGISADlHDKQMSELENNQK 161
Cdd:PRK11288 78 AAGVAIIYQELHLV----------PEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDID-PDTPLKYLSIGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499595078 162 VKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLedF-LIN---FDNTVIV-VSH 210
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSAREIEQL--FrVIRelrAEGRVILyVSH 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-230 |
6.00e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 49.74 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRfgdrKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDerlavlkqdhfaYEEE 79
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKP------------VTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGherlyevmkekdeIYMKPdfsdEDgiRAAEleGEFAEMN-GWNAEAdaASLLSGlGisadlhdkqmselen 158
Cdd:cd03215 68 SPRDAIRAG-------------IAYVP----ED--RKRE--GLVLDLSvAENIAL--SSLLSG-G--------------- 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 159 NQKvKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03215 109 NQQ-KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADagkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-230 |
6.08e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.84 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLF---------EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLK- 70
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 71 QDHFAYEeeRVLDVVIKgherlyevmkekDEI-YMKPDFSdedgIRA--AELEGEFAEMNGWNAEADAASLLSGLGISAD 147
Cdd:PRK10419 82 AQRKAFR--RDIQMVFQ------------DSIsAVNPRKT----VREiiREPLRHLLSLDKAERLARASEMLRAVDLDDS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 148 LHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDI----PAISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIA 223
Cdd:PRK10419 144 VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM 223
|
....*..
gi 499595078 224 DLDFGKI 230
Cdd:PRK10419 224 VMDNGQI 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-192 |
7.15e-07 |
|
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: 50.23 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKST-------FLKILSGEI---DSQTGHVSMGKDERLAV--L 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTtfymivgLVKPDSGKIlldGQDITKLPMHKRARLGIgyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 70 KQDHFAYeeeRVLDVvikgherlyevmkekdeiymkpdfsdEDGIRAAElegEFAEMNGWNAEADAASLLSGLGISAdLH 149
Cdd:cd03218 81 PQEASIF---RKLTV--------------------------EENILAVL---EIRGLSKKEREEKLEELLEEFHITH-LR 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499595078 150 DKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAIS 192
Cdd:cd03218 128 KSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
330-475 |
7.19e-07 |
|
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: 50.56 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGemepdegtfkwgvttslSYFPKDNSEFFEGVDMNLVD--WLR 407
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR-----------------FYVPENGRVLVDGHDLALADpaWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 408 QYAPEDEQTETFLRG------FLGRMLFSGEEVKKKASV------------------------LSGGEKVRCMLSKMMLS 457
Cdd:cd03252 76 RQVGVVLQENVLFNRsirdniALADPGMSMERVIEAAKLagahdfiselpegydtivgeqgagLSGGQRQRIAIARALIH 155
|
170
....*....|....*...
gi 499595078 458 SANVLLLDEPTNHLDLES 475
Cdd:cd03252 156 NPRILIFDEATSALDYES 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-230 |
7.60e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 13 DRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDerlaVLKQDHFAYEEErvldVVIKGHER 91
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVP----LVQYDHHYLHRQ----VALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 92 LYEVMKEKDEIYMKPDFSDEDGIRAAElegefaemngwnAEADAASLLSGL--GISADLHDKQmSELENNQKVKVLLAQS 169
Cdd:TIGR00958 565 VLFSGSVRENIAYGLTDTPDEEIMAAA------------KAANAHDFIMEFpnGYDTEVGEKG-SQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595078 170 LFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDNTVIVVSHDRHFLNNvCTHIADLDFGKI 230
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-230 |
9.04e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGDRKLFE-----DVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAYEEER 80
Cdd:PRK13645 11 NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHE-RLYEVMKEKDeIYMKPDFSDEDGIRAAELEGEfaemngwnaeadaasLLSGLGISADLHDKQMSELENN 159
Cdd:PRK13645 91 EIGLVFQFPEyQLFQETIEKD-IAFGPVNLGENKQEAYKKVPE---------------LLKLVQLPEDYVKRSPFELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAiswLEDFL-------INFDNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKG---EEDFInlferlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-230 |
9.15e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.56 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 3 QVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKQDHFAYEEErvl 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAFARKVA--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 83 dvvikgherlyevmkekdeiYMKPDFSDEDGIRAAELE-----------GEFAEMNgwNAEADAASLLSGLgisADLHDK 151
Cdd:PRK10575 89 --------------------YLPQQLPAAEGMTVRELVaigrypwhgalGRFGAAD--REKVEEAISLVGL---KPLAHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIP----AISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDF 227
Cdd:PRK10575 144 LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvdVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
...
gi 499595078 228 GKI 230
Cdd:PRK10575 224 GEM 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-211 |
1.26e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.12 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGD-RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVsmgkderlavlkqdhfayeeeR 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---------------------K 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKgHERLYEVMKEKDEIYMKPD---FSD---ED---GIRAAELEGEfaEMNGWNAEAdaaslLSGLGISaDLHDK 151
Cdd:PRK13647 64 VMGREVN-AENEKWVRSKVGLVFQDPDdqvFSStvwDDvafGPVNMGLDKD--EVERRVEEA-----LKAVRMW-DFRDK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 152 QMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHD 211
Cdd:PRK13647 135 PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHD 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
320-533 |
1.35e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.47 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGtfkwgvttSLSYFPKDNSEfFEGVD 399
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG--------HIRFHGTDVSR-LHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 400 MNLVDWLRQYAPEDEQTETFLRGFLGRML-----FSGEEVKKKA-----------------SVLSGGEKVRCMLSKMMLS 457
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVLprrerPNAAAIKAKVtqllemvqlahladrypAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 458 SANVLLLDEPTNHLDLESITAVNDGL----ASFKGSIIFTSYDFEFINTIANRVIDLNQSG----GLSKEVPYE------ 523
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNieqaGTPDQVWREpatrfv 233
|
250
....*....|.
