|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-540 |
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: 588.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNDNLSVKDALN 88
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YELKEIFDARDEYEKVLAQISnehDNPELLHRQDELVKFIESKDGWNIENKIERILDSFGL-REYENRLVNSLSGGEIRR 167
Cdd:COG0488 84 DGDAELRALEAELEELEAKLA---EPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 168 VALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGYANYLTK 247
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 248 KEEILRSLAKSHETLIKNLKSEEEWLRR-GVKAR-LKRNEGRKQRILAMREEAKKNPGliRRVKLELERASKSfngggln 325
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARkAKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERL------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 326 qnrKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGE-IKIGYFDQSRK 404
Cdd:COG0488 312 ---GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtVKIGYFDQHQE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 405 SISDDKSLIELFCpnggdHIMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDL 484
Cdd:COG0488 389 ELDPDKTVLDELR-----DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 485 DIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQIYMEYSEYLD 540
Cdd:COG0488 464 DIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-609 |
2.20e-160 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 474.44 E-value: 2.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNDN 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 LSVKDALNYELKEIFDARDEYEKVLAQIsnEHDNPE-LLHRQDELVKFIESKDGWNIENKIERILDSFGLREyeNRLVNS 159
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLV--ETDPSEkNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP--DAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDG 239
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 240 GYANYLTKKEEILRSLAKSHETLIKNLKSEEEWLRRGVKARLKRNEGRKQRILAMREEAKKNPGLIRRVKLELERASKSf 319
Cdd:PRK11147 237 NYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRS- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 320 nggglnqnrKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRG-EIKIGY 398
Cdd:PRK11147 316 ---------GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtKLEVAY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 FDQSRKSISDDKSLIElfcpNGGD---HIMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCL 475
Cdd:PRK11147 387 FDQHRAELDPEKTVMD----NLAEgkqEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 476 ILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYE-NGKIEQIYMEYSEYLDIEEELNQLSDIESE 554
Cdd:PRK11147 463 ILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHDARQQQAQYLALKQPAVK 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 555 LGQSIETKEKQ--KTSKVKLTYKQNQILQNHPALIEALESRISELNHALSTPEIYQK 609
Cdd:PRK11147 543 KKEEAAAPKAEtvKRSSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQ 599
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-538 |
2.01e-119 |
|
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: 366.57 E-value: 2.01e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKF-GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGeceID---SGRVIRQNSISIEMLAQSPKFNDNLSVK 84
Cdd:TIGR03719 10 VSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DALNYELKEIFDARDEYEKVLAQISNEHDN-PELLHRQDELVKFIESKDGWNIENKIERILDSFGLREYENRlVNSLSGG 163
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFNEISAKYAEPDADfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDAD-VTKLSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGYAN 243
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 244 YLTKKEEILRSLAKSHETLIKNLKSEEEWLRRGVKARLKRNEGRKQRI--LAMREEAKKNPglirrvKLEL-----ERAs 316
Cdd:TIGR03719 246 WLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYeeLLSQEFQKRNE------TAEIyippgPRL- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 317 ksfngGGLnqnrkkmLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGE-IK 395
Cdd:TIGR03719 319 -----GDK-------VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 396 IGYFDQSRKSISDDKSLIELFcPNGGDHIMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCL 475
Cdd:TIGR03719 387 LAYVDQSRDALDPNKTVWEEI-SGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 476 ILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYE-NGKIEQIYMEYSEY 538
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-538 |
1.21e-112 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 349.03 E-value: 1.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFG-DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGeceID---SGRVIRQNSISIEMLAQSPKFNDNLSVK 84
Cdd:PRK11819 12 VSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkefEGEARPAPGIKVGYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DALNYELKEIFDARDEYEKVLAQISNEH-DNPELLHRQDELVKFIESKDGWNIENKIERILDSFGLREYENRlVNSLSGG 163
Cdd:PRK11819 89 ENVEEGVAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAK-VTKLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGYAN 243
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 244 YLTKKEEILRSLAKSHETLIKNLKSEEEWLRRGVKARLKRNEGRKQRI--LAMREEAKKNPglirrvKLEL-----ERas 316
Cdd:PRK11819 248 WLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYeeLLSEEYQKRNE------TNEIfippgPR-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 317 ksfngggLNQNrkkmLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGE-IK 395
Cdd:PRK11819 320 -------LGDK----VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 396 IGYFDQSRKSISDDKSLIELFcPNGGDHIMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCL 475
Cdd:PRK11819 389 LAYVDQSRDALDPNKTVWEEI-SGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 476 ILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYE-NGKIEQIYMEYSEY 538
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEY 531
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-539 |
2.12e-71 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 240.18 E-value: 2.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGdkiilnetnfnvnEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNDNLSVKDALN 88
Cdd:PRK15064 20 ISVKFG-------------GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YELKEIFDARDEYEKVLAqisnehdNPEL-----LHRQDELVKFIEsKDGWNIENKIERILDSFGL-REYENRLVNSLSG 162
Cdd:PRK15064 87 MGHTELWEVKQERDRIYA-------LPEMseedgMKVADLEVKFAE-MDGYTAEARAGELLLGVGIpEEQHYGLMSEVAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGYA 242
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 243 NYLTK----KEEILRSLAKSHETlIKNLKSeeewlrrgVKARLKRNEGrKQRILAMReeAKKnpglIRRVKLELERASKS 318
Cdd:PRK15064 239 EYMTAatqaRERLLADNAKKKAQ-IAELQS--------FVSRFSANAS-KAKQATSR--AKQ----IDKIKLEEVKPSSR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 319 FNGG-GLNQNRK--KMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGE-I 394
Cdd:PRK15064 303 QNPFiRFEQDKKlhRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEnA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 395 KIGYFDQ-SRKSISDDKSLIELFC---PNGGDHIMVRGrnyhvygYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTK 470
Cdd:PRK15064 383 NIGYYAQdHAYDFENDLTLFDWMSqwrQEGDDEQAVRG-------TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 471 EYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQIYMEYSEYL 539
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYL 524
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-605 |
4.76e-62 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 217.73 E-value: 4.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQ-SPKFNdnlsvKDALNYelk 92
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQeTPALP-----QPALEY--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 93 eIFDARDEYEKVLA--QISNEHDNPE---LLHRQdelvkfIESKDGWNIENKIERILDSFGL-REYENRLVNSLSGGEIR 166
Cdd:PRK10636 84 -VIDGDREYRQLEAqlHDANERNDGHaiaTIHGK------LDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 167 RVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGYANYLT 246
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 247 KKEEIL---RSLAKSHETLIKNLKSeeewlrrgvkarlkrnegrkqRILAMREEAKKNPGLIRRVKLeLERASK------ 317
Cdd:PRK10636 237 QRATRLaqqQAMYESQQERVAHLQS---------------------YIDRFRAKATKAKQAQSRIKM-LERMELiapahv 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 318 ------SFNGgglNQNRKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINR 391
Cdd:PRK10636 295 dnpfhfSFRA---PESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 392 GE-IKIGYFDQSRKSI--SDDKSLIELfcpnggDHIMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLF 468
Cdd:PRK10636 372 AKgIKLGYFAQHQLEFlrADESPLQHL------ARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 469 TKEYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQIYMEYSEY----LDIEEE 544
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYqqwlSDVQKQ 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 545 LNQLSDIESEL-GQSIETKEKQKTSKVKLTyKQNQILQNHpalIEALESRISELNHALSTPE 605
Cdd:PRK10636 526 ENQTDEAPKENnANSAQARKDQKRREAELR-TQTQPLRKE---IARLEKEMEKLNAQLAQAE 583
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-544 |
3.97e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 196.05 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 335 CKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINR-GEIKIGYFDQ-----SRKSISD 408
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLPQeppldDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 409 -----DKSLIELF--------CPNGGDHIMVR-----GRNYHVYGY---------LKNFLFPKEFLDKPVGVLSGGEKNR 461
Cdd:COG0488 81 tvldgDAELRALEaeleeleaKLAEPDEDLERlaelqEEFEALGGWeaearaeeiLSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 462 LALA-LLFTkEYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQIYMEYSEYLD 540
Cdd:COG0488 161 VALArALLS-EPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
....
gi 1196666485 541 IEEE 544
Cdd:COG0488 240 QRAE 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-527 |
4.24e-55 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 184.19 E-value: 4.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGE-IKIGYFDQsrksisddksl 412
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ielfcpnggdhimvrgrnyhvygylknflfpkefldkpvgvLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINIL 492
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 1196666485 493 EEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGK 527
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-247 |
7.93e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 186.81 E-value: 7.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPK-FNDNL 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEeLDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKDalnyELKEIFDARDEYEkvlaqisnehdnpellhrqdelvkfieskdgwnienkIERILDSFGLREYE-NRLVNSL 160
Cdd:COG0488 395 TVLD----ELRDGAPGGTEQE-------------------------------------VRGYLGRFLFSGDDaFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 161 SGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGG 240
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGG 513
|
....*..
gi 1196666485 241 YANYLTK 247
Cdd:COG0488 514 YDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-538 |
1.45e-41 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 160.80 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILR--------GECEIDSgrvIRQNSISIEMLAQSPKFNDNLSVKD 85
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipKNCQILH---VEQEVVGDDTTALQCVLNTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 ALNYELKEIFDARD-EYEKVLAQISNEH----DNPELLHRQDELVKFIESKDGWNIENKIERILDSFGLR-EYENRLVNS 159
Cdd:PLN03073 265 LLEEEAQLVAQQRElEFETETGKGKGANkdgvDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTpEMQVKATKT 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDG 239
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 240 GYANYLTKKEEILRSLAKSHETliknlkseeewlrrgvkarlkrNEGRKQRILA----MREEAKKNPGLIRRVKlELERA 315
Cdd:PLN03073 425 DYDTFERTREEQLKNQQKAFES----------------------NERSRSHMQAfidkFRYNAKRASLVQSRIK-ALDRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 316 sksfngGGLNQ--NRKKMLFEcknlSKTIDNK-------------------VLFSDFNARVLQGERIGIVGRNGSGKSTM 374
Cdd:PLN03073 482 ------GHVDAvvNDPDYKFE----FPTPDDRpgppiisfsdasfgypggpLLFKNLNFGIDLDSRIAMVGPNGIGKSTI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 375 LKILLGELEADSGVINRG-EIKIGYFDQSRK---SISDDKSLIELFCPNGGDHIMVRgrnyhvyGYLKNFLFPKEFLDKP 450
Cdd:PLN03073 552 LKLISGELQPSSGTVFRSaKVRMAVFSQHHVdglDLSSNPLLYMMRCFPGVPEQKLR-------AHLGSFGVTGNLALQP 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 451 VGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQ 530
Cdd:PLN03073 625 MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTP 704
|
....*...
gi 1196666485 531 IYMEYSEY 538
Cdd:PLN03073 705 FHGTFHDY 712
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-232 |
6.94e-41 |
|
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: 145.67 E-value: 6.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQspkfndnlsv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 kdalnyelkeifdardeyekvlaqisnehdnpellhrqdelvkfieskdgwnienkierildsfglreyenrlvnsLSGG 163
Cdd:cd03221 71 ----------------------------------------------------------------------------LSGG 74
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:cd03221 75 EKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-520 |
1.03e-35 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 142.25 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 32 IAIIGKNGGGKSTLMKILRGECEIDSGRvirqnsisiemlaqspkFNDNLSVKDALNY----ELKEIFdaRDEYEKVL-- 105
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGD-----------------YEEEPSWDEVLKRfrgtELQNYF--KKLYNGEIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 106 -------AQISNEHDNP--ELLHRQDElvkfieskdgwniENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILK 176
Cdd:PRK13409 163 vhkpqyvDLIPKVFKGKvrELLKKVDE-------------RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 177 KPDVLLLDEPTNHLDVY----MVRFLEEllLASNQTIVFISHDRYFIDRLATrSVEIEDGAlrsfDGGYAnyltkkeeil 252
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRqrlnVARLIRE--LAEGKYVLVVEHDLAVLDYLAD-NVHIAYGE----PGAYG---------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 253 rslakshetLIKNLKSeeewLRRGVKARLK---RNEGrkqrilaMReeakknpglIRRVKLELE-RASKSfnggglnQNR 328
Cdd:PRK13409 293 ---------VVSKPKG----VRVGINEYLKgylPEEN-------MR---------IRPEPIEFEeRPPRD-------ESE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 329 KKMLFECKNLSKTIDNKVLFSDfNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRgEIKIGYFDQsrkSISD 408
Cdd:PRK13409 337 RETLVEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKPQ---YIKP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 409 DKSL-IELFCPNGGDHImvrGRNYhvygYLKNFLFP---KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDL 484
Cdd:PRK13409 412 DYDGtVEDLLRSITDDL---GSSY----YKSEIIKPlqlERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1196666485 485 D----IATINILEEYLLSFEGAILIVSHDRYFIDKITNKL 520
Cdd:PRK13409 485 DveqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-516 |
7.06e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.88 E-value: 7.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKF--GDKIILNETNFNVNEKERIAIIGKNGGGKSTL----MKILRGECEID-----SGRVIRQNSIS--- 67
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLalalMGLLPHGGRISgevllDGRDLLELSEAlrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 --IEMLAQSPKfndnlsvkDALNYElkeifdardeyeKVLAQISNEHDNPELLHRQdelvkfieskdgwnIENKIERILD 145
Cdd:COG1123 83 rrIGMVFQDPM--------TQLNPV------------TVGDQIAEALENLGLSRAE--------------ARARVLELLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 146 SFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDRYFIDR 221
Cdd:COG1123 129 AVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 222 LATRSVEIEDGALRsFDGgyanyltKKEEILRSLAKSHETLiknlkseeewlrrgvkaRLKRNEGRKQRILAMREEAkkn 301
Cdd:COG1123 209 IADRVVVMDDGRIV-EDG-------PPEEILAAPQALAAVP-----------------RLGAARGRAAPAAAAAEPL--- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 302 pglirrvkLELERASKSFNGGGLNqnrkkmlfecknlsktiDNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGE 381
Cdd:COG1123 261 --------LEVRNLSKRYPVRGKG-----------------GVRAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 382 LEADSGVI----------NRGEIK-----IGY-F---DQS---RKSISDdkSLIE-LFCPNGGDHIMVRGRnyhVYGYLK 438
Cdd:COG1123 315 LRPTSGSIlfdgkdltklSRRSLRelrrrVQMvFqdpYSSlnpRMTVGD--IIAEpLRLHGLLSRAERRER---VAELLE 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 439 NFLFPKEFLDKPVGVLSGGEKNRL----ALALlftkEYDCLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSHD- 509
Cdd:COG1123 390 RVGLPPDLADRYPHELSGGQRQRVaiarALAL----EPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDl 465
|
570
....*....|
gi 1196666485 510 ---RYFIDKI 516
Cdd:COG1123 466 avvRYIADRV 475
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-528 |
2.54e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-----NRGEI-------KIGYFD 400
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMpppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 401 QSrksiSDdkslieLFCPNGGDHI----MVRGRNY---HVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLAL--ALLFTKe 471
Cdd:COG4619 81 QE----PA------LWGGTVRDNLpfpfQLRERKFdreRALELLERLGLPPDILDKPVERLSGGERQRLALirALLLQP- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 472 yDCLILDEPTNDLDIATINILEEYLLSF----EGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:COG4619 150 -DVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-531 |
2.62e-33 |
|
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: 134.16 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG--ECEIDSGRVIRQNSISIEMLAQSPKFNDNL 81
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKDALNYELKEIFDARDEYEKVLAQISNEhdNPELLHR-------QDELVKFIESKD--GWNIENKIERILDSFGLREY 152
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWNLSDKLRRRIRKR--IAIMLQRtfalygdDTVLDNVLEALEeiGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 153 ENRLVN---SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRF----LEELLLASNQTIVFISHDRYFIDRLATR 225
Cdd:TIGR03269 159 SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 226 SVEIEDGALRSfDGGYANYLTKKEEILRSLAKSHETLIKNlkseeewlrrgvkarlkrnegrkqRILAMREEAKKnpgli 305
Cdd:TIGR03269 239 AIWLENGEIKE-EGTPDEVVAVFMEGVSEVEKECEVEVGE------------------------PIIKVRNVSKR----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 306 rrvKLELERAsksfnggglnqnrkkmlfecknLSKTIDNkvlfSDFNarVLQGERIGIVGRNGSGKSTMLKILLGELEAD 385
Cdd:TIGR03269 289 ---YISVDRG----------------------VVKAVDN----VSLE--VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 386 SG-----------------VINRGEIK--IGYFDQS------RKSISDDKSLIELFCPnggDHIMVRgRNYHVygyLKNF 440
Cdd:TIGR03269 338 SGevnvrvgdewvdmtkpgPDGRGRAKryIGILHQEydlyphRTVLDNLTEAIGLELP---DELARM-KAVIT---LKMV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 441 LF----PKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLL----SFEGAILIVSHDRYF 512
Cdd:TIGR03269 411 GFdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDF 490
|
570
....*....|....*....