gi 499595078 524 -EYLQEIGVLQ 533
Cdd:PRK10851 234 lEFMGEVNRLQ 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
317-524 |
1.45e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.58 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 317 NDLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKwgVTTSLSYFPKDNSEFFE 396
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIV--VNGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 397 GVDMNLVDWLR-------QY---------------AP-------EDEQTETFLRgFLGRMLFSGEEVKKKASVLSGGEKV 447
Cdd:PRK10619 81 VADKNQLRLLRtrltmvfQHfnlwshmtvlenvmeAPiqvlglsKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 448 RCMLSKMMLSSANVLLLDEPTNHLDLESITAV---NDGLASFKGSIIFTSYDFEFINTIANRVIDLNQsGGLSKEVPYEE 524
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVlriMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ-GKIEEEGAPEQ 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-187 |
1.51e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKIL--------------------SGE----IDSQTGHVSmg 61
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlfgrrrgSGEtiwdIKKHIGYVS-- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 62 kderlavlKQDHFAYE-EERVLDVVIKGherlyevmkekdeiymkpdFSDEDGIRAAELEGEFAEMNGWnaeadaaslLS 140
Cdd:PRK10938 343 --------SSLHLDYRvSTSVRNVILSG-------------------FFDSIGIYQAVSDRQQKLAQQW---------LD 386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499595078 141 GLGISADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK10938 387 ILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.63e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGD-RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVsmgkderlaVLKQDHFAYEEE 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV---------LIKGEPIKYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLdvvikgherlyEVMKEKDEIYMKPDfsdeDGIRAAELEGE--FAEMN-GWNAE------ADAaslLSGLGISaDLHD 150
Cdd:PRK13639 72 SLL-----------EVRKTVGIVFQNPD----DQLFAPTVEEDvaFGPLNlGLSKEevekrvKEA---LKAVGME-GFEN 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 151 KQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHD 211
Cdd:PRK13639 133 KPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
334-508 |
1.73e-06 |
|
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: 49.07 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 334 VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKwgVTTSLSYFpkdnseFFEGVDMNlvdwlrqyaPEd 413
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT--VRGRVSSL------LGLGGGFN---------PE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 414 eqtetfLRG-----FLGRML-FSGEEVKKKA-----------------SVLSGGEKVRCMLSKMMLSSANVLLLDEptnh 470
Cdd:cd03220 99 ------LTGreniyLNGRLLgLSRKEIDEKIdeiiefselgdfidlpvKTYSSGMKARLAFAIATALEPDILLIDE---- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499595078 471 ldlesITAVNDglASFK--------------GSIIFTSYDFEFINTIANRVI 508
Cdd:cd03220 169 -----VLAVGD--AAFQekcqrrlrellkqgKTVILVSHDPSSIKRLCDRAL 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-224 |
1.81e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.45 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 32 LIGANGAGKSTFLKILSGEIDSQtGHVS-MGKD------ERLAVlkqdHFAYEEERVLDV-VIKGHERLyevmkekdeiy 103
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLLPGQ-GEILlNGRPlsdwsaAELAR----HRAYLSQQQSPPfAMPVFQYL----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 104 mkpDFSDEDGIRAAELEGEFAEmngwnaeadaasLLSGLGIsADLHDKQMSELENNQKVKVLLAQSLF-----GEPD--V 176
Cdd:COG4138 91 ---ALHQPAGASSEAVEQLLAQ------------LAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499595078 177 LLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDrhfLNNVCTHiAD 224
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD---LNHTLRH-AD 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-187 |
1.81e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRK---LFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMG-----KD-------ERL 66
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDinlkwwrSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 AVLKQDHFAYEEErvldvvIKGHERlYEVMKEKDEIYMKpDFSDEDGIRA-----------AELEGEFAEMNGWNAEADA 135
Cdd:PTZ00265 463 GVVSQDPLLFSNS------IKNNIK-YSLYSLKDLEALS-NYYNEDGNDSqenknkrnscrAKCAGDLNDMSNTTDSNEL 534
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 136 ASLLSGLGISAD-----------LHD--------------KQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PTZ00265 535 IEMRKNYQTIKDsevvdvskkvlIHDfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-210 |
1.81e-06 |
|
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: 49.15 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGD--RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDER----------LAVLKQD 72
Cdd:cd03251 5 NVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRdytlaslrrqIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAYEeervlDVVikgherlyevmkeKDEI-YMKPDFSDEDGIRAAELEG--EFAEM--NGWNAE-ADAASLLSGlgisa 146
Cdd:cd03251 85 VFLFN-----DTV-------------AENIaYGRPGATREEVEEAARAANahEFIMElpEGYDTViGERGVKLSG----- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 147 dlhdkqmselenNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINF--DNTVIVVSH 210
Cdd:cd03251 142 ------------GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-375 |
2.04e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 2.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT 375
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS 60
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-528 |
2.08e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEK-VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTfkwgVTTSLSYFPKDN----SE 393
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGS----VLIRGEPITKENirevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 394 FFEGVDMNLVDWLrqYAPEDEQTETFLRGFLG--------------RMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSA 459
Cdd:PRK13652 79 FVGLVFQNPDDQI--FSPTVEQDIAFGPINLGldeetvahrvssalHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 460 NVLLLDEPTNHLDLES----ITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQSGGLSKEVPYEEYLQE 528
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
319-512 |
2.14e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPD----------------EGTFKWGVTT 382
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqrEGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 383 SLSYFPKDNSEFfegvdmNLVD------------------W---LRQYAPEDEQTETFLRGFLGRMLFSGEEVkkkaSVL 441
Cdd:PRK09984 84 SRANTGYIFQQF------NLVNrlsvlenvligalgstpfWrtcFSWFTREQKQRALQALTRVGMVHFAHQRV----STL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 442 SGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG----SIIFTSYDFEFINTIANRVIDLNQ 512
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQ 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-187 |
2.41e-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: 48.26 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 12 GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM--GKDERLAVLKQDHFAYeeervldvviKGH 89
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLngGPLDFQRDSIARGLLY----------LGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 90 ER-LYEVMKEKDEIYMKPDFSDEDGIRAAelegeFAEMNgwnaeadaaslLSGLGisadlhDKQMSELENNQKVKVLLAQ 168
Cdd:cd03231 81 APgIKTTLSVLENLRFWHADHSDEQVEEA-----LARVG-----------LNGFE------DRPVAQLSAGQQRRVALAR 138
|
170
....*....|....*....
gi 499595078 169 SLFGEPDVLLLDEPTNGLD 187
Cdd:cd03231 139 LLLSGRPLWILDEPTTALD 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-507 |
2.55e-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: 48.52 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 322 VQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTfKW-----------GVTTSLSYFPKD 390
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-ATvaghdvvreprEVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 391 NSeffegVDMNLVDWLRQY----------APEDEQTETFLRgFLGRMLFSGEEVKKkasvLSGGEKVRCMLSKMMLSSAN 460
Cdd:cd03265 82 LS-----VDDELTGWENLYiharlygvpgAERRERIDELLD-FVGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499595078 461 VLLLDEPTNHLDLESITAV----NDGLASFKGSIIFTSYDFEFINTIANRV 507
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVweyiEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
330-531 |
2.61e-06 |
|
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: 48.77 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG------VT-TSL----SYFPKDNSEFFEGV 398
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdireVTlDSLrraiGVVPQDTVLFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 DMNlVDWLRQYAPEDEQTETFLRGFLGRMLFSGEE-----VKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDL 473
Cdd:cd03253 92 GYN-IRYGRPDATDEEVIEAAKAAQIHDKIMRFPDgydtiVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595078 474 ESITAVNDGLAS-FKG-SIIFTSYDfefINTIAN--RVIDLNQsGGLSKEVPYEEYLQEIGV 531
Cdd:cd03253 171 HTEREIQAALRDvSKGrTTIVIAHR---LSTIVNadKIIVLKD-GRIVERGTHEELLAKGGL 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-187 |
2.79e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 14 RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFAYE------EERVLDVVIK 87
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-DDEDISLLPLHARARRgigylpQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 88 GHERLYEVMKEKDEIYmkpdfSDEDGIRAAELEGEFaemngwnaeaDAASLLSGLGISadlhdkqmseLENNQKVKVLLA 167
Cdd:PRK10895 95 VYDNLMAVLQIRDDLS-----AEQREDRANELMEEF----------HIEHLRDSMGQS----------LSGGERRRVEIA 149
|
170 180
....*....|....*....|
gi 499595078 168 QSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVD 169
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
334-483 |
3.02e-06 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 48.62 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 334 VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT--------------FKWGVTTSLSYFP-------KDNS 392
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlldgkpisqyehkYLHSKVSLVGQEPvlfarslQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 393 EF-FEGVDMNLVDWLRQYAPEDEQTETFLRGFlgrmlfsGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHL 471
Cdd:cd03248 109 AYgLQSCSFECVKEAAQKAHAHSFISELASGY-------DTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170
....*....|..