gi 1196666485 513 IDKITNKLWAYENGKIEQI 531
Cdd:TIGR03269 491 VLDVCDRAALMRDGKIVKI 509
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-232 |
1.20e-32 |
|
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: 124.89 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSI-----SIEMLAQSPK---FN 78
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLngllgptSGEVLVD-GKDLTKLSLkelrrKVGLVFQNPDdqfFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLsvkdalnyelkeifdaRDEyekvLAQisnehdNPELLHRQDElvkfieskdgwNIENKIERILDSFGLREYENRLVN 158
Cdd:cd03225 91 PTV----------------EEE----VAF------GLENLGLPEE-----------EIEERVEEALELVGLEGLRDRSPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKklkAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-234 |
1.31e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 125.56 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSISIE----MLAQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRrrigYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 SPKFNDNLSVKDALNYeLKEIFDardeyekvlaqisnehdnpellhrqdelvkfiesKDGWNIENKIERILDSFGLREYE 153
Cdd:COG1131 81 EPALYPDLTVRENLRF-FARLYG----------------------------------LPRKEARERIDELLELFGLTDAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHDRYFIDRLATRSVEIE 230
Cdd:COG1131 126 DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRelaAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
....
gi 1196666485 231 DGAL 234
Cdd:COG1131 206 KGRI 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-520 |
4.05e-32 |
|
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: 131.45 E-value: 4.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 32 IAIIGKNGGGKSTLMKILRGECEIDSGRvirqnsisiemlaqspkFNDNLSVKDALNY----ELKEIFdaRDEYEKVL-- 105
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGD-----------------YDEEPSWDEVLKRfrgtELQDYF--KKLANGEIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 106 -------AQISNEHDNP--ELLHRQDElvkfieskdgwniENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILK 176
Cdd:COG1245 163 ahkpqyvDLIPKVFKGTvrELLEKVDE-------------RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 177 KPDVLLLDEPTNHLDVY----MVRFLEElLLASNQTIVFISHDRYFIDRLATrSVEIEDGAlrsfDGGYAnyltkkeeil 252
Cdd:COG1245 230 DADFYFFDEPSSYLDIYqrlnVARLIRE-LAEEGKYVLVVEHDLAILDYLAD-YVHILYGE----PGVYG---------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 253 rslakshetLIKNLKSeeewLRRGVKARLK---RNEGrkqrilaMReeakknpglIRRVKLELE-RASKSFNGGglnqnr 328
Cdd:COG1245 294 ---------VVSKPKS----VRVGINQYLDgylPEEN-------VR---------IRDEPIEFEvHAPRREKEE------ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 329 kKMLFECKNLSKTIDNKVLFSDfNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINrGEIKIGYFDQSRKSISD 408
Cdd:COG1245 339 -ETLVEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKPQYISPDYD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 409 DksLIELFcpnggdhimVRGRNYHVYG--YLKN-FLFP---KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTN 482
Cdd:COG1245 416 G--TVEEF---------LRSANTDDFGssYYKTeIIKPlglEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1196666485 483 DLD----IATINILEEYLLSFEGAILIVSHDRYFIDKITNKL 520
Cdd:COG1245 485 HLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-248 |
1.92e-31 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 128.86 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 8 EVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQ--SPKFNDNLSVKD 85
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdhAYDFENDLTLFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 ALnyelkeifdardeyekvlAQISNEHDNpellhrqDELVKFIeskdgwnienkIERILdsFGLREYeNRLVNSLSGGEI 165
Cdd:PRK15064 404 WM------------------SQWRQEGDD-------EQAVRGT-----------LGRLL--FSQDDI-KKSVKVLSGGEK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 166 RRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGYANYL 245
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYL 524
|
...
gi 1196666485 246 TKK 248
Cdd:PRK15064 525 RSQ 527
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-271 |
2.40e-31 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 122.27 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDSGRVIRQNSI---SIEMLA 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLagllkpdSGSILIDGEDVRKEPREarrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPKFNDNLSVKDALNY--ELKEIFDARdeyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIERILDSFGLR 150
Cdd:COG4555 81 DERGLYDRLTVRENIRYfaELYGLFDEE-------------------------------------LKKRIEELIELLGLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA---SNQTIVFISHDRYFIDRLATRSV 227
Cdd:COG4555 124 EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlkkEGKTVLFSSHIMQEVEALCDRVV 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1196666485 228 EIEDGALRsfdggyanYLTKKEEILRSLAKSH--ETLIKNLKSEEE 271
Cdd:COG4555 204 ILHKGKVV--------AQGSLDELREEIGEENleDAFVALIGSEEG 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
1.43e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.15 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI----RQNSISIE-------MLA 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkPLSAMPPPewrrqvaYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPKFNDNlSVKDALNYELkeifdardeyekvlaQISNEHDNPEllhrqdelvkfieskdgwnienKIERILDSFGLRE- 151
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPF---------------QLRERKFDRE----------------------RALELLERLGLPPd 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFISHDRYFIDRLATRSV 227
Cdd:COG4619 123 ILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLReylaEEGRAVLWVSHDPEQIERVADRVL 202
|
....*..
gi 1196666485 228 EIEDGAL 234
Cdd:COG4619 203 TLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-233 |
5.81e-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: 117.19 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIE---------ML 71
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlWNGEPIRDAredyrrrlaYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 72 AQSPKFNDNLSVKDALNYelkeifdardeyekvLAQISNEHDNPELlhrqdelvkfieskdgwnienkIERILDSFGLRE 151
Cdd:COG4133 81 GHADGLKPELTVRENLRF---------------WAALYGLRADREA----------------------IDEALEAVGLAG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL---LASNQTIVFISHDRYFIDrlATRSVE 228
Cdd:COG4133 124 LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELA--AARVLD 201
|
....*
gi 1196666485 229 IEDGA 233
Cdd:COG4133 202 LGDFK 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-253 |
5.49e-29 |
|
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: 115.12 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKF-GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkFNDnls 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL---------------VDG--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vKDALNYELKEIfdardeYEKV--LAQisnehdNPEllhrqDELVKFIESKD--------GWN---IENKIERILDSFGL 149
Cdd:COG1122 63 -KDITKKNLREL------RRKVglVFQ------NPD-----DQLFAPTVEEDvafgpenlGLPreeIRERVEEALELVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 150 REYENRLVNSLSGGEIRRVAL-GALILkKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHDRYFIDRLATR 225
Cdd:COG1122 125 EHLADRPPHELSGGQKQRVAIaGVLAM-EPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADR 203
|
250 260
....*....|....*....|....*...
gi 1196666485 226 SVEIEDGALRsFDGGYANYLTKKEEILR 253
Cdd:COG1122 204 VIVLDDGRIV-ADGTPREVFSDYELLEE 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
331-514 |
7.68e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.11 E-value: 7.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgeiKIGYFDQSRKSISDDK 410
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAG-------EVLWNGEPIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLIELFCpngGDHIMVRGR-----NYHVYGYLKNFLFPKE-------------FLDKPVGVLSGGEKNRLALALLFTKEY 472
Cdd:COG4133 74 RRRLAYL---GHADGLKPEltvreNLRFWAALYGLRADREaidealeavglagLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1196666485 473 DCLILDEPTNDLDIATINILEEYLLSF---EGAILIVSHDRYFID 514
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-234 |
1.50e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 114.52 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFG----DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-----------IRQNSIS 67
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 IEMLAQSPK--FNDNLSVKDALnyelkeifdarDEyekvlaqisnehdnPELLHRQDElvkfieskdgwnIENKIERILD 145
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDRIL-----------AE--------------PLRIHGLPD------------REERIAELLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 146 SFGL-REYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFI 219
Cdd:COG1124 124 QVGLpPSFLDRYPHQLSGGQRQRVAIArALILE-PELLLLDEPTSALDVSvqaeILNLLKDLREERGLTYLFVSHDLAVV 202
|
250
....*....|....*
gi 1196666485 220 DRLATRSVEIEDGAL 234
Cdd:COG1124 203 AHLCDRVAVMQNGRI 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-235 |
1.52e-28 |
|
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: 113.75 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGD--KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMLAQS------ 74
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSIRTDRKAARqslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 75 PKFN---DNLSVKDALnyelkEIFdARdeyekvlaqisnehdnpellhrqdelVKFIESKDgwnIENKIERILDSFGLRE 151
Cdd:cd03263 81 PQFDalfDELTVREHL-----RFY-AR--------------------------LKGLPKSE---IKEEVELLLRVLGLTD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA--SNQTIVFISHDRYFIDRLATRSVEI 229
Cdd:cd03263 126 KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTHSMDEAEALCDRIAIM 205
|
....*.
gi 1196666485 230 EDGALR 235
Cdd:cd03263 206 SDGKLR 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-264 |
1.81e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.03 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSISIEMLAQS 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 75 PKFNDN--LSVKD--ALNyelkeifdardeyekvlaqisnehdnpelLHRQDELVKFIESKDgwniENKIERILDSFGLR 150
Cdd:COG1121 84 AEVDWDfpITVRDvvLMG-----------------------------RYGRRGLFRRPSRAD----REAVDEALERVGLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHDRYFIDRLATRSV 227
Cdd:COG1121 131 DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVL 210
|
250 260 270
....*....|....*....|....*....|....*..
gi 1196666485 228 EIEDGALrsFDGGYANYLTkkEEILRSLAKSHETLIK 264
Cdd:COG1121 211 LLNRGLV--AHGPPEEVLT--PENLSRAYGGPVALLA 243
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-223 |
2.35e-28 |
|
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: 113.99 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS----------IEMLAQSPKF 77
Cdd:COG1120 7 LSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlLDGRDLAslsrrelarrIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 78 NDNLSVKD--ALnyelkeifdARDEYEKVLAQISnEHDnpellhrqdelvkfieskdgwniENKIERILDSFGLREYENR 155
Cdd:COG1120 87 PFGLTVRElvAL---------GRYPHLGLFGRPS-AED-----------------------REAVEEALERTGLEHLADR 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 156 LVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHD-----RYFiDRLA 223
Cdd:COG1120 134 PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHDlnlaaRYA-DRLV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-232 |
2.61e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 111.34 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNsisiemlaqspkfndnlsv 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 kdalnyelkeiFDARDEYEKVLAQISNEHDNPELLHRqdelvkfieskdgwnienkierildsfgLREYENrlvNSLSGG 163
Cdd:cd03230 62 -----------KDIKKEPEEVKRRIGYLPEEPSLYEN----------------------------LTVREN---LKLSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-234 |
8.69e-28 |
|
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: 111.43 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKI----ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkFNDnlsvk 84
Cdd:cd03255 6 LSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR---------------VDG----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 dalnyelkeiFDARDEYEKVLAQISNEH-----DNPELLHRQD-----ELVKFIESKDGWNIENKIERILDSFGLREYEN 154
Cdd:cd03255 66 ----------TDISKLSEKELAAFRRRHigfvfQSFNLLPDLTalenvELPLLLAGVPKKERRERAEELLERVGLGDRLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRyFIDRLATRSVEIE 230
Cdd:cd03255 136 HYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkeVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELR 214
|
....
gi 1196666485 231 DGAL 234
Cdd:cd03255 215 DGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-232 |
1.51e-27 |
|
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: 110.69 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-----------IRQNSISieMLA 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIG--MVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPKFNDNLSVKDALNYELKEIFDARDEyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIERILDSFGLREY 152
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAE-----------------------------------IRARVRELLELVGLEGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 153 ENRLVNSLSGGEIRRVALG-ALIlKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDRYFIDRLATRSV 227
Cdd:cd03259 124 LNRYPHELSGGQQQRVALArALA-REPSLLLLDEPLSALDAklreELREELKELQRELGITTIYVTHDQEEALALADRIA 202
|
....*
gi 1196666485 228 EIEDG 232
Cdd:cd03259 203 VMNEG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
334-528 |
5.65e-27 |
|
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: 107.48 E-value: 5.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINR-GEIKIGYFDQSRKSISddksl 412
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRIG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ielFCPnggDHIMvrgrnyhVYGYLKnflfPKEFLDkpvgvLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINIL 492
Cdd:cd03230 77 ---YLP---EEPS-------LYENLT----VRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 1196666485 493 EEYLLSF---EGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03230 135 WELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-232 |
1.27e-26 |
|
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: 106.18 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 6 LIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisiemlaqspkfndnlsvkd 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 alnyELKEIFDARDEYEKVLAQISnehdnpellhrqdelvkfieskdgwnienkierildsfglreyenrLVNSLSGGEI 165
Cdd:cd00267 57 ----LIDGKDIAKLPLEELRRRIG----------------------------------------------YVPQLSGGQR 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 166 RRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:cd00267 87 QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELlreLAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-509 |
2.12e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-------NRGEIKIGYFDQSRksi 406
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkppRRARRRIGYVPQRA--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDDKSLielfcPnggdhIMVR-----GRnyhvYGYLKNFLFPK-----------------EFLDKPVGVLSGGEKNRLAL 464
Cdd:COG1121 85 EVDWDF-----P-----ITVRdvvlmGR----YGRRGLFRRPSradreavdealervgleDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLDIATINILEEYL--LSFEG-AILIVSHD 509
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLreLRREGkTILVVTHD 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-527 |
4.36e-26 |
|
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: 104.63 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgeikigyfdqsrksisddksli 413
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 elfcpnggdHIMVRGRNYHVYgylknflfPKEFLDKPVGV---LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATIN 490
Cdd:cd00267 55 ---------EILIDGKDIAKL--------PLEELRRRIGYvpqLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1196666485 491 ILEEYLLSF--EG-AILIVSHDRYFIDKITNKLWAYENGK 527
Cdd:cd00267 118 RLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-236 |
7.53e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 106.28 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDK----IILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkF 77
Cdd:COG1136 3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL---------------I 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 78 NDnlsvkdalnyelKEIFDARDeyeKVLAQISNEH-----------------DNPELLHRqdelvkfIESKDGWNIENKI 140
Cdd:COG1136 68 DG------------QDISSLSE---RELARLRRRHigfvfqffnllpeltalENVALPLL-------LAGVSRKERRERA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 141 ERILDSFGLREYENRLVNSLSGGEIRRVALG-ALIlKKPDVLLLDEPTNHLD------VymVRFLEELLLASNQTIVFIS 213
Cdd:COG1136 126 RELLERVGLGDRLDHRPSQLSGGQQQRVAIArALV-NRPKLILADEPTGNLDsktgeeV--LELLRELNRELGTTIVMVT 202
|
250 260
....*....|....*....|...
gi 1196666485 214 HDRyFIDRLATRSVEIEDGALRS 236
Cdd:COG1136 203 HDP-ELAARADRVIRLRDGRIVS 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
336-565 |
1.22e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 106.10 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEI-----------KIGYFDQ--- 401
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrQIGVLPDerg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 402 --SRKSIsddKSLIELFCP-NGgdhIMVRGRNYHVYGYLKNFLFPkEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILD 478
Cdd:COG4555 85 lyDRLTV---RENIRYFAElYG---LFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 479 EPTNDLDIATINILEEYLLSF---EGAILIVSHDRYFIDKITNKLWAYENGKIeqIYMEYSEylDIEEELNQlSDIESEL 555
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV--VAQGSLD--ELREEIGE-ENLEDAF 232
|
250
....*....|
gi 1196666485 556 GQSIETKEKQ 565
Cdd:COG4555 233 VALIGSEEGE 242
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-234 |
3.00e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.36 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKF-GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV---------IRQNSI-----SI 68
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrLKRREIpylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 69 EMLAQSPKFNDNLSVkdalnyelkeifdardeYEKV-LAQISNEHDNPEllhrqdelvkfieskdgwnIENKIERILDSF 147
Cdd:COG2884 82 GVVFQDFRLLPDRTV-----------------YENVaLPLRVTGKSRKE-------------------IRRRVREVLDLV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 148 GLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHDRYFIDRLAT 224
Cdd:COG2884 126 GLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrgtTVLIATHDLELVDRMPK 205
|
250
....*....|
gi 1196666485 225 RSVEIEDGAL 234
Cdd:COG2884 206 RVLELEDGRL 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-527 |
3.60e-25 |
|
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: 103.70 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDN--KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFdqSRKSISDDKS 411
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL--SLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 412 LI------ELFCPNGGDHIMVRGRNYH---------VYGYLKNFLFpKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLI 476
Cdd:cd03225 79 LVfqnpddQFFGPTVEEEVAFGLENLGlpeeeieerVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 477 LDEPTNDLDIATINILEEYLLSF--EG-AILIVSHDRYFIDKITNKLWAYENGK 527
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-235 |
3.76e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.45 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 8 EVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS--------IEMLAQSPKFN 78
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQkniealrrIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLSVKDALNYELKeifdardeyekvLAQISNEhdnpellhrqdelvkfieskdgwnienKIERILDSFGLREYENRLVN 158
Cdd:cd03268 85 PNLTARENLRLLAR------------LLGIRKK---------------------------RIDEVLDVVGLKDSAKKKVK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHDRYFIDRLATRSVEIEDGALR 235
Cdd:cd03268 126 GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILslrDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-516 |
3.83e-25 |
|
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: 103.77 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-------RGEIKIGYFDQsRKSI 406
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkpleKERKRIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDDkslielFCPNGGDHIMVrGRnyhvYGYLKNFLFPK-----------------EFLDKPVGVLSGGEKNRLALALLFT 469
Cdd:cd03235 80 DRD------FPISVRDVVLM-GL----YGHKGLFRRLSkadkakvdealervglsELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 470 KEYDCLILDEPTNDLDIATINILEEYL--LSFEG-AILIVSHD----RYFIDKI 516
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLreLRREGmTILVVTHDlglvLEYFDRV 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-528 |
5.41e-25 |
|
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: 104.36 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI----------NRGEI--KIGYF 399
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaslSRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 400 DQSRkSISDDKSLIELfcpnggdhiMVRGRnyhvYGYLKNFLFPKE-----------------FLDKPVGVLSGGEKNRL 462
Cdd:COG1120 81 PQEP-PAPFGLTVREL---------VALGR----YPHLGLFGRPSAedreaveealertglehLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 463 ALALLFTKEYDCLILDEPTNDLDIA----TINILEEyLLSFEG-AILIVSHD-----RYFidkitNKLWAYENGKI 528
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR-LARERGrTVVMVLHDlnlaaRYA-----DRLVLLKDGRI 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-232 |
9.78e-25 |
|
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: 102.97 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-----------------IRQNsi 66
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaelyrLRRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 67 sIEMLAQSPKFNDNLSVKDALNYELKEifdardeyekvlaqisnehdnpellHRQDELvkfieskdgWNIENKIERILDS 146
Cdd:cd03261 79 -MGMLFQSGALFDSLTVFENVAFPLRE-------------------------HTRLSE---------EEIREIVLEKLEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 147 FGLREYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFISHDRYFIDR 221
Cdd:cd03261 124 VGLRGAEDLYPAELSGGMKKRVALArALALD-PELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFA 202
|
250
....*....|.
gi 1196666485 222 LATRSVEIEDG 232
Cdd:cd03261 203 IADRIAVLYDG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-528 |
1.13e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.36 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGyfDQSRKSISDDKSL- 412
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA--SLSPKELARKIAYv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ---IELFcpnGGDHimvrgrnyhvygylknflfpkeFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA-- 487
Cdd:cd03214 79 pqaLELL---GLAH----------------------LADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhq 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 488 --TINILEEYLLSFEGAILIVSHD-----RYFidkitNKLWAYENGKI 528
Cdd:cd03214 134 ieLLELLRRLARERGKTVVMVLHDlnlaaRYA-----DRVILLKDGRI 176
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
1.33e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 103.25 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKF----GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSISIE 69
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptSGEVLVD-GKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 70 MLAQspkfNDNL----SVKD--ALNYELKEIfdARDEYEKvlaqisnehdnpellhrqdelvkfieskdgwnienKIERI 143
Cdd:COG1116 84 VVFQ----EPALlpwlTVLDnvALGLELRGV--PKAERRE-----------------------------------RAREL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 144 LDSFGLREYENRLVNSLSGGEIRRVALG-ALILkKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDryf 218
Cdd:COG1116 123 LELVGLAGFEDAYPHQLSGGMRQRVAIArALAN-DPEVLLMDEPFGALDAltreRLQDELLRLWQETGKTVLFVTHD--- 198
|
250
....*....|
gi 1196666485 219 ID---RLATR 225
Cdd:COG1116 199 VDeavFLADR 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-528 |
1.52e-24 |
|
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: 102.41 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTI-DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI----------NRGEI--KIGY- 398
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkkNLRELrrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 F----DQsrksisddkslieLFCPNGGDHIMvrgrnyhvYGyLKNFLFPKE-----------------FLDKPVGVLSGG 457
Cdd:COG1122 81 FqnpdDQ-------------LFAPTVEEDVA--------FG-PENLGLPREeirerveealelvglehLADRPPHELSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 458 EKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL--LSFEG-AILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLkrLNKEGkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-215 |
2.01e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 100.59 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisiemlaqspKFNDnlsvKDALN 88
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---------------LLDG----KDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YELKEIfdARdeYEKVLAQIsnehdnpellhrqdelvkfieskdgwnienkieriLDSFGLREYENRLVNSLSGGEIRRV 168
Cdd:cd03214 66 LSPKEL--AR--KIAYVPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRV 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 169 ALGALILKKPDVLLLDEPTNHLDV-YMVRFLE---ELLLASNQTIVFISHD 215
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIaHQIELLEllrRLARERGKTVVMVLHD 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-254 |
2.29e-24 |
|
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: 102.37 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-----------------IRQN 64
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglsekelyeLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 65 sisIEMLAQSPKFNDNLSVKDALNYELKEIFD-ARDEyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIERI 143
Cdd:COG1127 84 ---IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAE-----------------------------------IRELVLEK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 144 LDSFGLREYENRLVNSLSGGEIRRVALG-ALILkKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYF 218
Cdd:COG1127 126 LELVGLPGAADKMPSELSGGMRKRVALArALAL-DPEILLYDEPTAGLDPITSAVIDELIRELRDelglTSVVVTHDLDS 204
|
250 260 270
....*....|....*....|....*....|....*.
gi 1196666485 219 IDRLATRSVEIEDGALRsFDGgyanyltKKEEILRS 254
Cdd:COG1127 205 AFAIADRVAVLADGKII-AEG-------TPEELLAS 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
334-509 |
4.12e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 101.29 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI---------NRGEIK--IGYfdqs 402
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvarDPAEVRrrIGY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 rksISDDKSLIELFcpNGGDHIMVRGRNYH---------VYGYLKNF-LfpKEFLDKPVGVLSGGEKNRLALALLFTKEY 472
Cdd:COG1131 78 ---VPQEPALYPDL--TVRENLRFFARLYGlprkearerIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1196666485 473 DCLILDEPTNDLDIATINILEEYLLSF--EG-AILIVSHD 509
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-215 |
8.92e-24 |
|
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: 99.92 E-value: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSISIEMLAQSPKFNDN- 80
Cdd:cd03235 5 LTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkptSGSIRVF-GKPLEKERKRIGYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 -LSVKDALnyelkeifdardeyekvlaqisnehdnpeLLHRQDELVKF-IESKDGWNienKIERILDSFGLREYENRLVN 158
Cdd:cd03235 84 pISVRDVV-----------------------------LMGLYGHKGLFrRLSKADKA---KVDEALERVGLSELADRQIG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHD 215
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRelrREGMTILVVTHD 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-215 |
1.11e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.84 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG-EcEIDSGRVI----RQNSIS-----IEM 70
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlE-DPTSGEILiggrDVTDLPpkdrnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVKDALNYELKeifdardeyekvLAQISnehdnpellhrQDElvkfieskdgwnIENKIERILDSFGLR 150
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLK------------LRKVP-----------KAE------------IDRRVREAAELLGLE 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALG-ALIlKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHD 215
Cdd:COG3839 125 DLLDRKPKQLSGGQRQRVALGrALV-REPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-225 |
1.22e-23 |
|
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: 99.47 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDK----IILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSISIEMLA 72
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIaglerptSGEVLVD-GEPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QspkfNDNL----SVKD--ALNYELKEIfDARDEYEKVlaqisnehdnpellhrqdelvkfieskdgwnienkiERILDS 146
Cdd:cd03293 80 Q----QDALlpwlTVLDnvALGLELQGV-PKAEARERA------------------------------------EELLEL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 147 FGLREYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVYMVRFLEELLLA----SNQTIVFISHDryfID- 220
Cdd:cd03293 119 VGLSGFENAYPHQLSGGMRQRVALArALAVD-PDVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD---IDe 194
|
....*..
gi 1196666485 221 --RLATR 225
Cdd:cd03293 195 avFLADR 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-232 |
1.62e-23 |
|
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: 98.03 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-------------IRQNSISIEM 70
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVKDalnyelkeifdardeyekvlaqisnehdnpellhrqdelvkfieskdgwNIenkierildSFGLr 150
Cdd:cd03229 81 VFQDFALFPHLTVLE-------------------------------------------------NI---------ALGL- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 eyenrlvnslSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYFIDRLATRS 226
Cdd:cd03229 102 ----------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRV 171
|
....*.
gi 1196666485 227 VEIEDG 232
Cdd:cd03229 172 VVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
3.29e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 101.33 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS--------IEML 71
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlLDGRDVTglppekrnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 72 AQS----PkfndNLSVKDALNYELKEIFDARDEyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIERILDSF 147
Cdd:COG3842 83 FQDyalfP----HLTVAENVAFGLRMRGVPKAE-----------------------------------IRARVAELLELV 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 148 GLREYENRLVNSLSGGEIRRVALG-ALIlKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDR 216
Cdd:COG3842 124 GLEGLADRYPHQLSGGQQQRVALArALA-PEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-214 |
3.81e-23 |
|
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: 99.00 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGE--------CEI---DSGRV----IRQNs 65
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygndVRLfgeRRGGEdvweLRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 66 I---SIEMLAQspkFNDNLSVKDALnyelkeifdardeyekvlaqISNEHDNPELLHRQDElvkfieskdgwNIENKIER 142
Cdd:COG1119 80 IglvSPALQLR---FPRDETVLDVV--------------------LSGFFDSIGLYREPTD-----------EQRERARE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 143 ILDSFGLREYENRLVNSLSGGEIRRVALG-ALIlKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISH 214
Cdd:COG1119 126 LLELLGLAHLADRPFGTLSQGEQRRVLIArALV-KDPELLILDEPTAGLDLGarelLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-188 |
5.49e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.41 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQN-----------SISIEMLAQSPKFNDNLSVKDAL 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 88 NYELKEIFDARDEYekvlaqisnehdnpellhrqdelvkfieskdgwniENKIERILDSFGLREYENRLV----NSLSGG 163
Cdd:pfam00005 81 RLGLLLKGLSKREK-----------------------------------DARAEEALEKLGLGDLADRPVgerpGTLSGG 125
|
170 180
....*....|....*....|....*
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTN 188
Cdd:pfam00005 126 QRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
310-539 |
9.01e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.84 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 310 LELERASKSFNGGGLNQNRKKMLFECKNLSKTIDNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWAL-KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 390 NRgeikigyfdqsRKSISddkSLIEL---FCPN--GGDHIMVRGRnyhVYGYLKNF---LFPK--------EFLDKPVGV 453
Cdd:COG1134 84 EV-----------NGRVS---ALLELgagFHPEltGRENIYLNGR---LLGLSRKEideKFDEivefaelgDFIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 454 LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA----TINILEEYLLSfEGAILIVSHDRYFIDKITNK-LW-----AY 523
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRaIWlekgrLV 225
|
250
....*....|....*.
gi 1196666485 524 ENGKIEQIYMEYSEYL 539
Cdd:COG1134 226 MDGDPEEVIAAYEALL 241
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-235 |
9.37e-23 |
|
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: 102.54 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIE------------MLAQSPK-FN-- 78
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS-ITLGGVDLRdldeddlrrriaVVPQRPHlFDtt 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 --DNLSVKDAlnyelkeifDARDEyekvlaqisnehdnpELLH--RQDELVKFIES-KDGWNienkieRILDSFGLReye 153
Cdd:COG4987 425 lrENLRLARP---------DATDE---------------ELWAalERVGLGDWLAAlPDGLD------TWLGEGGRR--- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 154 nrlvnsLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVR-FLEELL-LASNQTIVFISHDRYFIDRlATRSVEIED 231
Cdd:COG4987 472 ------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLeALAGRTVLLITHRLAGLER-MDRILVLED 544
|
....
gi 1196666485 232 GALR 235
Cdd:COG4987 545 GRIV 548
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-540 |
4.49e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 100.58 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTID-NKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeLEADSGvinrGE------IKIGYFDQSRK---- 404
Cdd:PRK11819 10 NRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFE----GEarpapgIKVGYLPQEPQldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 405 ---------SISDDKSLIELFcpnggDHIMVrgrnyhvygylkNFLFPKEFLDK-------------------------- 449
Cdd:PRK11819 85 ktvrenveeGVAEVKAALDRF-----NEIYA------------AYAEPDADFDAlaaeqgelqeiidaadawdldsqlei 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 450 ------------PVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFIDKIT 517
Cdd:PRK11819 148 amdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVA 227
|
250 260
....*....|....*....|....*
gi 1196666485 518 NklWAYENGKIEQIYME--YSEYLD 540
Cdd:PRK11819 228 G--WILELDRGRGIPWEgnYSSWLE 250
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-239 |
5.03e-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: 94.57 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVnEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSIS-----------IEMLA 72
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGT-IRIDGQDvlkqpqklrrrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPKFNDNLSVKDALNYelkeifdardeyekvLAqisnehdnpellhrqdeLVKFIESKDgwnIENKIERILDSFGLREY 152
Cdd:cd03264 79 QEFGVYPNFTVREFLDY---------------IA-----------------WLKGIPSKE---VKARVDEVLELVNLGDR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 153 ENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV-YMVRFLeELL--LASNQTIVFISHDRYFIDRLATRSVEI 229
Cdd:cd03264 124 AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeERIRFR-NLLseLGEDRIVILSTHIVEDVESLCNQVAVL 202
|
250
....*....|
gi 1196666485 230 EDGALRsFDG 239
Cdd:cd03264 203 NKGKLV-FEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-223 |
5.52e-22 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 99.98 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKF-----GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV--------------IRQ 63
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 64 NSISIEMLAQSPK--FNDNLSVKDALNYELKeifdardeyekvlaqisnehdnpelLHRQdelvkfiesKDGWNIENKIE 141
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGDIIAEPLR-------------------------LHGL---------LSRAERRERVA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 142 RILDSFGL-REYENRLVNSLSGGEIRRVAL-GALILKkPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHD 215
Cdd:COG1123 386 ELLERVGLpPDLADRYPHELSGGQRQRVAIaRALALE-PKLLILDEPTSALDVSvqaqILNLLRDLQRELGLTYLFISHD 464
|
250
....*....|..
gi 1196666485 216 ----RYFIDRLA 223
Cdd:COG1123 465 lavvRYIADRVA 476
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-234 |
1.53e-21 |
|
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: 93.09 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKI-ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------RQNSISIEMLAQSPkfND 79
Cdd:cd03226 5 ISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpikaKERRKSIGYVMQDV--DY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 NL---SVKDALNYELKEIFDArdeyekvlaqisnehdnpellhrqdelvkfieskdgwniENKIERILDSFGLREYENRL 156
Cdd:cd03226 83 QLftdSVREELLLGLKELDAG---------------------------------------NEQAETVLKDLDLYALKERH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISHDRYFIDRLATRSVEIEDGA 233
Cdd:cd03226 124 PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
.
gi 1196666485 234 L 234
Cdd:cd03226 204 I 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-235 |
3.04e-21 |
|
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: 92.32 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI---------RQNSISIEMLAQS 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 75 PKFNDNLSVKDALNYELKeifdardeyekvlaqisnehdnpelLHRQDELvkfieskdgwNIENKIERILDSFGLREYEN 154
Cdd:cd03301 81 YALYPHMTVYDNIAFGLK-------------------------LRKVPKD----------EIDERVREVAELLQIEHLLD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVyMVRF-----LEELLLASNQTIVFISHDRYFIDRLATRSVEI 229
Cdd:cd03301 126 RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA-KLRVqmraeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
....*.
gi 1196666485 230 EDGALR 235
Cdd:cd03301 205 NDGQIQ 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
310-531 |
4.48e-21 |
|
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: 92.21 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 310 LELERASKSFNGGGLNQNRKKMLFECKNLSKTIDNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWAL-KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 390 NRgeikigyfdqsRKSISddkSLIEL---FCPN--GGDHIMVRGRnyhVYGYLKNFLFPK-----------EFLDKPVGV 453
Cdd:cd03220 80 TV-----------RGRVS---SLLGLgggFNPEltGRENIYLNGR---LLGLSRKEIDEKideiiefselgDFIDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 454 LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT----INILEEyLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIE 529
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFqekcQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
..
gi 1196666485 530 QI 531
Cdd:cd03220 222 FD 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
357-482 |
5.11e-21 |
|
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: 90.01 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEI------------KIGYFDQ-----SRKSISDDKSLIELFCPN 419
Cdd:pfam00005 10 PGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkEIGYVFQdpqlfPRLTVRENLRLGLLLKGL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 420 GGDHImvRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTN 482
Cdd:pfam00005 90 SKREK--DARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-225 |
5.12e-21 |
|
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: 92.50 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI---------RQNSISIEMLA---QSPK 76
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglPPHEIARLGIGrtfQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 FNDNLSVKDALnyelkeifdardeyeKVLAQISNEHDNPELLHRQDELVkfieskdgwnIENKIERILDSFGLREYENRL 156
Cdd:cd03219 86 LFPELTVLENV---------------MVAAQARTGSGLLLARARREERE----------ARERAEELLERVGLADLADRP 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPT---NHLDVY-MVRFLEElLLASNQTIVFISHDRYFIDRLATR 225
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLADR 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-508 |
5.45e-21 |
|
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: 90.52 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDN--KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSIsdd 409
Cdd:cd03228 2 EFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 410 kslielfcpnggdhimvrgrnyhvyGYL--KNFLFPKEFLDKpvgVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA 487
Cdd:cd03228 79 -------------------------AYVpqDPFLFSGTIREN---ILSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|...