gi 499595078 472 DLESITAVNDGL 483
Cdd:cd03248 182 DAESEQQVQQAL 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-230 |
3.14e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.59 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILS------------GEIDSQTGHvSMGKDERL-- 66
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTAR-SLSQQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 AVLKQDHFAYE------EERVLDVVIKGHerlYEVMKEKDEiymkpdfsdedgiraaelegefaemngwNAEADAASLLS 140
Cdd:PRK11264 82 QLRQHVGFVFQnfnlfpHRTVLENIIEGP---VIVKGEPKE----------------------------EATARARELLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 141 GLGISADlHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD-------IPAISWLEDflinFDNTVIVVSHDRH 213
Cdd:PRK11264 131 KVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQ----EKRTMVIVTHEMS 205
|
250
....*....|....*..
gi 499595078 214 FLNNVCTHIADLDFGKI 230
Cdd:PRK11264 206 FARDVADRAIFMDQGRI 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-230 |
3.51e-06 |
|
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: 47.87 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKLfeDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkderlavlKQDH-FAYEEER 80
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN--------GVDVtAAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKgherlyevmkekdEIYMKPDFSDEDGIRAAELEGefAEMNGWNAEAdAASLLSGLGIsADLHDKQMSELENNQ 160
Cdd:cd03298 71 PVSMLFQ-------------ENNLFAHLTVEQNVGLGLSPG--LKLTAEDRQA-IEVALARVGL-AGLEKRLPGELSGGE 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 161 KVKVLLAQSLFGEPDVLLLDEPTNGLDiPAI-SWLEDFLINF----DNTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:cd03298 134 RQRVALARVLVRDKPVLLLDEPFAALD-PALrAEMLDLVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-229 |
3.77e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.45 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgKDERLAVLKQDHFAyeeeR 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL-RGQHIEGLPGHQIA----R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVVIKGHERLYEVMKEKDEIYMKPDFSDEDGIraaeLEGEFAEMNGWNAEAD----AASLLSGLGISaDLHDKQMSEL 156
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGL----FSGLLKTPAFRRAESEaldrAATWLERVGLL-EHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 157 ENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPA--------ISWLEDfliNFDNTVIVVSHDRHFLNNVCTHIADLDFG 228
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLN-PKetkeldelIAELRN---EHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
.
gi 499595078 229 K 229
Cdd:PRK11300 231 T 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-199 |
3.83e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GK-----DERLAVLKQDHF 74
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInNInynklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 75 AYEEERVLDvVIKGHERLYeVMKEKDEIYMKPDFSDedgiraaelegeFAEMngwnaEADAASLLSGLGISADLhDKQMS 154
Cdd:PRK09700 85 IYQELSVID-ELTVLENLY-IGRHLTKKVCGVNIID------------WREM-----RVRAAMMLLRVGLKVDL-DEKVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499595078 155 ELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLedFLI 199
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLI 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-79 |
4.23e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 4.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDErlavLKQDHFAYEEE 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS----IKKDLCTYQKQ 75
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-485 |
4.82e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMePDEGTFKW-GVttslsyfpkdnseffEGVDMNLVDWLRQ 408
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKInGI---------------ELRELDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 409 YA-----P------------------EDEQTETFLRG-----FLgRMLFSG--EEVKKKASVLSGGEKVRCMLSKMMLSS 458
Cdd:PRK11174 425 LSwvgqnPqlphgtlrdnvllgnpdaSDEQLQQALENawvseFL-PLLPQGldTPIGDQAAGLSVGQAQRLALARALLQP 503
|
170 180
....*....|....*....|....*..
gi 499595078 459 ANVLLLDEPTNHLDLESITAVNDGLAS 485
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-483 |
5.60e-06 |
|
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: 47.61 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGtfkwgvttslsyfpkdnSEFFEGVDMNLVDW--LR 407
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSG-----------------RILIDGHDVRDYTLasLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 408 QYAPEDEQtETFLrgflgrmlFSG---------------EEVKKKA------------------------SVLSGGEKVR 448
Cdd:cd03251 76 RQIGLVSQ-DVFL--------FNDtvaeniaygrpgatrEEVEEAAraanahefimelpegydtvigergVKLSGGQRQR 146
|
170 180 190
....*....|....*....|....*....|....*
gi 499595078 449 CMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGL 483
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
330-475 |
6.88e-06 |
|
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: 47.77 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGdseiA----KTTLLKILAGEMEPDEG---------TFKW---------G-VTTSL-S 385
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILG----PngagKSTLLSLITGDLPPTYGndvrlfgerRGGEdvwelrkriGlVSPALqL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 386 YFPKDNSeffeGVDMNL------VDWLRQYAPEDEQ-TETFLRgflgrmLFSGEEVKKKA-SVLSGGEKVRCMLSKMMLS 457
Cdd:COG1119 90 RFPRDET----VLDVVLsgffdsIGLYREPTDEQRErARELLE------LLGLAHLADRPfGTLSQGEQRRVLIARALVK 159
|
170
....*....|....*...
gi 499595078 458 SANVLLLDEPTNHLDLES 475
Cdd:COG1119 160 DPELLILDEPTAGLDLGA 177
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
319-495 |
1.03e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT---FKWGVTTSLSYFPKDNSeFF 395
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEilfERQSIKKDLCTYQKQLC-FV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 396 ---EGVDMNLVdwLRQYAPEDEQTETFLRGF--LGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNH 470
Cdd:PRK13540 80 ghrSGINPYLT--LRENCLYDIHFSPGAVGIteLCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*...