gi 1196666485 488 TINILEEYLLSFEG--AILIVSH 508
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-223 |
5.97e-21 |
|
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: 91.80 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKI----ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSI------------ 66
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 67 --SIEMLAQSP--KFNDNLSVKDALnyelKEIFdardeyekvlaqisnehdnpellhrqdeLVKFIESKDgWNIENKIER 142
Cdd:cd03257 81 rkEIQMVFQDPmsSLNPRMTIGEQI----AEPL----------------------------RIHGKLSKK-EARKEAVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 143 ILDSFGL-REYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFISHD- 215
Cdd:cd03257 128 LLVGVGLpEEVLNRYPHELSGGQRQRVAIArALALN-PKLLIADEPTSALDVSVQAQILDLLKklqeELGLTLLFITHDl 206
|
250
....*....|.
gi 1196666485 216 ---RYFIDRLA 223
Cdd:cd03257 207 gvvAKIADRVA 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-232 |
6.41e-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: 91.57 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNS-ISIEmlaqspkfndnls 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpLDIA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYELKEifdaRDEYEKVlaQIsnehdnpellhrQDELVKFIESKdGWNIE---NKIERILDSFGLREYENRLVNS 159
Cdd:cd03269 68 ARNRIGYLPEE----RGLYPKM--KV------------IDQLVYLAQLK-GLKKEearRRIDEWLERLELSEYANKRVEE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-239 |
8.21e-21 |
|
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: 91.86 E-value: 8.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGD-KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkFNDNls 82
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL---------------IDGT-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vkDALNYELKEIFDARdeyekvlAQISNEHDNPELLHRQDEL----------VKFIESKDGWNIENKIER---ILDSFGL 149
Cdd:cd03256 64 --DINKLKGKALRQLR-------RQIGMIFQQFNLIERLSVLenvlsgrlgrRSTWRSLFGLFPKEEKQRalaALERVGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 150 REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYFIDRLATR 225
Cdd:cd03256 135 LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQVDLAREYADR 214
|
250
....*....|....
gi 1196666485 226 SVEIEDGALrSFDG 239
Cdd:cd03256 215 IVGLKDGRI-VFDG 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-235 |
1.02e-20 |
|
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: 91.28 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSI----SIEMLAQ 73
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdVVREPRevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 SPkfndnlSVKDALN-YELKEIFdardeyekvlAQISNehdnpellhrqdelVKFIESKdgwnieNKIERILDSFGLREY 152
Cdd:cd03265 81 DL------SVDDELTgWENLYIH----------ARLYG--------------VPGAERR------ERIDELLDFVGLLEA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 153 ENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVE 228
Cdd:cd03265 125 ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPqtraHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAI 204
|
....*..
gi 1196666485 229 IEDGALR 235
Cdd:cd03265 205 IDHGRII 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-244 |
3.43e-20 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 94.85 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQspkfndnls 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vkdalnYELkeifdardEYEKVlaqisnehDNPELLHrqdeLVKFIESKdgwnIENKIERILDSFGLR-EYENRLVNSLS 161
Cdd:PRK10636 383 ------HQL--------EFLRA--------DESPLQH----LARLAPQE----LEQKLRDYLGGFGFQgDKVTEETRRFS 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFDGGY 241
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDL 512
|
...
gi 1196666485 242 ANY 244
Cdd:PRK10636 513 EDY 515
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-232 |
3.76e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.13 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkFND---- 79
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV---------------LNGrdlf 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 -NLSVKD------ALNYELkeiFdardeyekvlaqisnEH----DNpellhrqdelVKF-----IESKDgwNIENKIERI 143
Cdd:COG1118 68 tNLPPRErrvgfvFQHYAL---F---------------PHmtvaEN----------IAFglrvrPPSKA--EIRARVEEL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 144 LDSFGLREYENRLVNSLSGGEIRRVALG-ALILkKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDR-- 216
Cdd:COG1118 118 LELVQLEGLADRYPSQLSGGQRQRVALArALAV-EPEVLLLDEPFGALDAKvrkeLRRWLRRLHDELGGTTVFVTHDQee 196
|
250
....*....|....*..
gi 1196666485 217 -YfidRLATRSVEIEDG 232
Cdd:COG1118 197 aL---ELADRVVVMNQG 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-215 |
6.27e-20 |
|
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: 89.22 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS--------IEMLAQS 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlLDGKDITnlpphkrpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 75 PKFNDNLSVKDALNYELKeifdardeyekvlaqisnehdnpellhrqdelvkfIESKDGWNIENKIERILDSFGLREYEN 154
Cdd:cd03300 81 YALFPHLTVFENIAFGLR-----------------------------------LKKLPKAEIKERVAEALDLVQLEGYAN 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHD 215
Cdd:cd03300 126 RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-529 |
7.05e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 89.48 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLfECKNLSKTIDNK-----VLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGY------- 398
Cdd:COG1124 1 ML-EVRNLSVSYGQGgrrvpVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrrkafr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 ------FDQS------RKSIsdDKSLIELFCPNGGDHIMVRgrnyhVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALAL 466
Cdd:COG1124 79 rrvqmvFQDPyaslhpRHTV--DRILAEPLRIHGLPDREER-----IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 467 LFTKEYDCLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIE 529
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
334-528 |
7.23e-20 |
|
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: 88.43 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgEIKIGYFDQSRKSISDDKSLI 413
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 EL--FCPN--GGDHIMVRGRnyhVYGYLKNFLfpKEFLD---------KPVGVLSGGEKNRLALALLFTKEYDCLILDEP 480
Cdd:cd03268 79 EApgFYPNltARENLRLLAR---LLGIRKKRI--DEVLDvvglkdsakKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 481 TNDLDIATINILEEYLLS---FEGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03268 154 TNGLDPDGIKELRELILSlrdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-232 |
7.44e-20 |
|
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: 88.36 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV----------------IRQNsis 67
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkknineLRQK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 IEMLAQSpkFN--DNLSVKDALnyelkeifdardeyekVLAQIsnehdnpELLHRQDELVkfieskdgwniENKIERILD 145
Cdd:cd03262 78 VGMVFQQ--FNlfPHLTVLENI----------------TLAPI-------KVKGMSKAEA-----------EERALELLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 146 SFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LA-SNQTIVFISHDRYFIDRL 222
Cdd:cd03262 122 KVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMkdLAeEGMTMVVVTHEMGFAREV 201
|
250
....*....|
gi 1196666485 223 ATRSVEIEDG 232
Cdd:cd03262 202 ADRVIFMDDG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-234 |
2.30e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 87.08 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKII-LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGrVIRQNSISIEML--AQSPKFNDN 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG-TIRVNGQDVSDLrgRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 LSVkdalnyelkeIFdardeyekvlaqisneHDNPELLHRQD-ELVKF---IESKDGWNIENKIERILDSFGLREYENRL 156
Cdd:cd03292 80 IGV----------VF----------------QDFRLLPDRNVyENVAFaleVTGVPPREIRKRVPAALELVGLSHKHRAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHDRYFIDRLATRSVEIEDGA 233
Cdd:cd03292 134 PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGK 213
|
.
gi 1196666485 234 L 234
Cdd:cd03292 214 L 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
343-530 |
2.80e-19 |
|
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: 91.74 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSIS---------DDkS 411
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAwvpqnpylfAG-T 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 412 LIE---LFCPNGGDHIMVRG-RNYHVYGYLKNFlfPKEfLDKPVGV----LSGGEKNRLALALLFTKEYDCLILDEPTND 483
Cdd:COG4988 427 IREnlrLGRPDASDEELEAAlEAAGLDEFVAAL--PDG-LDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 484 LDIATINILEEYLLS-FEG-AILIVSHDRYFI---DKItnklWAYENGKIEQ 530
Cdd:COG4988 504 LDAETEAEILQALRRlAKGrTVILITHRLALLaqaDRI----LVLDDGRIVE 551
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-232 |
3.38e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.12 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSisiEMLAQSPK-------FNDN-----LSVKD----A 86
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ---DLTALPPAerpvsmlFQENnlfphLTVAQniglG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 87 LNYELKeifdardeyekvlaqisnehdnpelLHRQDElvkfieskdgwnieNKIERILDSFGLREYENRLVNSLSGGEIR 166
Cdd:COG3840 96 LRPGLK-------------------------LTAEQR--------------AQVEQALERVGLAGLLDRLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 167 RVALG-ALILKKPdVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDryfID---RLATRSVEIEDG 232
Cdd:COG3840 137 RVALArCLVRKRP-ILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVLLVADG 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
4.01e-19 |
|
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: 87.40 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIEMLA-------- 72
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDITGLPphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 -----QSPKFNDNLSVKD----ALNYELKEIFdardeyekvlaqISNEHDNPELLHRQDELVKfieskdgwnienKIERI 143
Cdd:COG0411 81 iartfQNPRLFPELTVLEnvlvAAHARLGRGL------------LAALLRLPRARREEREARE------------RAEEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 144 LDSFGLREYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPT---NHLDV-YMVRFLEELLLASNQTIVFISHDRYF 218
Cdd:COG0411 137 LERVGLADRADEPAGNLSYGQQRRLEIArALATE-PKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDL 215
|
....*..
gi 1196666485 219 IDRLATR 225
Cdd:COG0411 216 VMGLADR 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-232 |
4.09e-19 |
|
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: 91.82 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGD--KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSI-----SIEM 70
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidLRQIDPaslrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPK-FN----DNLSVKDAlNYELKEIFDArdeyekvlAQISNEHDnpellhrqdelvkFIESkdgwnIENKIERILD 145
Cdd:COG2274 554 VLQDVFlFSgtirENITLGDP-DATDEEIIEA--------ARLAGLHD-------------FIEA-----LPMGYDTVVG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 146 SFGlreyenrlvNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLlaSNQTIVFISHDRYFIdR 221
Cdd:COG2274 607 EGG---------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAeteaIILENLRRLL--KGRTVIIIAHRLSTI-R 674
|
250
....*....|.
gi 1196666485 222 LATRSVEIEDG 232
Cdd:COG2274 675 LADRIIVLDKG 685
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
5.61e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKF-GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMLAQSPKFn 78
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlIRGEPITKENIREVRKF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 dnlsVKDALNYELKEIFDARDEYEKVLAQISNEHDNPELLHRQDELVKFIeskdgwnienkierildsfGLREYENRLVN 158
Cdd:PRK13652 80 ----VGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-------------------GLEELRDRVPH 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFIDRLA 223
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQgvkeLIDFLNDLPETYGMTVIFSTHQLDLVPEMA 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-238 |
5.78e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 11 KKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSIS--IEMLAqspKFNDNLSVKDalN 88
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalLELGA---GFHPELTGRE--N 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YELKeifdardeyekvlAQISNehdnpelLHRQDelvkfieskdgwnIENKIERILDsF-GLREYENRLVNSLSGGEIRR 167
Cdd:COG1134 109 IYLN-------------GRLLG-------LSRKE-------------IDEKFDEIVE-FaELGDFIDQPVKTYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 168 VALGALILKKPDVLLLDEptnhldVYMV---RF-------LEElLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSF 237
Cdd:COG1134 155 LAFAVATAVDPDILLVDE------VLAVgdaAFqkkclarIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
.
gi 1196666485 238 D 238
Cdd:COG1134 228 G 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-234 |
6.71e-19 |
|
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: 90.59 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisiemlaqspKFNDNlsvkdalnyELKE 93
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI---------------LINGV---------DLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 IfdARDEYEKVLAQISNehdNPELLH---RQdelvkfieskdgwNI--------ENKIERILDSFGLREYENRLVN---- 158
Cdd:COG4988 404 L--DPASWRRQIAWVPQ---NPYLFAgtiRE-------------NLrlgrpdasDEELEAALEAAGLDEFVAALPDgldt 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 159 -------SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEEllLASNQTIVFISHDRYFIdRLATRSV 227
Cdd:COG4988 466 plgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAeteaEILQALRR--LAKGRTVILITHRLALL-AQADRIL 542
|
....*..
gi 1196666485 228 EIEDGAL 234
Cdd:COG4988 543 VLDDGRI 549
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-238 |
7.41e-19 |
|
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: 85.66 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISiEMLAQSPKFNDNLSVKDalnyelke 93
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-SLLGLGGGFNPELTGRE-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 ifdardeyekvlaqisNEHDNPELL-HRQDElvkfieskdgwnIENKIERILDSFGLREYENRLVNSLSGGEIRRVALGA 172
Cdd:cd03220 104 ----------------NIYLNGRLLgLSRKE------------IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 173 LILKKPDVLLLDEPTNHLDVY----MVRFLEElLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFD 238
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAfqekCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-527 |
2.15e-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: 83.01 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigYFDQsrKSISDDKSL 412
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI--------LIDG--EDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 IELFCPNGGdhiMVrgrnyhvygyLKNF-LFP-KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATIN 490
Cdd:cd03229 71 LPPLRRRIG---MV----------FQDFaLFPhLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1196666485 491 ILEEYLLS----FEGAILIVSHDRYFIDKITNKLWAYENGK 527
Cdd:cd03229 138 EVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-316 |
3.22e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.55 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMLAQ--------- 73
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlWDGEPLDPEDRRRigylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 -SPKfndnLSVKDALNYelkeifdardeyekvLAQisnehdnpelLH---RQDelvkfieskdgwnIENKIERILDSFGL 149
Cdd:COG4152 82 lYPK----MKVGEQLVY---------------LAR----------LKglsKAE-------------AKRRADEWLERLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 150 REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHDRYFIDRLATRS 226
Cdd:COG4152 120 GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRelaAKGTTVIFSSHQMELVEELCDRI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 227 VEIEDGALRsFDGgyanyltKKEEILRSLAKSHETLIknLKSEEEWLR----------RGVKARLK-RNEGRKQRILAmr 295
Cdd:COG4152 200 VIINKGRKV-LSG-------SVDEIRRQFGRNTLRLE--ADGDAGWLRalpgvtvveeDGDGAELKlEDGADAQELLR-- 267
|
330 340
....*....|....*....|.
gi 1196666485 296 eEAKKNpGLIRRvkLELERAS 316
Cdd:COG4152 268 -ALLAR-GPVRE--FEEVRPS 284
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-236 |
4.38e-18 |
|
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: 83.50 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 6 LIEVSKKFGDKIIlnETNFNVNEkERIAIIGKNGGGKSTLMKILRGECEIDSGRVI---------RQNSI------SIEM 70
Cdd:cd03297 3 CVDIEKRLPDFTL--KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsRKKINlppqqrKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVKDALNYELKEifdardeyekvlaqisneHDNPELLHRQDElvkfieskdgwnienkierILDSFGLR 150
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKR------------------KRNREDRISVDE-------------------LLDLLGLD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYM----VRFLEELLLASNQTIVFISHDRYFIDRLATRS 226
Cdd:cd03297 123 HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRI 202
|
250
....*....|
gi 1196666485 227 VEIEDGALRS 236
Cdd:cd03297 203 VVMEDGRLQY 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-225 |
5.24e-18 |
|
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: 84.00 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 10 SKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQN-SISIEMLAQSPKFNdnLSVKDALN 88
Cdd:cd03237 6 MKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYE--GTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YELKeifdarDEYEKvlAQISNEHDNPEllhrqdelvkfieskdgwnienKIERILDsfglreyenRLVNSLSGGEIRRV 168
Cdd:cd03237 84 SITK------DFYTH--PYFKTEIAKPL----------------------QIEQILD---------REVPELSGGELQRV 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 169 ALGALILKKPDVLLLDEPTNHLDV---YMV-RFLEELLLASNQTIVFISHDRYFIDRLATR 225
Cdd:cd03237 125 AIAACLSKDADIYLLDEPSAYLDVeqrLMAsKVIRRFAENNEKTAFVVEHDIIMIDYLADR 185
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
332-516 |
5.61e-18 |
|
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: 83.32 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLF----SDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG-VINRGEIKIGYFDQSRKSI 406
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDD-------------------KSLIELFCPNGGDHIMVRgRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALL 467
Cdd:cd03257 81 RKEiqmvfqdpmsslnprmtigEQIAEPLRIHGKLSKKEA-RKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 468 FTKEYDCLILDEPTNDLDIAT-INILEeyLL-----SFEGAILIVSHD----RYFIDKI 516
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVqAQILD--LLkklqeELGLTLLFITHDlgvvAKIADRV 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-232 |
7.04e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 81.28 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKI--ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvirqnsISIemlaqspkfnDNL 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE------ILI----------DGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKDalnYELKEIFDardeyekvlaQISNEHDNPELLHrqdelvkfieskdgwnienkierilDSfgLREyenrlvNSLS 161
Cdd:cd03228 65 DLRD---LDLESLRK----------NIAYVPQDPFLFS-------------------------GT--IRE------NILS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdRYFIDRLATRSVEIEDG 232
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALraLAKGKTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-237 |
7.98e-18 |
|
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: 85.55 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 7 IEVSKKFGDKIIlnETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnSISIEMLAQSPK---------- 76
Cdd:TIGR02142 3 ARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI----VLNGRTLFDSRKgiflppekrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 ----FND-----NLSVKDALNYELKeifDARDEYEKVlaqisnehdnpellhrqdelvkfieskdgwnienKIERILDSF 147
Cdd:TIGR02142 77 igyvFQEarlfpHLSVRGNLRYGMK---RARPSERRI----------------------------------SFERVIELL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 148 GLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDRYFIDRLA 223
Cdd:TIGR02142 120 GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLA 199
|
250
....*....|....