gi 499595078 471 LDLESITAVNDGLASFK---GSIIFTSY 495
Cdd:PRK13540 158 LDELSLLTIITKIQEHRakgGAVLLTSH 185
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
350-508 |
1.19e-05 |
|
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: 46.03 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 350 LIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTsLSYFPkdnseffegvdmnlvdwlrQYAPedeqtetflrgflgrmlf 429
Cdd:cd03222 30 IVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-PVYKP-------------------QYID------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 430 sgeevkkkasvLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASF----KGSIIFTSYDFEFINTIAN 505
Cdd:cd03222 72 -----------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSD 140
|
...
gi 499595078 506 RVI 508
Cdd:cd03222 141 RIH 143
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
308-528 |
1.22e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.54 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 308 KFTPEREIGND-LLTVQGLS-----KTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvt 381
Cdd:PRK13631 9 KLKVPNPLSDDiILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 382 tslSYFPKDNSEFFEGVDMNLVDWLRQYApEDEQTETFLRGFLGRMLF-----------------SGEEVKKKASV---- 440
Cdd:PRK13631 87 ---DIYIGDKKNNHELITNPYSKKIKNFK-ELRRRVSMVFQFPEYQLFkdtiekdimfgpvalgvKKSEAKKLAKFylnk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 441 --------------LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD----LESITAVNDGLASFKGSIIFTsYDFEFINT 502
Cdd:PRK13631 163 mglddsylerspfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgeHEMMQLILDAKANNKTVFVIT-HTMEHVLE 241
|
250 260
....*....|....*....|....*.
gi 499595078 503 IANRVIDLNQSGGLSKEVPYEEYLQE 528
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-473 |
1.33e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.70 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 321 TVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF--------KW---GVTTSLSYFPK 389
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWsskAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 390 -----DNSEFFEGVDMNLVDW---LRQYAPEDEQ------TETFLRGFLGRMLFSgeevkkkasvLSGGEKVRCMLSKMM 455
Cdd:PRK10575 93 qlpaaEGMTVRELVAIGRYPWhgaLGRFGAADREkveeaiSLVGLKPLAHRLVDS----------LSGGERQRAWIAMLV 162
|
170
....*....|....*...
gi 499595078 456 LSSANVLLLDEPTNHLDL 473
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDI 180
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
331-472 |
1.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 331 GEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG--VTTSLS----------------YFPKdnS 392
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdiVVSSTSkqkeikpvrkkvgvvfQFPE--S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 393 EFFEGVDMNLVDWLRQ-YAPEDEQTETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHL 471
Cdd:PRK13643 96 QLFEETVLKDVAFGPQnFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
.
gi 499595078 472 D 472
Cdd:PRK13643 176 D 176
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-472 |
1.58e-05 |
|
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: 46.77 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSK--TIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTL----LKILAGEMEPDEGTFKWGVTT------SLSYF 387
Cdd:cd03289 3 MTVKDLTAkyTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTEGDIQIDGVSWNSVPlqkwrkAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 388 PKDNSEFFEGVDMNLvDWLRQYAPED-----EQT--ETFLRGFLGRMLFSGEEvkkKASVLSGGEKVRCMLSKMMLSSAN 460
Cdd:cd03289 83 PQKVFIFSGTFRKNL-DPYGKWSDEEiwkvaEEVglKSVIEQFPGQLDFVLVD---GGCVLSHGHKQLMCLARSVLSKAK 158
|
170
....*....|..
gi 499595078 461 VLLLDEPTNHLD 472
Cdd:cd03289 159 ILLLDEPSAHLD 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
319-473 |
1.83e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGVTTSLSYfpkdNSEFFEGV 398
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTL----NGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 399 DMNLVDWLRQYAPEDEQ-------TETFLRGFLGRMLFSGEE--------------------VKKKASVLSGGEKVRCML 451
Cdd:PRK13547 77 DAPRLARLRAVLPQAAQpafafsaREIVLLGRYPHARRAGALthrdgeiawqalalagatalVGRDVTTLSGGELARVQF 156
|
170 180 190
....*....|....*....|....*....|.
gi 499595078 452 SKMM---------LSSANVLLLDEPTNHLDL 473
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-222 |
1.92e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF----GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGeidsqtghvsMGKDE-RLAVlkqDHFA 75
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG----------VTKDNwRVTA---DRMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 76 YEEERVLDVVIKGHERLyeVMKEKDEIYMKP----DFSDEDG------IRAAELEGEFAEMNGWNaEADAASLLSGLGIS 145
Cdd:PRK15093 70 FDDIDLLRLSPRERRKL--VGHNVSMIFQEPqsclDPSERVGrqlmqnIPGWTYKGRWWQRFGWR-KRRAIELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 146 AdlHDKQMS----ELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFL--INFDN--TVIVVSHDRHFLNN 217
Cdd:PRK15093 147 D--HKDAMRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNntTILLISHDLQMLSQ 224
|
....*
gi 499595078 218 VCTHI 222
Cdd:PRK15093 225 WADKI 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-49 |
2.05e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG 49
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
332-480 |
2.12e-05 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 45.72 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 332 EKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwGVTtslsyfpkdnseFFEGVDMNLVDWLRQ--Y 409
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQI------------LFNGQPRKPDQFQKCvaY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 410 APED---------EQTETFLRGFLGRMLFSGEEVKKKASV------------------LSGGEKVRCMLSKMMLSSANVL 462
Cdd:cd03234 86 VRQDdillpgltvRETLTYTAILRLPRKSSDAIRKKRVEDvllrdlaltriggnlvkgISGGERRRVSIAVQLLWDPKVL 165
|
170
....*....|....*...
gi 499595078 463 LLDEPTNHLDleSITAVN 480
Cdd:cd03234 166 ILDEPTSGLD--SFTALN 181
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-58 |
2.17e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 2.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 3 QVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHV 58
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
159-190 |
2.24e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.24e-05
10 20 30
....*....|....*....|....*....|..
gi 499595078 159 NQKvKVLLAQSLFGEPDVLLLDEPTNGLDIPA 190
Cdd:NF040905 409 NQQ-KVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
2.63e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSgeidsqtGHVSMgkderlAVLKQDHFaYEEER 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA-------GHPAY------KILEGDIL-FKGES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLDVV--IKGHERLYEVMKEKDEIymkPDFSDEDGIRAAelegefaemngWNA--------EADAASLLSGLGISADLHD 150
Cdd:CHL00131 73 ILDLEpeERAHLGIFLAFQYPIEI---PGVSNADFLRLA-----------YNSkrkfqglpELDPLEFLEIINEKLKLVG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 151 KQMSELENN--------QKVKVLLAQSLFGEPDVLLLDEPTNGLDIPA---ISWLEDFLINFDNTVIVVSHDRHFLN 216
Cdd:CHL00131 139 MDPSFLSRNvnegfsggEKKRNEILQMALLDSELAILDETDSGLDIDAlkiIAEGINKLMTSENSIILITHYQRLLD 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-211 |
2.95e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.18 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVT--DVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkDERLAVLKqdhfayEE 78
Cdd:PRK11000 1 MASVTlrNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG-EKRMNDVP------PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 79 ERVLDVVIKG-----HERLYEVM--------KEKDEIYMKPdfsdedgiraaelegefaemngwNAEADAASLlsglgis 145
Cdd:PRK11000 74 ERGVGMVFQSyalypHLSVAENMsfglklagAKKEEINQRV-----------------------NQVAEVLQL------- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595078 146 ADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIP-------AISWLEDFLinfDNTVIVVSHD 211
Cdd:PRK11000 124 AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHD 193
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-230 |
3.54e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.84 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRK-----LfEDVNIKFTEGNCYGLIGANGAGKSTFLKIL-------SGEIdsqtgHVSmGKD----- 63
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtaL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllerptSGSV-----LVD-GVDltals 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 64 -ERLAVLKQD------HFAYEEER-VLDVV-----IKGherlyevmKEKDEIymkpdfsDEdgiRAAELegefaemngwn 130
Cdd:COG1135 74 eRELRAARRKigmifqHFNLLSSRtVAENValpleIAG--------VPKAEI-------RK---RVAEL----------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 131 aeadaasL-LSGLgisADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiP----AI-SWLEDflIN--FD 202
Cdd:COG1135 125 -------LeLVGL---SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD-PettrSIlDLLKD--INreLG 191
|
250 260
....*....|....*....|....*...
gi 499595078 203 NTVIVVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:COG1135 192 LTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
319-472 |
3.56e-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: 45.12 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEK----VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvttslsyfpkdnsef 394
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 395 feGVDMNLVDwlrqyapEDEQTEtfLR----GF-------LGRM-----------LFSGEEVKKKA-------------- 438
Cdd:COG4181 73 --GQDLFALD-------EDARAR--LRarhvGFvfqsfqlLPTLtalenvmlpleLAGRRDARARArallervglghrld 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 499595078 439 ---SVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:COG4181 142 hypAQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
326-467 |
3.62e-05 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 44.77 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 326 SKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvtTSLSYFP----------KDN---- 391
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--GSIAYVSqepwiqngtiRENilfg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 392 ----SEFFEGV--------DMNLVdwlrqyaPEDEQTETflrgflgrmlfsGEevkkKASVLSGGEKVRCMLSKMMLSSA 459
Cdd:cd03250 90 kpfdEERYEKVikacalepDLEIL-------PDGDLTEI------------GE----KGINLSGGQKQRISLARAVYSDA 146
|
....*...
gi 499595078 460 NVLLLDEP 467
Cdd:cd03250 147 DIYLLDDP 154
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
4.05e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 45.39 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGD--RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGkderlavlkqdHFAYEEE 79
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-----------GMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVldvvikgherlYEVMKEKDEIYMKPDfsdedgiraaeleGEFAemnGWNAEADAASLLSGLGISAD---------LHD 150
Cdd:PRK13635 75 TV-----------WDVRRQVGMVFQNPD-------------NQFV---GATVQDDVAFGLENIGVPREemvervdqaLRQ 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 151 KQMSE--------LENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD-------IPAISWLEDfliNFDNTVIVVSHD 211
Cdd:PRK13635 128 VGMEDflnrephrLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-520 |
5.02e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.07 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 330 DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWGvTTSLSYFPKDNSEFFEGVDM---NLVDWL 406
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEPIKYDKKSLLEVRKTVGIvfqNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 407 rqYAPEDEQTETFLRGFLGrmlFSGEEVKKK-----ASV------------LSGGEKVRCMLSKMMLSSANVLLLDEPTN 469
Cdd:PRK13639 92 --FAPTVEEDVAFGPLNLG---LSKEEVEKRvkealKAVgmegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 470 HLDLESITAVNDGLASF--KG-SIIFTSYDFEFINTIANRVIDLNQ----SGGLSKEV 520
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnkEGiTIIISTHDVDLVPVYADKVYVMSDgkiiKEGTPKEV 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-472 |
5.84e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.59 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 305 PYVKF--TPEREIGNDLLTVQGLSKTIDGE--KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgv 380
Cdd:PRK11160 322 PEVTFptTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 381 ttSLSYFP-KDNSE---------------FFEGvdmNLVDWLRQYAPE--DEQTETFLR------------------GFL 424
Cdd:PRK11160 398 --LLNGQPiADYSEaalrqaisvvsqrvhLFSA---TLRDNLLLAAPNasDEALIEVLQqvgleklleddkglnawlGEG 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499595078 425 GRMLfsgeevkkkasvlSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:PRK11160 473 GRQL-------------SGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-472 |
6.21e-05 |
|
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: 44.38 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 335 LDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTF-------------KWGVTTSLSYFPkdnsefFEGVDMN 401
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVilegkqitepgpdRMVVFQNYSLLP------WLTVREN 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499595078 402 L---VDWLRQYAPEDEQtETFLRGFLgRMLFSGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:TIGR01184 75 IalaVDRVLPDLSKSER-RAIVEEHI-ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
7.22e-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: 43.46 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFG--DRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLavlkqdhfAYEEE 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--------DLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RvldvvikghERLYEVMKEKDEIYmkpdfsdedgiraaelegefaemngwnaeadAASLLSGLGIsadlhdkqmsELENN 159
Cdd:cd03247 73 L---------SSLISVLNQRPYLF-------------------------------DTTLRNNLGR----------RFSGG 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLD-IPAISWLEDFLINF-DNTVIVVSH 210
Cdd:cd03247 103 ERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLkDKTLIWITH 155
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-233 |
7.58e-05 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 43.94 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDR--KLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKD----------ERLAV 68
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDistipledlrSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 69 LKQDhfayeeERVLDVVIKGHERLYEvmkekdeiymkpDFSDEDGIRAAELEGefaemngwnaeadaasllSGLGISAdl 148
Cdd:cd03369 87 IPQD------PTLFSGTIRSNLDPFD------------EYSDEEIYGALRVSE------------------GGLNLSQ-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 149 hdkqmselenNQKVKVLLAQSLFGEPDVLLLDEPTNGLDipaisWLEDFLIN------FDN-TVIVVSHDRHFLNNvCTH 221
Cdd:cd03369 129 ----------GQRQLLCLARALLKRPRVLVLDEATASID-----YATDALIQktireeFTNsTILTIAHRLRTIID-YDK 192
|
250
....*....|..