gi 1196666485 224 TRSVEIEDGALRSF 237
Cdd:TIGR02142 200 DRVVVLEDGRVAAA 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-239 |
9.93e-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: 82.77 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------RQNS----ISIeMLAQSPK 76
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkRRKKflrrIGV-VFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 FNDNLSVKDALNYeLKEIFDARD-EYEKVLAQISnehdnpELLhrqdelvkfieskdgwnienKIERILDSfglreyenr 155
Cdd:cd03267 106 LWWDLPVIDSFYL-LAAIYDLPPaRFKKRLDELS------ELL--------------------DLEELLDT--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 156 LVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYFIDRLATRSVEIED 231
Cdd:cd03267 150 PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVLVIDK 229
|
....*...
gi 1196666485 232 GALrSFDG 239
Cdd:cd03267 230 GRL-LYDG 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-225 |
1.08e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.79 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDkIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNdnLS 82
Cdd:PRK13409 340 LVEYPDLTKKLGD-FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYD--GT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALnyelkeifdardeyEKVLAQISNEHDNPELLHRQdelvkfieskdgwnienKIERILDsfglreyenRLVNSLSG 162
Cdd:PRK13409 417 VEDLL--------------RSITDDLGSSYYKSEIIKPL-----------------QLERLLD---------KNVKDLSG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDV---YMV-----RFLEElllaSNQTIVFISHDRYFIDRLATR 225
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVakairRIAEE----REATALVVDHDIYMIDYISDR 523
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
350-510 |
1.12e-17 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 86.57 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSIS--------DDKSL---IELF 416
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAwvpqhpflFAGTIaenIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 417 CPNGGDHiMVRGRNYHVYgyLKNFL--FPkEFLDKPVGV----LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATIN 490
Cdd:TIGR02857 420 RPDASDA-EIREALERAG--LDEFVaaLP-QGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180
....*....|....*....|..
gi 1196666485 491 ILEEYLLSF-EGAI-LIVSHDR 510
Cdd:TIGR02857 496 EVLEALRALaQGRTvLLVTHRL 517
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-510 |
4.14e-17 |
|
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: 80.61 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKT----IDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-------------NRGEI-- 394
Cdd:cd03255 2 ELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekELAAFrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 395 -KIGYFDQS-----RKSISDDKSLIELFCPNGGDHIMVRGRnyHVYGYLKnfLfpKEFLDKPVGVLSGGEKNRLALALLF 468
Cdd:cd03255 82 rHIGFVFQSfnllpDLTALENVELPLLLAGVPKKERRERAE--ELLERVG--L--GDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1196666485 469 TKEYDCLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSHDR 510
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-225 |
5.01e-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: 84.84 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 26 VNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEmlAQSPKFNDNLSVKDALNYELKEIFDARDEYEkvl 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK--PQYISPDYDGTVEEFLRSANTDDFGSSYYKT--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 106 aqisnehdnpELLHRQdelvkfieskdgwnienKIERILDsfglreyenRLVNSLSGGEIRRVALGALILKKPDVLLLDE 185
Cdd:COG1245 438 ----------EIIKPL-----------------GLEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 186 PTNHLDV---YMV-----RFLEElllaSNQTIVFISHDRYFIDRLATR 225
Cdd:COG1245 482 PSAHLDVeqrLAVakairRFAEN----RGKTAMVVDHDIYLIDYISDR 525
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-234 |
5.96e-17 |
|
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: 80.30 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL------------RGECEIDsGRVIRQNSISIE-- 69
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipgapdEGEVLLD-GKDIYDLDVDVLel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 70 -----MLAQSPK-FNdnLSVKDALNYELKeifdardeyekvlaqISNEHDNPELlhrqDELVkfieskdgwnienkiERI 143
Cdd:cd03260 80 rrrvgMVFQKPNpFP--GSIYDNVAYGLR---------------LHGIKLKEEL----DERV---------------EEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 144 LDSFGLREYENRLVN--SLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHDRYF 218
Cdd:cd03260 124 LRKAALWDEVKDRLHalGLSGGQQQRLCLArALANE-PEVLLLDEPTSALDPISTAKIEELIaeLKKEYTIVIVTHNMQQ 202
|
250
....*....|....*.
gi 1196666485 219 IDRLATRSVEIEDGAL 234
Cdd:cd03260 203 AARVADRTAFLLNGRL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-234 |
6.88e-17 |
|
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: 80.32 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDK----IILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------------RQN 64
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 65 SISIEMLAQspKFNdnlsvkdalnyelkeIFDARDEYEKVlaqisnehdnpellhrqdELVKFIESKDGWNIENKIERIL 144
Cdd:cd03258 81 RRRIGMIFQ--HFN---------------LLSSRTVFENV------------------ALPLEIAGVPKAEIEERVLELL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 145 DSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYFID 220
Cdd:cd03258 126 ELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVK 205
|
250
....*....|....
gi 1196666485 221 RLATRSVEIEDGAL 234
Cdd:cd03258 206 RICDRVAVMEKGEV 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-232 |
7.38e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 80.42 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV----------------IRQNsi 66
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedltdskkdinkLRRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 67 sIEMLAQSpkFN--DNLSVKDALnyelkeifdardeyekVLAQIsnehdnpELLHRqdelvkfieSKDgwNIENKIERIL 144
Cdd:COG1126 79 -VGMVFQQ--FNlfPHLTVLENV----------------TLAPI-------KVKKM---------SKA--EAEERAMELL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 145 DSFGLREYENRLVNSLSGGEIRRVALG-ALILkKPDVLLLDEPTNHLDVYMVRfleELL-----LA-SNQTIVFISHDRY 217
Cdd:COG1126 122 ERVGLADKADAYPAQLSGGQQQRVAIArALAM-EPKVMLFDEPTSALDPELVG---EVLdvmrdLAkEGMTMVVVTHEMG 197
|
250
....*....|....*
gi 1196666485 218 FIDRLATRSVEIEDG 232
Cdd:COG1126 198 FAREVADRVVFMDGG 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-224 |
8.93e-17 |
|
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: 79.97 E-value: 8.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIR---QNSI--SIEMLAQ-SPKFND-- 79
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILID-GQDIRevtLDSLrrAIGVVPQdTVLFNDti 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 -------NLSVKDAlnyelkEIFDArdeyekvlAQISNEHDnpellhrqdelvkFIEskdgwNIENKIERILDSFGLRey 152
Cdd:cd03253 92 gynirygRPDATDE------EVIEA--------AKAAQIHD-------------KIM-----RFPDGYDTIVGERGLK-- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 153 enrlvnsLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT 224
Cdd:cd03253 138 -------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALrdVSKGRTTIVIAH------RLST 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-509 |
1.71e-16 |
|
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: 78.70 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKT--IDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKI-GYFDQS-----RKSIS 407
Cdd:cd03263 4 RNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS-----GTAYInGYSIRTdrkaaRQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 408 ddkslielFCP---------NGGDHI----MVRGRN-----YHVYGYLKNFLFpKEFLDKPVGVLSGGEKNRLALALLFT 469
Cdd:cd03263 79 --------YCPqfdalfdelTVREHLrfyaRLKGLPkseikEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196666485 470 KEYDCLILDEPTNDLDIATINILEEYLLSFEG--AILIVSHD 509
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-232 |
1.91e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGrvirqnsisiEMLAQSPKFNDnlsVKDaln 88
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG----------ELLAGTAPLAE---ARE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 yELKEIF-DARD-EYEKVLaqisnehDNPELLHRQDelvkfieskdgWniENKIERILDSFGLREYENRLVNSLSGGEIR 166
Cdd:PRK11247 82 -DTRLMFqDARLlPWKKVI-------DNVGLGLKGQ-----------W--RDAALQALAAVGLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 167 RVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
344-529 |
1.94e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 77.74 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 344 NKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIG-YFDQSRKSISDDKSLIELFCPNGGD 422
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdLEKALSSLISVLNQRPYLFDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 423 HIMVRgrnyhvygylknflfpkefldkpvgvLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSF--E 500
Cdd:cd03247 94 NLGRR--------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkD 147
|
170 180
....*....|....*....|....*....
gi 1196666485 501 GAILIVSHDRYFIDKItNKLWAYENGKIE 529
Cdd:cd03247 148 KTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-239 |
2.27e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.56 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDK----IILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvirqnsISIEML--AQSPk 76
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF------ATVDGFdvVKEP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 fndnLSVKDALNYelkeIFDARDEYEKVLAQisnehdnpellhrqdELVKF---IESKDGWNIENKIERILDSFGLREYE 153
Cdd:cd03266 74 ----AEARRRLGF----VSDSTGLYDRLTAR---------------ENLEYfagLYGLKGDELTARLEELADRLGMEELL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISHDRYFIDRLATRSVEIE 230
Cdd:cd03266 131 DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFirqLRALGKCILFSTHIMQEVERLCDRVVVLH 210
|
....*....
gi 1196666485 231 DGALRsFDG 239
Cdd:cd03266 211 RGRVV-YEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
336-528 |
2.77e-16 |
|
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: 78.00 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGeRIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIG-YFDQSRKSISddkslie 414
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkQPQKLRRRIG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 415 lFCPNggdHIMVRgRNYHVYGYLKNFLFPK---------------------EFLDKPVGVLSGGEKNRLALALLFTKEYD 473
Cdd:cd03264 76 -YLPQ---EFGVY-PNFTVREFLDYIAWLKgipskevkarvdevlelvnlgDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 474 CLILDEPTNDLD----IATINILEEylLSfEGAILIVS-HDRYFIDKITNKLWAYENGKI 528
Cdd:cd03264 151 ILIVDEPTAGLDpeerIRFRNLLSE--LG-EDRIVILStHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
357-524 |
2.89e-16 |
|
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: 78.99 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQsrKSISDDKSLIELFcpnggdhIMVRGRNYHVYGY 436
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ--YIKADYEGTVRDL-------LSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 437 LK----NFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD----IATINILEEYLLSFEGAILIVSH 508
Cdd:cd03237 95 FKteiaKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEH 174
|
170
....*....|....*.
gi 1196666485 509 DRYFIDKITNKLWAYE 524
Cdd:cd03237 175 DIIMIDYLADRLIVFE 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
354-528 |
3.69e-16 |
|
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: 78.02 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 354 RVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSIS---DDKSL--------IELFCPNG 420
Cdd:cd03245 26 TIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGyvpQDVTLfygtlrdnITLGAPLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 421 GDHIMVRGRNyhvYGYLKNFL--FPKEFlDKPVG----VLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEE 494
Cdd:cd03245 106 DDERILRAAE---LAGVTDFVnkHPNGL-DLQIGergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKE 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1196666485 495 YLLSFEG--AILIVSHdRYFIDKITNKLWAYENGKI 528
Cdd:cd03245 182 RLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
4.25e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.25 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILR------------GECEIDSGRVIRQNSISI 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 69 EMLAQSPKF---NDNLsvkdalnyelkeiFDARDEYEKVLaqisnehDNPELLHRqdelvkfiESKDgwNIENKIERILD 145
Cdd:PRK11264 81 RQLRQHVGFvfqNFNL-------------FPHRTVLENII-------EGPVIVKG--------EPKE--EATARARELLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 146 SFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMV-------RFLEElllaSNQTIVFISHDRYF 218
Cdd:PRK11264 131 KVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgevlntiRQLAQ----EKRTMVIVTHEMSF 206
|
250
....*....|....
gi 1196666485 219 IDRLATRSVEIEDG 232
Cdd:PRK11264 207 ARDVADRAIFMDQG 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-233 |
5.69e-16 |
|
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: 77.47 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKF-----GDKII--LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMLAQ 73
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 SPKfnDNLSV-KDALNYE---LKEI--FDARDeyekVLAQisnehdnPeLLHRqdelvkfieskdGWNIE---NKIERIL 144
Cdd:COG4778 83 SPR--EILALrRRTIGYVsqfLRVIprVSALD----VVAE-------P-LLER------------GVDREearARARELL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 145 DSFGLREyenRL----VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEElLLASNQTIVFISHDR 216
Cdd:COG4778 137 ARLNLPE---RLwdlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanrAVVVELIEE-AKARGTAIIGIFHDE 212
|
250
....*....|....*..
gi 1196666485 217 YFIDRLATRSVEIEDGA 233
Cdd:COG4778 213 EVREAVADRVVDVTPFS 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
33-215 |
7.49e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.12 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 33 AIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNDNL--SVKDALNYELkeiFDARDEYEKvlaqisn 110
Cdd:NF040873 22 AVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLVAMGR---WARRGLWRR------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 111 ehdnpelLHRQDELVkfieskdgwnienkIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHL 190
Cdd:NF040873 92 -------LTRDDRAA--------------VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 1196666485 191 DVYMVRFLEELL---LASNQTIVFISHD 215
Cdd:NF040873 151 DAESRERIIALLaeeHARGATVVVVTHD 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-234 |
8.36e-16 |
|
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: 76.86 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRViRQNSISIEMLaqspkfndnlsvkdalnyelkeifDARDeye 102
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTDIRQL------------------------DPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 103 kVLAQISNEHDNPELLH---RQDelvkfIESKDGWNIENKIERILDSFGLREYENRLVN-----------SLSGGEIRRV 168
Cdd:cd03245 76 -LRRNIGYVPQDVTLFYgtlRDN-----ITLGAPLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 169 ALGALILKKPDVLLLDEPTNHLDVYM-VRFLEEL-LLASNQTIVFISHdRYFIDRLATRSVEIEDGAL 234
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSeERLKERLrQLLGDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-232 |
9.18e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.06 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRqnsisiemlaqspkfnDNLS 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV----------------DGLK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDAlNYELKEIfdaRDEYEKVLAQIsneHDNPELLHRqdELVKF----IESKDGWNIENKIERILDSFGLREYENRLVN 158
Cdd:PRK09493 65 VNDP-KVDERLI---RQEAGMVFQQF---YLFPHLTAL--ENVMFgplrVRGASKEEAEKQARELLAKVGLAERAHHYPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLD------VYMV-RFLEElllaSNQTIVFISHDRYFIDRLATRSVEIED 231
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpelrheVLKVmQDLAE----EGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
.
gi 1196666485 232 G 232
Cdd:PRK09493 212 G 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
347-509 |
1.16e-15 |
|
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: 80.20 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 347 LFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSIS---------DDkSLIE- 414
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlRRRIAvvpqrphlfDT-TLREn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 415 --LFCPNGGDHIMVR-----GrnyhvygyLKNFL--FPKEfLDKPVGV----LSGGEKNRLALALLFTKEYDCLILDEPT 481
Cdd:COG4987 429 lrLARPDATDEELWAalervG--------LGDWLaaLPDG-LDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|
gi 1196666485 482 NDLDIATI-NILEEYLLSFEG-AILIVSHD 509
Cdd:COG4987 500 EGLDAATEqALLADLLEALAGrTVLLITHR 529
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-234 |
1.27e-15 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 77.30 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 8 EVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-----------------IRQNSISieM 70
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamsrkelreLRRKKIS--M 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVKDALNYELkeifdardEYEKVLAQISNEhdnpellhrqdelvkfieskdgwnienKIERILDSFGLR 150
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFGL--------EVQGVPRAEREE---------------------------RAAEALELVGLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA----SNQTIVFISHDRYFIDRLATRS 226
Cdd:cd03294 152 GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqaeLQKTIVFITHDLDEALRLGDRI 231
|
....*...
gi 1196666485 227 VEIEDGAL 234
Cdd:cd03294 232 AIMKDGRL 239
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-232 |
1.31e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGrvirqnsisiemlaqspkfndNLSV 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG---------------------KITV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 kdalnyeLKEIFDARDEYEKVLAQISNEHDN--PELLHRQDELV--KFIESKdGWNIENKIERILDSFGLREYENRLVNS 159
Cdd:PRK13536 101 -------LGVPVPARARLARARIGVVPQFDNldLEFTVRENLLVfgRYFGMS-TREIEAVIPSLLEFARLESKADARVSD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYmVRFL--EEL--LLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLiwERLrsLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
333-509 |
1.33e-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: 80.65 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKT--IDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-----NRGEI-------KIGY 398
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgiDLRQIdpaslrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 FDQ---------------SRKSISDDK-----------SLIELFcPNGGDH-IMVRGRNyhvygylknflfpkefldkpv 451
Cdd:COG2274 554 VLQdvflfsgtirenitlGDPDATDEEiieaarlaglhDFIEAL-PMGYDTvVGEGGSN--------------------- 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 452 gvLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEG--AILIVSHD 509
Cdd:COG2274 612 --LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-485 |
1.50e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.67 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRviRQNS------ISIEMLAQ- 73
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--RQSQfshitrLSFEQLQKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 -SPKFNDNlsvkdalNYELkeIFDARDEYEKVLAQ-ISNEHDNPELlhrqdelvkfieskdgwnienkIERILDSFGLRE 151
Cdd:PRK10938 79 vSDEWQRN-------NTDM--LSPGEDDTGRTTAEiIQDEVKDPAR----------------------CEQLAQQFGITA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFIShdryfidrlaTRSVE 228
Cdd:PRK10938 128 LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELlasLHQSGITLVLVL----------NRFDE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 229 IEDgalrsfdggYANYLTkkeeilrSLAKSHETLIknlKSEEEWLRRGVKARLKRNEGRKQRILAMREEAKKNPGLIRrv 308
Cdd:PRK10938 198 IPD---------FVQFAG-------VLADCTLAET---GEREEILQQALVAQLAHSEQLEGVQLPEPDEPSARHALPA-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 309 klelerasksfnggglNQNRkkmlFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGelEADSGV 388
Cdd:PRK10938 257 ----------------NEPR----IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGY 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 389 IN--------RG------EIK--IGYFDQS-----RKSISDDKSLIELFCPNGGDHIMVRGRNYHVYG-YLKNFLFPKEF 446
Cdd:PRK10938 315 SNdltlfgrrRGsgetiwDIKkhIGYVSSSlhldyRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQqWLDILGIDKRT 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1196666485 447 LDKPVGVLSGGEKnRLAL---ALLftKEYDCLILDEPTNDLD 485
Cdd:PRK10938 395 ADAPFHSLSWGQQ-RLALivrALV--KHPTLLILDEPLQGLD 433
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-215 |
1.52e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI----RQNSI-----SIEML 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekRMNDVppaerGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 72 AQSPKFNDNLSVKDALNYELKeifdardeyekvLAQISNEhdnpellhrqdelvkfieskdgwNIENKIERILDSFGLRE 151
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLK------------LAGAKKE-----------------------EINQRVNQVAEVLQLAH 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 152 YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHD 215
Cdd:PRK11000 126 LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-204 |
2.00e-15 |
|
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: 75.09 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkFNDnlsvkdalnyelKE 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR---------------WNG------------TP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 IFDARDEYEKVLAQISneHDN---PELLHRqdELVKFIeSKDGWNIENKIERILDSFGLREYENRLVNSLSGGEIRRVAL 170
Cdd:TIGR01189 64 LAEQRDEPHENILYLG--HLPglkPELSAL--ENLHFW-AAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLAL 138
|
170 180 190
....*....|....*....|....*....|....
gi 1196666485 171 GALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA 204
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-216 |
2.85e-15 |
|
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: 78.87 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIE-------------------MLAQSPKFNDNLSV 83
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-IAVNGVPLAdadadswrdqiawvpqhpfLFAGTIAENIRLAR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDALNYELKEIFDAR--DEYEKVLaqisnehdnPELLHRQdelvkfieskdgwnienkieriLDSFGLReyenrlvnsLS 161
Cdd:TIGR02857 421 PDASDAEIREALERAglDEFVAAL---------PQGLDTP----------------------IGEGGAG---------LS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVYM-VRFLEELL-LASNQTIVFISHDR 216
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRaLAQGRTVLLVTHRL 517
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-256 |
2.90e-15 |
|
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: 75.80 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGD-KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIemLAQSPkfndnLS 82
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGE-IFIDGEDI--REQDP-----VE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYelkeifdardeyekVLAQISnehdnpeLL-HRQ-DELVKFIESKDGWNIENKIERILDSFGL-----REYENR 155
Cdd:cd03295 73 LRRKIGY--------------VIQQIG-------LFpHMTvEENIALVPKLLKWPKEKIRERADELLALvgldpAEFADR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 156 LVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDryfID---RLATRSVE 228
Cdd:cd03295 132 YPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelgkTIVFVTHD---IDeafRLADRIAI 208
|
250 260
....*....|....*....|....*...
gi 1196666485 229 IEDGALRSFDggyanyltKKEEILRSLA 256
Cdd:cd03295 209 MKNGEIVQVG--------TPDEILRSPA 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-509 |
4.20e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI---RQNSIS---------IEM 70
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgKPVRIRsprdaialgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVkdalnyelkeifdardeYEKVLaqISNEHDNPELLHRQDelvkfieskdgwnIENKIERILDSFGLR 150
Cdd:COG3845 85 VHQHFMLVPNLTV-----------------AENIV--LGLEPTKGGRLDRKA-------------ARARIRELSERYGLD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVAlgalILK----KPDVLLLDEPTNHL---DVymvrflEELL-----LASNQ-TIVFISHdry 217
Cdd:COG3845 133 VDPDAKVEDLSVGEQQRVE----ILKalyrGARILILDEPTAVLtpqEA------DELFeilrrLAAEGkSIIFITH--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 218 fidrlatrsveiedgalrsfdggyanyltKKEEIlrsLAKSHETLIknlkseeewLRRG-VKARLKRNEGRKQRILAM-- 294
Cdd:COG3845 200 -----------------------------KLREV---MAIADRVTV---------LRRGkVVGTVDTAETSEEELAELmv 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 295 -REeakknpglirrVKLELERASKsfnggglnqNRKKMLFECKNLS-KTIDNKVLFSDFNARVLQGERIGIVGRNGSGKS 372
Cdd:COG3845 239 gRE-----------VLLRVEKAPA---------EPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQS 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 373 TMLKILLGELEADSgvinrGEIKIGYFDQSRKSIsddKSLIELfcpnGGDHI----MVRG-------------RNYHVYG 435
Cdd:COG3845 299 ELAEALAGLRPPAS-----GSIRLDGEDITGLSP---RERRRL----GVAYIpedrLGRGlvpdmsvaenlilGRYRRPP 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 436 YLKNFLFP------------KEF------LDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLL 497
Cdd:COG3845 367 FSRGGFLDrkairafaeeliEEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLL 446
|
570
....*....|....*
gi 1196666485 498 SF--EG-AILIVSHD 509
Cdd:COG3845 447 ELrdAGaAVLLISED 461
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
4.41e-15 |
|
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: 73.23 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvirqnsISIEMLAQSPkfndnLSV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILVDGKEVSF-----ASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDAlnyelkeifdardeyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIErildsfglreyenrLVNSLSGG 163
Cdd:cd03216 70 RDA-------------------------------------------------RRAGIA--------------MVYQLSVG 86
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISH 214
Cdd:cd03216 87 ERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH 140
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-232 |
5.17e-15 |
|
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: 74.45 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 30 ERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQnsiSIEMLAQSPK-------FNDNlsvkdalnyelkEIFDARDEYE 102
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN---GVDVTAAPPAdrpvsmlFQEN------------NLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 103 KV-LAQISNEHDNPEllHRQdelvkfieskdgwnienKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVL 181
Cdd:cd03298 90 NVgLGLSPGLKLTAE--DRQ-----------------AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 182 LLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-235 |
5.89e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRViRQNSISIEMLAQSPKFNDN 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-LVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 LSVKD--ALNYElkeiFDARDEYEkvlaqisnehdnpelLHRQDELVKFieskDGWNIENK--IERILDSFGLREYENRL 156
Cdd:PRK09536 80 ASVPQdtSLSFE----FDVRQVVE---------------MGRTPHRSRF----DTWTETDRaaVERAMERTGVAQFADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV-YMVRFLEEL--LLASNQTIVFISHDRYFIDRLATRSVEIEDGA 233
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGR 216
|
..
gi 1196666485 234 LR 235
Cdd:PRK09536 217 VR 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
334-528 |
6.44e-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: 74.33 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG---------VINRGEIK--IGYFDQS 402
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdvVREPREVRrrIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 RksiSDDKSLielfcpNGGDHIMVRGRnyhVYGY-----------LKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKE 471
Cdd:cd03265 82 L---SVDDEL------TGWENLYIHAR---LYGVpgaerrerideLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 472 YDCLILDEPTNDLDIATINILEEYL----LSFEGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIeklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-233 |
7.17e-15 |
|
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: 72.57 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNDnLSVKDALNYelkei 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPL-GTLREQLIY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 fdardeyekvlaqisnehdnPellhrqdelvkfieskdgWNIEnkierildsfglreyenrlvnsLSGGEIRRVALGALI 174
Cdd:cd03223 87 --------------------P------------------WDDV----------------------LSGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 175 LKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISHdRYFIDRLATRSVEIEDGA 233
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-232 |
7.80e-15 |
|
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: 74.30 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPK----FND 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNvgfvFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 -----NLSVKDALNYELKEifdardeyeKVLAQISNEHDnpellhrqdelvkfieskdgwnIENKIERILDSFGLREYEN 154
Cdd:cd03296 83 yalfrHMTVFDNVAFGLRV---------KPRSERPPEAE----------------------IRAKVHELLKLVQLDWLAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIE 230
Cdd:cd03296 132 RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKvrkeLRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMN 211
|
..
gi 1196666485 231 DG 232
Cdd:cd03296 212 KG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-508 |
1.15e-14 |
|
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: 72.08 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgeikigyfdqsrksisddksl 412
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ielfcpnggdHIMVRGRNYHvygylknFLFPKEFLDKPVGV---LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATI 489
Cdd:cd03216 56 ----------EILVDGKEVS-------FASPRDARRAGIAMvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180
....*....|....*....|..
gi 1196666485 490 NILEEYL--LSFEG-AILIVSH 508
Cdd:cd03216 119 ERLFKVIrrLRAQGvAVIFISH 140
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-215 |
1.15e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 74.39 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKF--GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV---------------IRQNsi 66
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldtldeenlweIRKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 67 sIEMLAQSPkfnDNlsvkdalnyelkeifdardeyekvlaQISN---EHD---NPELLHrqdelVKFIEskdgwnIENKI 140
Cdd:TIGR04520 79 -VGMVFQNP---DN--------------------------QFVGatvEDDvafGLENLG-----VPREE------MRKRV 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 141 ERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHD 215
Cdd:TIGR04520 118 DEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKgrkeVLETIRKLNKEEGITVISITHD 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-528 |
1.23e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 73.06 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKS--ISDDkSLIELFCPNGGDHIMVR 427
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIgyVMQD-VDYQLFTDSVREELLLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 428 GRNYHVYG-----YLKNfLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEG- 501
Cdd:cd03226 97 LKELDAGNeqaetVLKD-LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAq 175
|
170 180
....*....|....*....|....*....
gi 1196666485 502 --AILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03226 176 gkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-509 |
1.58e-14 |
|
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: 73.48 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINrgeikigYFDQSRKSISDDksli 413
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL-------VDGQDITGLSEK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELFcpnggdhiMVRGRnyhvYGYL-------------KNFLFP-KEFLDKP--------------VGV----------LS 455
Cdd:COG1127 76 ELY--------ELRRR----IGMLfqggalfdsltvfENVAFPlREHTDLSeaeirelvleklelVGLpgaadkmpseLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 456 GGEKNRLALA--------LLFtkeydcliLDEPTNDLD-IATINILEeyLL-----SFEGAILIVSHD 509
Cdd:COG1127 144 GGMRKRVALAralaldpeILL--------YDEPTAGLDpITSAVIDE--LIrelrdELGLTSVVVTHD 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-528 |
1.74e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.16 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVL-FSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI----------NRGEI-----KIG 397
Cdd:COG2884 3 RFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrlKRREIpylrrRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 398 YFDQSRKSIsDDKSLIElfcpNggdhIM----VRGRNYHVYGY-----LKNF-LFPKEflDKPVGVLSGGEKNRLALALL 467
Cdd:COG2884 83 VVFQDFRLL-PDRTVYE----N----VAlplrVTGKSRKEIRRrvrevLDLVgLSDKA--KALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 468 FTKEYDCLILDEPTNDLDIAT----INILEEylLSFEG-AILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETsweiMELLEE--INRRGtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-253 |
2.28e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisieMLAQSPkfndnlsVKDALN 88
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---------RLNGRP-------LADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YELkeifdARdeYEKVLAQISN--------E------HDNPELLHRQDELVkfieskdgwnienkiERILDSFGLREYEN 154
Cdd:PRK13548 72 AEL-----AR--RRAVLPQHSSlsfpftveEvvamgrAPHGLSRAEDDALV---------------AAALAQVDLAHLAG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 155 RLVNSLSGGEIRRVALgALIL-------KKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHD-----RYf 218
Cdd:PRK13548 130 RDYPQLSGGEQQRVQL-ARVLaqlwepdGPPRWLLLDEPTSALDLAhqhhVLRLARQLAHERGLAVIVVLHDlnlaaRY- 207
|
250 260 270
....*....|....*....|....*....|....*
gi 1196666485 219 idrlATRSVEIEDGALRSfDGGYANYLTkkEEILR 253
Cdd:PRK13548 208 ----ADRIVLLHQGRLVA-DGTPAEVLT--PETLR 235
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-223 |
2.45e-14 |
|
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: 73.17 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 34 IIGKNGGGKSTLMKILRGECEIDSGrvirqnsisiemlaqspKFNDNLSVKDALNY----ELKEIFDA-RDEYEKV---- 104
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLG-----------------KFDDPPDWDEILDEfrgsELQNYFTKlLEGDVKVivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 105 --LAQISNEHDNP--ELLHRQDELvkfieskdgwnieNKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDV 180
Cdd:cd03236 94 qyVDLIPKAVKGKvgELLKKKDER-------------GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1196666485 181 LLLDEPTNHLDVY----MVRFLEELLLASNQTIVfISHDRYFIDRLA 223
Cdd:cd03236 161 YFFDEPSSYLDIKqrlnAARLIRELAEDDNYVLV-VEHDLAVLDYLS 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-530 |
2.82e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-----------RGEIKIGYFDQS 402
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrarHARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 rKSISDDKSLIElfcpnggdHIMVRGRNYHVYGYLKNFLFPK--EFL------DKPVGVLSGGEKNRLALALLFTKEYDC 474
Cdd:PRK13537 89 -DNLDPDFTVRE--------NLLVFGRYFGLSAAAARALVPPllEFAklenkaDAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 475 LILDEPTNDLDIATINILEEYLLSFEGA---ILIVSHDRYFIDKITNKLWAYENG-KIEQ 530
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERLCDRLCVIEEGrKIAE 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
331-509 |
3.54e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgeiKIGYFDQSRKSIS--- 407
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG-------EVRLNGRPLADWSpae 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 408 ------------------------------------DDKSLIelfcpnggDHIM-------VRGRNYHvygylknflfpk 444
Cdd:PRK13548 74 larrravlpqhsslsfpftveevvamgraphglsraEDDALV--------AAALaqvdlahLAGRDYP------------ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 445 efldkpvgVLSGGEKNRLALALLFT------KEYDCLILDEPTNDLDIA----TINILEEYLLSFEGAILIVSHD 509
Cdd:PRK13548 134 --------QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAhqhhVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
354-508 |
3.73e-14 |
|
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: 72.02 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 354 RVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeiKIGYFDQSRKSIsDDKSLIELFCPNGG--DHIMVR---- 427
Cdd:cd03266 27 TVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVKEPA-EARRRLGFVSDSTGlyDRLTARenle 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 428 --GRNYHVYG--------YLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL- 496
Cdd:cd03266 101 yfAGLYGLKGdeltarleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIr 180
|
170
....*....|....