gi 499595078 222 IADLDFGKIKLY 233
Cdd:cd03369 193 ILVMDAGEVKEY 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
292-512 |
7.68e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.30 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 292 IELDDIqpsSRRYPyVKFTPEREIGNDLLtvqGLSKTIDGEK-VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEME 370
Cdd:COG1134 5 IEVENV---SKSYR-LYHEPSRSLKELLL---RRRRTRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 371 PDEGTFKW-GVTTSLsyfpkdnsefFE-GVDMNlvdwlrqyaPEdeqtetfLRG-----FLGRML-FSGEEVKKK-ASVL 441
Cdd:COG1134 78 PTSGRVEVnGRVSAL----------LElGAGFH---------PE-------LTGreniyLNGRLLgLSRKEIDEKfDEIV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 442 ----------------SGGEKVRCMLSKMMLSSANVLLLDEptnhldlesITAVNDglASFK--------------GSII 491
Cdd:COG1134 132 efaelgdfidqpvktySSGMRARLAFAVATAVDPDILLVDE---------VLAVGD--AAFQkkclarirelresgRTVI 200
|
250 260
....*....|....*....|.
gi 499595078 492 FTSYDFEFINTIANRVIDLNQ 512
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEK 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-238 |
9.50e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 13 DRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDerlavlkqdhfaYEEERVLDVVIKGHER 91
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKD------------ISPRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 92 LYEVMKEKDeiyMKPDFSDEDGI------RAAELEGEFAEMNGWNAEADAASLLSGLGISADLHDKQMSELENNQKVKVL 165
Cdd:PRK09700 343 ITESRRDNG---FFPNFSIAQNMaisrslKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 166 LAQSLFGEPDVLLLDEPTNGLDIPA---ISWLEDFLINFDNTVIVVSHDRHFLNNVCTHIADLDFGKIKLYVGNYD 238
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-224 |
1.06e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.31 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF---GDRKLF----------EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVS-MGKDerl 66
Cdd:PRK15079 8 LLEVADLKVHFdikDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKD--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 67 aVLKQDHFAYEEERvldvvikgherlyevmKEKDEIYMKPDFS--------DedgIRAAELEGEFAEMNGWNAEADAASL 138
Cdd:PRK15079 85 -LLGMKDDEWRAVR----------------SDIQMIFQDPLASlnprmtigE---IIAEPLRTYHPKLSRQEVKDRVKAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 139 LSGLGISADLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLD--IPA--ISWLEDFLINFDNTVIVVSHDRhf 214
Cdd:PRK15079 145 MLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDvsIQAqvVNLLQQLQREMGLSLIFIAHDL-- 222
|
250
....*....|
gi 499595078 215 lnNVCTHIAD 224
Cdd:PRK15079 223 --AVVKHISD 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
316-374 |
1.13e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.99 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 316 GNDLLTVQGLSKTIDGEKVLDNISFTMnPNDKAILI-GDSEIAKTTLLKILAGEMEPDEG 374
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTV-PRGKITAImGPSGIGKTTLLRLIGGQIAPDHG 62
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-49 |
1.22e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.63 E-value: 1.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG 49
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYG 53
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-483 |
1.53e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 43.30 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 333 KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkwgvttslsyfpkdnseFFEGVDMNLVD--WLRQya 410
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-----------------LLDGVDIRDLNlrWLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 411 pedeqtetfLRGFLGR--MLFSG------------------EEVKKKA---------------------SVLSGGEKVRC 449
Cdd:cd03249 78 ---------QIGLVSQepVLFDGtiaenirygkpdatdeevEEAAKKAnihdfimslpdgydtlvgergSQLSGGQKQRI 148
|
170 180 190
....*....|....*....|....*....|....
gi 499595078 450 MLSKMMLSSANVLLLDEPTNHLDLESITAVNDGL 483
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
335-530 |
2.22e-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: 44.17 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 335 LDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGtfKWGVTTSLSYFPKD----NSEFFEGVDMNlvdwlRQYA 410
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--HVHMKGSVAYVPQQawiqNDSLRENILFG-----KALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 411 PEDEQTETFLRGFLG--RMLFSGE--EVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASF 486
Cdd:TIGR00957 727 EKYYQQVLEACALLPdlEILPSGDrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGP 806
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499595078 487 KGSI-----IFTSYDFEFINTIanRVIDLNQSGGLSKEVPYEEYLQEIG 530
Cdd:TIGR00957 807 EGVLknktrILVTHGISYLPQV--DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-229 |
2.24e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 134 DAASLLSGLGISADLHDKQMSELENNQKVKVLLAQSLFGEPD--VLLLDEPTNGLDIPAISWLEDF---LINFDNTVIVV 208
Cdd:cd03238 66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILI 145
|
90 100
....*....|....*....|...
gi 499595078 209 SHDRHFLNNvcthiAD--LDFGK 229
Cdd:cd03238 146 EHNLDVLSS-----ADwiIDFGP 163
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
432-523 |
2.33e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 432 EEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD---LESITAVNDGL-ASFKGSIIFTSYDFEFINTIANRV 507
Cdd:PRK13645 142 DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEV 221
|
90
....*....|....*.
gi 499595078 508 IDLNQSGGLSKEVPYE 523
Cdd:PRK13645 222 IVMHEGKVISIGSPFE 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
2.39e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRF-GDRKLFE---DVNIKFTEGNCYGLIGANGAGKSTFLKIL-------SGEI--DSQ--TghvSMGKDEr 65
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVlvDGQdlT---ALSEKE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 66 LAVLKQD------HFAYEEER-VLDVV-----IKGherlyevmKEKDEIymkpdfsdedgiraaelegefaemngwnaEA 133
Cdd:PRK11153 77 LRKARRQigmifqHFNLLSSRtVFDNValpleLAG--------TPKAEI-----------------------------KA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 134 DAASLLSGLGISaDLHDKQMSELENNQKVKVLLAQSLFGEPDVLLLDEPTNGLDiPAI--SWLEdfL---IN--FDNTVI 206
Cdd:PRK11153 120 RVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD-PATtrSILE--LlkdINreLGLTIV 195
|
250 260
....*....|....*....|....
gi 499595078 207 VVSHDRHFLNNVCTHIADLDFGKI 230
Cdd:PRK11153 196 LITHEMDVVKRICDRVAVIDAGRL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
320-378 |
2.66e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.17 E-value: 2.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 320 LTVQGLSKTIDGEKVLDNISFTMNPNdkailigdsEI--------A-KTTLLKILAGEMEPDEGTFKW 378
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKG---------EIfgllgpngAgKTTTIRIILGILAPDSGEVLW 60
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-210 |
2.67e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRK---LFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDER------------- 65
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 66 ----LAVLKQDHFAYEEE---------------------RVLDVVIKGHERLYEVMKEKD-----EIYMKPDFSDEDGIR 115
Cdd:PTZ00265 1246 eeqnVGMKNVNEFSLTKEggsgedstvfknsgkilldgvDICDYNLKDLRNLFSIVSQEPmlfnmSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 116 A-AELEGEFAEMNGWnaeadAASLLSGLGISADLHDKQMSeleNNQKVKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWL 194
Cdd:PTZ00265 1326 EdVKRACKFAAIDEF-----IESLPNKYDTNVGPYGKSLS---GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260
....*....|....*....|
gi 499595078 195 EDFLINF----DNTVIVVSH 210
Cdd:PTZ00265 1398 EKTIVDIkdkaDKTIITIAH 1417
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-472 |
4.63e-04 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 41.90 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 320 LTVQGLSKTI-DGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWG------------------V 380
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgedireqdpvelrrkigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 381 TTSLSYFP----KDNseffegvdMNLVDWLRQYAPE--DEQTETFLR-------GFLGRmlFSGEevkkkasvLSGGEKV 447
Cdd:cd03295 81 IQQIGLFPhmtvEEN--------IALVPKLLKWPKEkiRERADELLAlvgldpaEFADR--YPHE--------LSGGQQQ 142
|
170 180
....*....|....*....|....*
gi 499595078 448 RCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALD 167
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-190 |
4.69e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 18 EDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMGKDERLAVLKQDHFAY-----EEERVLDVVIKGHErl 92
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgivyiSEDRKRDGLVLGMS-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 93 yevMKEKDEIYMKPDFSDEDGI--RAAELE--GEFAEM-NGWNAEADAA-SLLSGlgisadlhdkqmseleNNQKvKVLL 166
Cdd:PRK10762 347 ---VKENMSLTALRYFSRAGGSlkHADEQQavSDFIRLfNIKTPSMEQAiGLLSG----------------GNQQ-KVAI 406
|
170 180
....*....|....*....|....
gi 499595078 167 AQSLFGEPDVLLLDEPTNGLDIPA 190
Cdd:PRK10762 407 ARGLMTRPKVLILDEPTRGVDVGA 430
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
319-521 |
6.32e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 41.60 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSK---------TIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKWgVTTSLSYFPK 389
Cdd:PRK10419 3 LLNVSGLSHhyahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 390 DNSEFFEG-VDMNLVDWLRQYAP------------------EDEQTETFLRGFLGRMLFSGEEVKKKASVLSGGEKVRCM 450
Cdd:PRK10419 82 AQRKAFRRdIQMVFQDSISAVNPrktvreiireplrhllslDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 451 LSKMMLSSANVLLLDEPTNHLDL----ESITAVNDGLASFKGSIIFTSYDFEFINTIANRVIDLNQsGGLSKEVP 521
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN-GQIVETQP 235
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
319-495 |
7.08e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAG-------------------EMEPDEGTFKwG 379
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyevtggtvefkgkdllELSPEDRAGE-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 380 VTTSLSY---FPKDNSEFFEGVDMNLVDWLRQYAPEDE-QTETFLRGFLGRMLFSGEEVKKKASV-LSGGEKVRCMLSKM 454
Cdd:PRK09580 80 IFMAFQYpveIPGVSNQFFLQTALNAVRSYRGQEPLDRfDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499595078 455 MLSSANVLLLDEPTNHLDLESITAVNDGLASFKGS----IIFTSY 495
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkrsfIIVTHY 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
441-476 |
7.15e-04 |
|
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: 41.05 E-value: 7.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499595078 441 LSGGEKV------RCMLSKMMLSSANVLLLDEPTNHLDLESI 476
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-187 |
7.49e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 40.69 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSqtGHVSmGkderlavlkqdhfayeeervlDVV 85
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTA--GVIT-G---------------------EIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 86 IKGHERlyevmkekdeiymKPDFSDEDGiraaelegeFAEMNgwNAEADAASLLSGLGISADLHDkqmseLENNQKVKVL 165
Cdd:cd03232 68 INGRPL-------------DKNFQRSTG---------YVEQQ--DVHSPNLTVREALRFSALLRG-----LSVEQRKRLT 118
|
170 180
....*....|....*....|..
gi 499595078 166 LAQSLFGEPDVLLLDEPTNGLD 187
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
319-507 |
7.82e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTSLSYfPKDNSEFFEG 397
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlGKEVTFNG-PKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 398 V---DMNLV----------------------DWLRQYAPEDeqtetflrGFLGRMLFSgEEVKKKASVLSGGEKVRCMLS 452
Cdd:PRK10762 83 IihqELNLIpqltiaeniflgrefvnrfgriDWKKMYAEAD--------KLLARLNLR-FSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499595078 453 KMMLSSANVLLLDEPTNHL---DLESITAVNDGLASFKGSIIFTSYDFEFINTIANRV 507
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDV 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
318-507 |
8.44e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.19 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 318 DLLTVQGLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKwgVTTSLSYFPKD-----NS 392
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKDifqidAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 393 EFFEGVDM---------------NLVDWLRQYAPEDEQ-----TETFLRGfLGRMLFSGEEVKKKASVLSGGEKVRCMLS 452
Cdd:PRK14246 87 KLRKEVGMvfqqpnpfphlsiydNIAYPLKSHGIKEKReikkiVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499595078 453 KMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKG--SIIFTSYDFEFINTIANRV 507
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-187 |
9.36e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDerLAVLKQDHFAYEEE 79
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGED--ISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGHERLYEVMKEKDEIymKPDFSDEDGIRAAelegefaemngwnaeadaaslLSGLGISADLHDKQMSELENN 159
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQI--RNQQPDPAIFLDD---------------------LERFALPDTILTKNIAELSGG 141
|
170 180
....*....|....*....|....*...
gi 499595078 160 QKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
15-218 |
1.07e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 15 KLFEDVNIKFTEG-NCygLIGANGAGKSTFLKILsgeidsqtgHVSMGKDERLAVLKQDHFAYEEERVLDVVIKGH--ER 91
Cdd:COG3593 12 RSIKDLSIELSDDlTV--LVGENNSGKSSILEAL---------RLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTfgSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 92 LYEVMKEKDEIYMKPDFSDEDGIRAAELEGEFAEMN----------GWNAEADAASLLSGL-----GISADLHDKQMSEL 156
Cdd:COG3593 81 LSRLLRLLLKEEDKEELEEALEELNEELKEALKALNellseylkelLDGLDLELELSLDELedllkSLSLRIEDGKELPL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499595078 157 ENN----QKVKVLLAQSLF------GEPDVLLLDEPTNGLDIPAISWLEDFLINF---DNTVIVVSHDRHFLNNV 218
Cdd:COG3593 161 DRLgsgfQRLILLALLSALaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELsekPNQVIITTHSPHLLSEV 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-187 |
1.08e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.87 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 6 DVSLRF-GDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSM-GKDER---LAVLKQD-HFAYEEE 79
Cdd:PRK13657 339 DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRtvtRASLRRNiAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 80 RVLDVVIKGHERLyevmkekdeiyMKPDFSDEDGIRAAELEG--EFAE--MNGWNAEA-DAASLLSGlgisadlhdkqms 154
Cdd:PRK13657 419 GLFNRSIEDNIRV-----------GRPDATDEEMRAAAERAQahDFIErkPDGYDTVVgERGRQLSG------------- 474
|
170 180 190
....*....|....*....|....*....|...