gi 1196666485 497 -LSFEG-AILIVSH 508
Cdd:cd03266 181 qLRALGkCILFSTH 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-234 |
4.08e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.92 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 12 KFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnSISIEMLAQSpkfndNLSVKDALNYEL 91
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV----SFRGQDLYQL-----DRKQRRAFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 92 KEIFdaRDEYEKVlaqisnehdNPELLHRQ--DELVKFIESKDGWNIENKIERILDSFGLR-EYENRLVNSLSGGEIRRV 168
Cdd:TIGR02769 91 QLVF--QDSPSAV---------NPRMTVRQiiGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 169 ALGALILKKPDVLLLDEPTNHLDVYM----VRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGAL 234
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLqaviLELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-241 |
6.40e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRViRQNSISIEmlAQSPKFNDNL-------SVKDA 86
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIR--RQRDEYHQDLlylghqpGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 87 LNYElkeifdardEYEKVLAQISNEHDnpellhrqdelvkfieskdgwniENKIERILDSFGLREYENRLVNSLSGGEIR 166
Cdd:PRK13538 89 LTAL---------ENLRFYQRLHGPGD-----------------------DEALWEALAQVGLAGFEDVPVRQLSAGQQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 167 RVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL---LASNQTIVFISHdryfidrlatRSVEIEDGALRSFDGGY 241
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhAEQGGMVILTTH----------QDLPVASDKVRKLRLGQ 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-232 |
7.44e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.54 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSIS----------IEMLAQSPKFNDNLSVKDALNYELk 92
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGS-LTLNGQDhtttppsrrpVSMLFQENNLFSHLTVAQNIGLGL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 93 eifdardeyekvlaqisneHDNPELLHRQDElvkfieskdgwnienKIERILDSFGLREYENRLVNSLSGGEIRRVALGA 172
Cdd:PRK10771 97 -------------------NPGLKLNAAQRE---------------KLHAIARQMGIEDLLARLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 173 LILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-239 |
7.91e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 72.10 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 16 KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsISIEMLAQSPKFNdnlsvkdalnyeLKEIf 95
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVT----IDGRDITAKKKKK------------LKDL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 96 daRdeyEKV--LAQisnehdNPEllhrqDELvkFIES--KD--------GWN---IENKIERILDSFGL-REYENRLVNS 159
Cdd:TIGR04521 81 --R---KKVglVFQ------FPE-----HQL--FEETvyKDiafgpknlGLSeeeAEERVKEALELVGLdEEYLERSPFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 160 LSGGEIRRVAL-GALILKkPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGAL 234
Cdd:TIGR04521 143 LSGGQMRRVAIaGVLAME-PEVLILDEPTAGLDpkgrKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
....*
gi 1196666485 235 rSFDG 239
Cdd:TIGR04521 222 -VLDG 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-232 |
8.06e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKF-NDNLsvKDALNYELKE 93
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLpLGTL--REALLYPATA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 IFDARDEYEKVLAQISNEHdnpeLLHRQDElvkfiesKDGWNienkierildsfglreyenrlvNSLSGGEIRRVALGAL 173
Cdd:COG4178 453 EAFSDAELREALEAVGLGH----LAERLDE-------EADWD----------------------QVLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 174 ILKKPDVLLLDEPTNHLDVYMVRFLEELLLAS--NQTIVFISHdRYFIDRLATRSVEIEDG 232
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-202 |
8.77e-14 |
|
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: 70.60 E-value: 8.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMlaqspkfndnlsvkdalnyelke 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ----------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 ifdaRDEYEKVLAQISNEHDNPELLHRQDELVKF--IESKDGwnienkIERILDSFGLREYENRLVNSLSGGEIRRVALG 171
Cdd:cd03231 68 ----RDSIARGLLYLGHAPGIKTTLSVLENLRFWhaDHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALA 137
|
170 180 190
....*....|....*....|....*....|.
gi 1196666485 172 ALILKKPDVLLLDEPTNHLDVYMVRFLEELL 202
Cdd:cd03231 138 RLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-234 |
9.67e-14 |
|
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: 74.07 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKF-----GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMlaQSPK 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDM--TKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 FNDNLSVKDALNYELKE--IFDARDEYEKVLAQISnehdnpelLHRQDELVK---FIESKDGWNIENKIERILDsfglre 151
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQEydLYPHRTVLDNLTEAIG--------LELPDELARmkaVITLKMVGFDEEKAEEILD------ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 yenRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD-VYMVRFLEELLLAS---NQTIVFISHDRYFIDRLATRSV 227
Cdd:TIGR03269 423 ---KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAA 499
|
....*..
gi 1196666485 228 EIEDGAL 234
Cdd:TIGR03269 500 LMRDGKI 506
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
348-531 |
1.13e-13 |
|
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: 70.40 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 348 FSDFN---ARVLQGERIGIVGRNGSGKSTMLKILLGELEADsgvinRGEIKIG---YFDqSRKSI--SDDKSLIELFCPN 419
Cdd:cd03297 10 LPDFTlkiDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPD-----GGTIVLNgtvLFD-SRKKInlPPQQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 420 GG--DHIMVRgRNYhVYGYLKNFLFPKEF--------------LDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTND 483
Cdd:cd03297 84 YAlfPHLNVR-ENL-AFGLKRKRNREDRIsvdelldllgldhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 484 LDIATINILEEYL----LSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:cd03297 162 LDRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
331-508 |
1.22e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigyfdqsrksisddk 410
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 slieLFCPNGGDHIMVRGRnYHVYGY---LKNFL-------FPKEFL--------------------DKPVGVLSGGEKN 460
Cdd:PRK13539 60 ----KLDGGDIDDPDVAEA-CHYLGHrnaMKPALtvaenleFWAAFLggeeldiaaaleavglaplaHLPFGYLSAGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 461 RLALALLFTKEYDCLILDEPTNDLDIATINILEEYL---LSFEGAILIVSH 508
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIrahLAQGGIVIAATH 185
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-224 |
1.37e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.66 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV---------IRQNSI--SIEMLAQSPK-FNDnl 81
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTLESLrrQIGVVPQDTFlFSG-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKD-----ALNYELKEIFDArdeyekvlAQISNEHDnpellhrqdelvkFIESK-DGWN--IEnkiERildsfGLReye 153
Cdd:COG1132 429 TIREnirygRPDATDEEVEEA--------AKAAQAHE-------------FIEALpDGYDtvVG---ER-----GVN--- 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 154 nrlvnsLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT 224
Cdd:COG1132 477 ------LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALerLMKGRTTIVIAH------RLST 537
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-214 |
1.57e-13 |
|
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: 69.26 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkfndnLSVKDALNYElkei 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-------------------LDGVPVSDLE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 fDARDEYEKVLAQisnehdNPELlhrqdelvkFIESkdgwnienkierILDSFGLReyenrlvnsLSGGEIRRVALGALI 174
Cdd:cd03247 71 -KALSSLISVLNQ------RPYL---------FDTT------------LRNNLGRR---------FSGGERQRLALARIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196666485 175 LKKPDVLLLDEPTNHLDVYMVRFLEELLL--ASNQTIVFISH 214
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFevLKDKTLIWITH 155
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-234 |
1.67e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSiSIEMLAQSPKfndnlsvKDALNYELKEIFda 97
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-PMSKLSSAAK-------AELRNQKLGFIY-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 98 rdEYEKVLAQISN-EHDNPELLhrqdelvkfIESKDGWNIENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILK 176
Cdd:PRK11629 94 --QFHHLLPDFTAlENVAMPLL---------IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 177 KPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFIDRLaTRSVEIEDGAL 234
Cdd:PRK11629 163 NPRLVLADEPTGNLDARnadsIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-509 |
1.71e-13 |
|
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: 70.19 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNK----VLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG-VINRGEI------KIGY-FDQ 401
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGeVLVDGEPvtgpgpDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 402 SR----KSISDDKSLIELFCPNGGDHIMVRGRNY-HVYGyLKNFL--FPKEfldkpvgvLSGGEKNRLALALLFTKEYDC 474
Cdd:cd03293 82 DAllpwLTVLDNVALGLELQGVPKAEARERAEELlELVG-LSGFEnaYPHQ--------LSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1196666485 475 LILDEPTNDLDIATINILEEYLL----SFEGAILIVSHD 509
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLdiwrETGKTVLLVTHD 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-215 |
1.73e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.95 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSIS--------I 68
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenIPAMSRSrlytvrkrM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 69 EMLAQSPKFNDNLSVKDALNYELKEifdardeyekvlaqisneHDN-PELLHRQDELVKfieskdgwnienkieriLDSF 147
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLRE------------------HTQlPAPLLHSTVMMK-----------------LEAV 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 148 GLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD-VYM---VRFLEELLLASNQTIVFISHD 215
Cdd:PRK11831 132 GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDpITMgvlVKLISELNSALGVTCVVVSHD 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-509 |
1.74e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.18 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 346 VLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINR-GEIKIGYFDQsRKSISD-------DKSLIELFC 417
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQ-RSEVPDslpltvrDLVAMGRWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 418 PNGG------------DHIMVRgrnyhvygylknfLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD 485
Cdd:NF040873 85 RRGLwrrltrddraavDDALER-------------VGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*..
gi 1196666485 486 IATINILEEYL--LSFEGA-ILIVSHD 509
Cdd:NF040873 152 AESRERIIALLaeEHARGAtVVVVTHD 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
1.85e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNsisiemlaqspkfndnlsvkDALNYELKEIFDAR 98
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG--------------------EPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 deyeKVLAQISNEHDNPELLHRQDELVKFIESKDGWN---IENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALIL 175
Cdd:PRK13639 78 ----KTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSkeeVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1196666485 176 KKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHD 215
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
345-512 |
2.97e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.62 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 345 KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG--VINRGEiKIGYFDQSRKSIsDDKSLI--------E 414
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGnvSLDPNE-RLGKLRQDQFAF-EEFTVLdtvimghtE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 415 LF-CPNGGDHI-----MVRGRNYHVY----------GY---------LKNFLFPKEFLDKPVGVLSGGEKNRLALA-LLF 468
Cdd:PRK15064 92 LWeVKQERDRIyalpeMSEEDGMKVAdlevkfaemdGYtaearagelLLGVGIPEEQHYGLMSEVAPGWKLRVLLAqALF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1196666485 469 TKEyDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYF 512
Cdd:PRK15064 172 SNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHF 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
334-529 |
3.39e-13 |
|
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: 69.45 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIGYFDQSRKSISDDKSLI 413
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS-----GEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 E----------LFcpnggDHIMVRgrnyhvygylKNFLFP-KEFLDKP--------------VGV----------LSGGE 458
Cdd:cd03261 77 RrmgmlfqsgaLF-----DSLTVF----------ENVAFPlREHTRLSeeeireivlekleaVGLrgaedlypaeLSGGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 459 KNRLALA--LLFTKEYdcLILDEPTNDLDIATINILEEYLLS----FEGAILIVSHDRYFIDKITNKLWAYENGKIE 529
Cdd:cd03261 142 KKRVALAraLALDPEL--LLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-528 |
3.43e-13 |
|
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: 68.01 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTI--DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKsisddk 410
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 slielfcpngGDHImvrgrnyhvyGYL--KNFLFPKEFLDKpvgVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT 488
Cdd:cd03246 75 ----------GDHV----------GYLpqDDELFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1196666485 489 INILEEYLLSFEGA---ILIVSHDRYFIdKITNKLWAYENGKI 528
Cdd:cd03246 132 ERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-509 |
3.76e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINR-GEIKIGYFDQsrkSISDDK 410
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRnGKLRIGYVPQ---KLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SL---IELFcpnggdhIMVRGrnyhvyGYLKNFLFP-------KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEP 480
Cdd:PRK09544 81 TLpltVNRF-------LRLRP------GTKKEDILPalkrvqaGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190
....*....|....*....|....*....|...
gi 1196666485 481 TNDLDI----ATINILEEYLLSFEGAILIVSHD 509
Cdd:PRK09544 148 TQGVDVngqvALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
333-528 |
4.39e-13 |
|
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: 69.13 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDN-KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-----NRGEIKIGYFDQSRKS- 405
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtDINKLKGKALRQLRRQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 --ISDDKSLIELFcpNGGDHIMVrGR-NYHvyGYLKNF--LFPKE----------------FLDKPVGVLSGGEKNRLAL 464
Cdd:cd03256 81 gmIFQQFNLIERL--SVLENVLS-GRlGRR--STWRSLfgLFPKEekqralaalervglldKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLDIATINILEEYLLSF---EGAILIVS-HDRYFIDKITNKLWAYENGKI 528
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGRI 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-244 |
4.58e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 69.18 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSIS-----IEMLAQSPK-FNDnlSVKD 85
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdVRDYTLAslrrqIGLVSQDVFlFND--TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 ALNYELKEIfdARDEYEKVlAQISNEHDnpellhrqdelvkFIEskdgwNIENKIERILDSFGLReyenrlvnsLSGGEI 165
Cdd:cd03251 95 NIAYGRPGA--TREEVEEA-ARAANAHE-------------FIM-----ELPEGYDTVIGERGVK---------LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 166 RRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT-----RSVEIEDG------ 232
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALerLMKNRTTFVIAH------RLSTienadRIVVLEDGkiverg 218
|
250
....*....|....*
gi 1196666485 233 ---ALRSFDGGYANY 244
Cdd:cd03251 219 theELLAQGGVYAKL 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
334-508 |
4.63e-13 |
|
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: 68.15 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigyfdqsrksISDDKSLI 413
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV----------------RWNGTPLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELfCPNGGDHIMVRGrnyHVYGyLKNFLFPKEFL---------------------------DKPVGVLSGGEKNRLALAL 466
Cdd:TIGR01189 66 EQ-RDEPHENILYLG---HLPG-LKPELSALENLhfwaaihggaqrtiedalaavgltgfeDLPAAQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1196666485 467 LFTKEYDCLILDEPTNDLDIATINILEEYL---LSFEGAILIVSH 508
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLrahLARGGIVLLTTH 185
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-215 |
5.49e-13 |
|
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: 69.46 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 33 AIIGKNGGGKSTLMKILRGECEIDSGRVI-----------RQNSISIEMLAQSPKFNDNLSVKDAlnyelkeIFDARDEY 101
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVEQDSDTAVPLTVRDV-------VALGRIPH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 102 EKVLAqISNEHDnpellhrqDELVkfieskdgwnienkiERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVL 181
Cdd:TIGR03873 104 RSLWA-GDSPHD--------AAVV---------------DRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196666485 182 LLDEPTNHLDVY----MVRFLEElLLASNQTIVFISHD 215
Cdd:TIGR03873 160 LLDEPTNHLDVRaqleTLALVRE-LAATGVTVVAALHD 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
334-508 |
5.61e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.29 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG--------------VINRGEIKIGYF 399
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrvllnggpldfqrdSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 400 DQSRKSISDDKSLiELFCPNGGD--------HIMVRGrnyhvygylknflfpkeFLDKPVGVLSGGEKNRLALALLFTKE 471
Cdd:cd03231 82 PGIKTTLSVLENL-RFWHADHSDeqveealaRVGLNG-----------------FEDRPVAQLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1196666485 472 YDCLILDEPTNDLDIATINILEEYL---LSFEGAILIVSH 508
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
334-531 |
5.75e-13 |
|
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: 68.31 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSIS---DDK 410
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGmvfQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLIelfcpnggDHIMVRgRNYhVYGyLKNFLFPKE-----------------FLDKPVGVLSGGEKNRLALALLFTKEYD 473
Cdd:cd03259 82 ALF--------PHLTVA-ENI-AFG-LKLRGVPKAeirarvrellelvglegLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 474 CLILDEPTNDLD-IATINILEEY--LLSFEGAILI-VSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:cd03259 151 LLLLDEPLSALDaKLREELREELkeLQRELGITTIyVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-232 |
8.97e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.45 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV----------IRQNSISIEML 71
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpsrARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 72 AQSPKFNDNLSVKDALnyelkEIFDardEYEKVLAQISNEHdNPELLhrqdELVKfieskdgwnIENKIERildsfglre 151
Cdd:PRK13537 86 PQFDNLDPDFTVRENL-----LVFG---RYFGLSAAAARAL-VPPLL----EFAK---------LENKADA--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 yenrLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVyMVRFL--EEL--LLASNQTIVFISHDRYFIDRLATRSV 227
Cdd:PRK13537 135 ----KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP-QARHLmwERLrsLLARGKTILLTTHFMEEAERLCDRLC 209
|
....*
gi 1196666485 228 EIEDG 232
Cdd:PRK13537 210 VIEEG 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-528 |
9.43e-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: 67.55 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIgyfDQSRKSISDDKSL 412
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL---TDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 I-------ELFcPNGG--DHIM-----VRGRNY-----HVYGYLKNF-LFPKEflDKPVGVLSGGEKNRLALALLFTKEY 472
Cdd:cd03262 78 VgmvfqqfNLF-PHLTvlENITlapikVKGMSKaeaeeRALELLEKVgLADKA--DAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 473 DCLILDEPTNDLDIATINileEYL-----LSFEG-AILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03262 155 KVMLFDEPTSALDPELVG---EVLdvmkdLAEEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
331-508 |
1.02e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 68.57 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrGEIKIgyFDQSRK--SISD 408
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRL--FGERRGgeDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 409 DKSLIELFCPNGGDHIMVRGRNYHV-----YGYLknFLFPK-------------------EFLDKPVGVLSGGEKNRLAL 464
Cdd:COG1119 76 LRKRIGLVSPALQLRFPRDETVLDVvlsgfFDSI--GLYREptdeqrerarellellglaHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSH 508
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-215 |
1.10e-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: 70.85 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV---------IRQNSIS--IEMLAQSPKFNDNlS 82
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssLDQDEVRrrVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYELKEIFDarDEYEKVLAQISnehdnpellhrqdelvkfieskdgwnIENKIERILDSFGLREYENrlVNSLSG 162
Cdd:TIGR02868 425 VRENLRLARPDATD--EELWAALERVG--------------------------LADWLRALPDGLDTVLGEG--GARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA--SNQTIVFISHD 215
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAalSGRTVVLITHH 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-186 |
1.20e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 67.95 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS-----------IEMLAQSPK 76
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlLDGQDITklpmhkrarlgIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 FNDNLSVKDALNYELKEIFDARDEyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIERILDSFGLREYENRL 156
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKE-----------------------------------REEKLEELLEEFHITHLRKSK 130
|
170 180 190
....*....|....*....|....*....|
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEP 186
Cdd:cd03218 131 ASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
336-521 |
1.29e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.84 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKT-----IDNKVL--FSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN------------------ 390
Cdd:COG4778 8 ENLSKTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqasprei 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 391 ----RGEIkiGYFDQ-----SRKSISD--DKSLIELfcpnGGDHIMVRGRNYHVygyLKNFLFPKEFLDKPVGVLSGGEK 459
Cdd:COG4778 88 lalrRRTI--GYVSQflrviPRVSALDvvAEPLLER----GVDREEARARAREL---LARLNLPERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 460 NRLALALLFTKEYDCLILDEPTNDLDIAT----INILEEYLLsfEG-AILIVSHDRYFIDKITNKLW 521
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA--RGtAIIGIFHDEEVREAVADRVV 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-297 |
1.51e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQN------SISIEM-----LAQspkfndNLSVK 84
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvptSGEVRVL-GYVPFKRrkefarRIGVVFgqrsqLWW------DLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DALNYeLKEIFD-ARDEYEKvlaqisnehdnpellhRQDELVKfieskdgwnienkierILDsfgLREYENRLVNSLSGG 163
Cdd:COG4586 115 DSFRL-LKAIYRiPDAEYKK----------------RLDELVE----------------LLD---LGELLDTPVRQLSLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDV---YMVR-FLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALRsFDG 239
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIReFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII-YDG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 240 gyanyltKKEEILRSLAKSHE---TLIKNLKSEEewLRRGVKarLKRNEGRKQRILAMREE 297
Cdd:COG4586 238 -------SLEELKERFGPYKTivlELAEPVPPLE--LPRGGE--VIEREGNRVRLEVDPRE 287
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-215 |
1.53e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.50 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV--------------IRQNsisIEMLAQSPkfnDN---- 80
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetvwdVRRQ---VGMVFQNP---DNqfvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 LSVKDALNYELKEIFDARDEYekvlaqisnehdnpellhrqdelvkfieskdgwnienkIERI---LDSFGLREYENRLV 157
Cdd:PRK13635 97 ATVQDDVAFGLENIGVPREEM--------------------------------------VERVdqaLRQVGMEDFLNREP 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 158 NSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD-------VYMVRFLEElllASNQTIVFISHD 215
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-214 |
1.69e-12 |
|
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: 66.42 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL--RGECEIDSGRV------IRQNSI--SIEMLA 72
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVlingrpLDKRSFrkIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPKFNDNLSVKDALNYELKeifdardeyekvlaqisnehdnpellhrqdelvkfieskdgwnienkierildsfgLRey 152
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAK--------------------------------------------------------LR-- 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 153 enrlvnSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LAS-NQTIVFISH 214
Cdd:cd03213 111 ------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLrrLADtGRTIICSIH 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-509 |
2.16e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSG----------VINR---------------GEI----KIGYFDQSRKSIs 407
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdeVLKRfrgtelqnyfkklynGEIkvvhKPQYVDLIPKVF- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 408 dDKSLIELFcpnggDHIMVRGrnyhVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDI- 486
Cdd:PRK13409 177 -KGKVRELL-----KKVDERG----KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIr 246
|
170 180
....*....|....*....|....*.