gi 499595078 155 elenNQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:PRK13657 475 ----GERQRLAIARALLKDPPILILDEATSALD 503
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-187 |
1.27e-03 |
|
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: 40.23 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 5 TDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQ--TGHVSM-GKDERLAVLKQdHFAY-EEER 80
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLInGRPLDKRSFRK-IIGYvPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 81 VLdvvikgHERL--YEVMkekdeiymkpDFSdedgiraAELEGefaemngwnaeadaaslLSGlgisadlhdkqmselen 158
Cdd:cd03213 92 IL------HPTLtvRETL----------MFA-------AKLRG-----------------LSG----------------- 114
|
170 180
....*....|....*....|....*....
gi 499595078 159 NQKVKVLLAQSLFGEPDVLLLDEPTNGLD 187
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
436-515 |
1.50e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 436 KKASVLSGGEKVRCMLSKMMLSSA--NVLLLDEPT---NHLDLESITAVNDGLASFKGSIIFTSYDFEFINTiANRVIDL 510
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPStglHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
....*....
gi 499595078 511 ----NQSGG 515
Cdd:cd03238 162 gpgsGKSGG 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-49 |
1.58e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 499595078 5 TDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSG 49
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG 46
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
434-528 |
1.77e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 434 VKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDL----ESITAVNDGLASFKGSIIFTSYDFEFINtIANRVID 509
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINELAAEGKGVIVISSELPELLG-MCDRIYV 476
|
90
....*....|....*....
gi 499595078 510 LNQsGGLSKEVPYEEYLQE 528
Cdd:NF040905 477 MNE-GRITGELPREEASQE 494
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-378 |
1.77e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 319 LLTVQGLSKTIDGEKVLDNISFTMNPNdkailigdsEI--------A-KTTLLKILAGEMEPDEGTFKW 378
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPG---------EIhallgengAgKSTLMKILYGLYQPDSGEILI 64
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-472 |
1.93e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 333 KVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFkWGvTTSLSYFP----------KDNSEFFEGVD-MN 401
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA-ERSIAYVPqqawimnatvRGNILFFDEEDaAR 751
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595078 402 LVDWLRQyapedEQTETFLRGFLGRMlfsGEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:PTZ00243 752 LADAVRV-----SQLEADLAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-188 |
2.15e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.20 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 1 MLQVTDVSLRFGDRKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQ--------TGHVSMgKDERLAVLKQD 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTL-NGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 73 HFAyeeeRVLDVVIKGHERLYEVmkEKDEIYMKPDFSdeDGIRAAELEGEFAEMnGWNA--EADAASLLsglgiSADLHD 150
Cdd:PRK13547 80 RLA----RLRAVLPQAAQPAFAF--SAREIVLLGRYP--HARRAGALTHRDGEI-AWQAlaLAGATALV-----GRDVTT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499595078 151 KQMSELENNQKVKVlLAQsLFGEPDV------LLLDEPTNGLDI 188
Cdd:PRK13547 146 LSGGELARVQFARV-LAQ-LWPPHDAaqppryLLLDEPTAALDL 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
441-529 |
2.51e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.92 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 441 LSGGEKVRCMLSKMML-------SSANVLLLDEPTNHLDLESITAVN---DGLASFKGSIIFTSYDFEFINTIANRVIDL 510
Cdd:PRK03695 127 LSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHDLNHTLRHADRVWLL 206
|
90 100
....*....|....*....|...
gi 499595078 511 NQ----SGGLSKEVPYEEYLQEI 529
Cdd:PRK03695 207 KQgkllASGRRDEVLTPENLAQV 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
324-375 |
2.68e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499595078 324 GLSKTIDGEKVLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGT 375
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS 54
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
334-507 |
2.86e-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: 40.70 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 334 VLDNISFTMNPNDKAILIGDSEIAKTTLLKILAGEMEPDEGTFKW-GVTTS----------LSYFPKDNSEFFEGVDMNL 402
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdGLNIAkiglhdlrfkITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 403 vDWLRQYAPEDEQTE---TFLRGFLGRMLFS-GEEVKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESita 478
Cdd:TIGR00957 1381 -DPFSQYSDEEVWWAlelAHLKTFVSALPDKlDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET--- 1456
|
170 180
....*....|....*....|....*....
gi 499595078 479 vnDGLASfkgSIIFTSYDFEFINTIANRV 507
Cdd:TIGR00957 1457 --DNLIQ---STIRTQFEDCTVLTIAHRL 1480
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-58 |
2.87e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 39.59 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499595078 1 MLQVTDVSLRFGD-RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHV 58
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV 59
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-211 |
3.86e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.89 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 14 RKLFEDVNIKFTEGNCYGLIGANGAGKSTFLKILSGEIDSQTGHVSMgkDERLAVLKQDHFAYE-------EERVLDVVI 86
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL--DGKPIDIRSPRDAIRagimlcpEDRKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595078 87 KGHerlyevmkekdeiymkpdfSDEDGI----RAAELEGEFAEMNGWNAEaDAASLLSGLGISADLHDKQMSELEN-NQK 161
Cdd:PRK11288 344 PVH-------------------SVADNInisaRRHHLRAGCLINNRWEAE-NADRFIRSLNIKTPSREQLIMNLSGgNQQ 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499595078 162 vKVLLAQSLFGEPDVLLLDEPTNGLDIPAISWLEDFLINFDN---TVIVVSHD 211
Cdd:PRK11288 404 -KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqgvAVLFVSSD 455
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-49 |
3.92e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 3.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 499595078 2 LQVTDVSLRFGDRKlFE--DVNIKFTEGNCYGLIGANGAGKSTFLKILSG 49
Cdd:PRK10522 323 LELRNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTG 371
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
441-473 |
5.23e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.09 E-value: 5.23e-03
10 20 30
....*....|....*....|....*....|...
gi 499595078 441 LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDL 473
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
177-224 |
7.66e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.38 E-value: 7.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499595078 177 LLLDEPTNGLDIPAISWLeDFLIN----FDNTVIVVSHDrhfLNNVCTHiAD 224
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAAL-DRLLSelcqQGIAVVMSSHD---LNHTLRH-AD 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
434-489 |
8.08e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 8.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499595078 434 VKKKASVLSGGEKVRCMLSKMMLSSANVLLLDEPTNHLDLESITAVNDGLASFKGS 489
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
441-472 |
8.47e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 37.85 E-value: 8.47e-03
10 20 30
....*....|....*....|....*....|..
gi 499595078 441 LSGGEKVRCMLSKMMLSSANVLLLDEPTNHLD 472
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
15-47 |
9.33e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 9.33e-03
10 20 30
....*....|....*....|....*....|...
gi 499595078 15 KLFEDVNIKFTEGNCygLIGANGAGKSTFLKIL 47
Cdd:COG4637 11 KSLRDLELPLGPLTV--LIGANGSGKSNLLDAL 41
|
|
| |