gi 1196666485 487 ---ATINILEEylLSFEGAILIVSHD 509
Cdd:PRK13409 247 qrlNVARLIRE--LAEGKYVLVVEHD 270
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-217 |
2.36e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 13 FGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILrgeceidsGRVIRQNSISIEMlaqspkfnDNLSVKDalnyelk 92
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF--------ARLLTPQSGTVFL--------GDKPISM------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 93 eiFDARdEYEKVLAQISNEHDNPELLHRQdELVKFIES-------KDGWNIENKIERILDSFGLREYENRLVNSLSGGEI 165
Cdd:PRK11231 69 --LSSR-QLARRLALLPQHHLTPEGITVR-ELVAYGRSpwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 166 RRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEElLLASNQTIVFISHD-----RY 217
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMRE-LNTQGKTVVTVLHDlnqasRY 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-214 |
2.53e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNS--------ISIEMLAQSPKFNDNLSVKD 85
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 ALnyelkeIFDARdeyekvlaqisnehdnpelLHRQDELvkfieskdgwnienKIERILDSFGLREYENRLVNSLSGGEI 165
Cdd:PRK13539 93 NL------EFWAA-------------------FLGGEEL--------------DIAAALEAVGLAPLAHLPFGYLSAGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 166 RRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL---LASNQTIVFISH 214
Cdd:PRK13539 134 RRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIrahLAQGGIVIAATH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-509 |
2.58e-12 |
|
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: 66.82 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIkiGYFDQSRKSISDDksL 412
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEV--LLDGKDIYDLDVD--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 IELFCPNGgdhiMVRGRNY--------------HVYGYLKNFLF-------------PKEFLDKPVGV-LSGGEKNRLAL 464
Cdd:cd03260 77 LELRRRVG----MVFQKPNpfpgsiydnvayglRLHGIKLKEELderveealrkaalWDEVKDRLHALgLSGGQQQRLCL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLD-IATINIlEEYLLSF--EGAILIVSHD 509
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDpISTAKI-EELIAELkkEYTIVIVTHN 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
331-486 |
2.76e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQ---SRK--S 405
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraaSRRvaS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 ISDDKSLIELFcpnGGDHIMVRGRNYHvygyLKNFLFPKE-----------------FLDKPVGVLSGGEKNRLALALLF 468
Cdd:PRK09536 82 VPQDTSLSFEF---DVRQVVEMGRTPH----RSRFDTWTEtdraaveramertgvaqFADRPVTSLSGGERQRVLLARAL 154
|
170
....*....|....*...
gi 1196666485 469 TKEYDCLILDEPTNDLDI 486
Cdd:PRK09536 155 AQATPVLLLDEPTASLDI 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-508 |
2.83e-12 |
|
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: 65.25 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLS-KTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRgeikigyfdqsrksisddks 411
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 412 lielfcPNGGDHIMVRGRNYHVYGYLknflfpKEFLDKPVG-VLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATin 490
Cdd:cd03223 61 ------PEGEDLLFLPQRPYLPLGTL------REQLIYPWDdVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES-- 126
|
170 180
....*....|....*....|..
gi 1196666485 491 ilEEYLLSF---EGAILI-VSH 508
Cdd:cd03223 127 --EDRLYQLlkeLGITVIsVGH 146
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
332-509 |
2.88e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 66.61 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDN-----KVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIGyfDQSRKSI 406
Cdd:COG1136 4 LLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTS-----GEVLID--GQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDDKsLIELfcpnggdhimvrgRNYHVyGY-------------LKNFLFP------------------------KEFLDK 449
Cdd:COG1136 76 SERE-LARL-------------RRRHI-GFvfqffnllpeltaLENVALPlllagvsrkerrerarellervglGDRLDH 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 450 PVGVLSGGEKNRLAL--ALLftKEYDCLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSHD 509
Cdd:COG1136 141 RPSQLSGGQQQRVAIarALV--NRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-216 |
2.95e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisiemlaqspKFNDN--- 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI---------------RFHGTdvs 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 -LSVKDA------LNYELkeiFDARDEYEKVLAQISnehdnpeLLHRQdelvkfiESKDGWNIENKIERILDSFGLREYE 153
Cdd:PRK10851 68 rLHARDRkvgfvfQHYAL---FRHMTVFDNIAFGLT-------VLPRR-------ERPNAAAIKAKVTQLLEMVQLAHLA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDR 216
Cdd:PRK10851 131 DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQvrkeLRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
350-528 |
3.71e-12 |
|
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: 65.98 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSISddksliELFCPNG-GDHIMVR- 427
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVS------MLFQENNlFAHLTVEq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 428 ----GRN----------YHVYGYLKNFLFPKEFLDKPvGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILE 493
Cdd:cd03298 90 nvglGLSpglkltaedrQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1196666485 494 EYLLSF----EGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03298 169 DLVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-191 |
3.82e-12 |
|
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: 66.14 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 11 KKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG---ECEIDSGRVI---RQNSI-----SIEMLAQSPKFND 79
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILfngQPRKPdqfqkCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 NLSVKDALNYelkeifdardeyekvLAQISnehdnpelLHRqdELVKFIESKdgwniENKIERILDsFGLREYENRLVNS 159
Cdd:cd03234 95 GLTVRETLTY---------------TAILR--------LPR--KSSDAIRKK-----RVEDVLLRD-LALTRIGGNLVKG 143
|
170 180 190
....*....|....*....|....*....|..
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:cd03234 144 ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
363-516 |
3.85e-12 |
|
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: 65.71 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 363 IVGRNGSGKSTMLKILL----GELEADSgvinrgeiKIGYFDQSRKSISDDKSLIEL-FCPNGGDHIMVRgRNYHVYgyl 437
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNS--------KGGAHDPKLIREGEVRAQVKLaFENANGKKYTIT-RSLAIL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 438 KNFLF-PKEFLDKP----VGVLSGGEKN------RLALALLFTKEYDCLILDEPTNDLD-----IATINILEEYLLSFEG 501
Cdd:cd03240 95 ENVIFcHQGESNWPlldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNF 174
|
170
....*....|....*
gi 1196666485 502 AILIVSHDRYFIDKI 516
Cdd:cd03240 175 QLIVITHDEELVDAA 189
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
334-528 |
4.97e-12 |
|
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: 65.51 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVL-FSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI--NRGEI------KIGYFDQSRK 404
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvNGQDVsdlrgrAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 405 SISDDKSLIelfcPNggdhimvrgRNyhVYgylKNFLFPKEFLDKP--------------VGV----------LSGGEKN 460
Cdd:cd03292 82 VVFQDFRLL----PD---------RN--VY---ENVAFALEVTGVPpreirkrvpaalelVGLshkhralpaeLSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 461 RLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGA---ILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-216 |
4.97e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.82 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSIS---IEMLAQS 74
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedVTHRSIQqrdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 75 PKFNDNLSVKDALNYELKeifdardeyekvLAQISNEhdnpELLHRQDELVKFIEskdgwnienkieriLDSFglreyEN 154
Cdd:PRK11432 87 YALFPHMSLGENVGYGLK------------MLGVPKE----ERKQRVKEALELVD--------------LAGF-----ED 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 155 RLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVYMVRFL----EELLLASNQTIVFISHDR 216
Cdd:PRK11432 132 RYVDQISGGQQQRVALArALILK-PKVLLFDEPLSNLDANLRRSMrekiRELQQQFNITSLYVTHDQ 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
343-509 |
5.49e-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: 68.54 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSISD--------DKSL 412
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVcaqdahlfDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 IE---LFCPNGGD------------HIMVRGRnyhvygylknflfpKEFLDKPVG----VLSGGEKNRLALALLFTKEYD 473
Cdd:TIGR02868 426 REnlrLARPDATDeelwaalervglADWLRAL--------------PDGLDTVLGeggaRLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196666485 474 CLILDEPTNDLDIATINILEEYLLSF--EGAILIVSHD 509
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
336-533 |
5.60e-12 |
|
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: 64.88 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKV------LFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEadsGVINRGEIKIGYFDQSRKSIsdd 409
Cdd:cd03213 7 RNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVLINGRPLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 410 KSLIelfcpnggdhIMVRgRNYHVYGYLKnflfPKEFLDKPVGV--LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA 487
Cdd:cd03213 81 RKII----------GYVP-QDDILHPTLT----VRETLMFAAKLrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1196666485 488 TINILEEYL--LSFEGAILIVS-HD-RYFIDKITNKLWAYENGKIeqIYM 533
Cdd:cd03213 146 SALQVMSLLrrLADTGRTIICSiHQpSSEIFELFDKLLLLSQGRV--IYF 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-485 |
5.62e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKS-TLMKILR-----------------GECEIDSG----RVIRQNSISieMLAQSP 75
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsppvvypsgdirfhGESLLHASeqtlRGVRGNKIA--MIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 76 KFNDNlsvkdalnyELKEIfdardeyEKVLAQISNehdnpelLHRqdelvkfieskdGWNIE---NKIERILDSFGLREY 152
Cdd:PRK15134 102 MVSLN---------PLHTL-------EKQLYEVLS-------LHR------------GMRREaarGEILNCLDRVGIRQA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 153 ENRLVN---SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDRYFIDRLATR 225
Cdd:PRK15134 147 AKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 226 SVEIEDGalRSFDGGYANYLTKkeeilrslAKSHETLIKNLKSEeewlrrgvkarlkrNEGRKqriLAMREEAkknPGLi 305
Cdd:PRK15134 227 VAVMQNG--RCVEQNRAATLFS--------APTHPYTQKLLNSE--------------PSGDP---VPLPEPA---SPL- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 306 rrvkLELERASKSFNGgglnqnrKKMLFEcknlsKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEAd 385
Cdd:PRK15134 276 ----LDVEQLQVAFPI-------RKGILK-----RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 386 sgvinRGEIkigYFDQ------SRKSISDDKSLIELFC--PNGG-------DHIMVRGRNYH------------VYGYLK 438
Cdd:PRK15134 339 -----QGEI---WFDGqplhnlNRRQLLPVRHRIQVVFqdPNSSlnprlnvLQIIEEGLRVHqptlsaaqreqqVIAVME 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 439 N--------FLFPKEFldkpvgvlSGGEKNRLALALLFTKEYDCLILDEPTNDLD 485
Cdd:PRK15134 411 EvgldpetrHRYPAEF--------SGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
334-551 |
5.98e-12 |
|
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: 68.29 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLG--ELEADSG-VINRGEI--KIGYFDQSRKSISD 408
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGrIIYHVALceKCGYVERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 409 DKSLIELFCPNGGDH----------------IMVRgRNYHVYG---YLKNFL-------FP-KEFLDKPVGV-------- 453
Cdd:TIGR03269 82 CPVCGGTLEPEEVDFwnlsdklrrrirkriaIMLQ-RTFALYGddtVLDNVLealeeigYEgKEAVGRAVDLiemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 454 --------LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLsfEGAI------LIVSHDRYFIDKITNK 519
Cdd:TIGR03269 161 rithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKasgismVLTSHWPEVIEDLSDK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1196666485 520 LWAYENGKIEQI---------YMEYSEYLDIEEELNQLSDI 551
Cdd:TIGR03269 239 AIWLENGEIKEEgtpdevvavFMEGVSEVEKECEVEVGEPI 279
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-254 |
6.29e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSI-------------SIEMLAQSPkfnDNlsvkd 85
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysrkglmklreSVGMVFQDP---DN----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 alnyelkEIFDArdeyeKVLAQISNEHDNPELlhRQDElvkfieskdgwnIENKIERILDSFGLREYENRLVNSLSGGEI 165
Cdd:PRK13636 94 -------QLFSA-----SVYQDVSFGAVNLKL--PEDE------------VRKRVDNALKRTGIEHLKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 166 RRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGALrSFDGGY 241
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV-ILQGNP 226
|
250
....*....|...
gi 1196666485 242 ANYLTKKeEILRS 254
Cdd:PRK13636 227 KEVFAEK-EMLRK 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
346-481 |
7.78e-12 |
|
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: 65.15 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 346 VLFsDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-------------RGEIKIGYFDQSRksisddksl 412
Cdd:cd03224 15 ILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditglppheRARAGIGYVPEGR--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 iELFcpnggDHIMVRGrNYHVYGYLKNF------------LFP--KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILD 478
Cdd:cd03224 85 -RIF-----PELTVEE-NLLLGAYARRRakrkarlervyeLFPrlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
...
gi 1196666485 479 EPT 481
Cdd:cd03224 158 EPS 160
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
351-509 |
8.44e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 351 FNARVLQGERIGIVGRNGSGKSTMLKILLGELEAdsgvinRGEIkigYFDQsrKSISD----------------DKSL-- 412
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG------QGEI---LLNG--RPLSDwsaaelarhraylsqqQSPPfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ------IELFCPNGGDHIMVRGRNYHVYGYLKnfLFPKefLDKPVGVLSGGEKNRLALALLFTK-------EYDCLILDE 479
Cdd:COG4138 84 mpvfqyLALHQPAGASSEAVEQLLAQLAEALG--LEDK--LSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1196666485 480 PTNDLDI----ATINILEEYLLSfEGAILIVSHD 509
Cdd:COG4138 160 PMNSLDVaqqaALDRLLRELCQQ-GITVVMSSHD 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-214 |
9.52e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.70 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL------------RGECEIDSGRVIRQNSIS- 67
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 ---IEMLAQSPKFNDNLSVKD--ALNYELKEIFDARDEYEKVLAQIsnehdnpellhrqdelvkfIESKDGWNienkier 142
Cdd:PRK14247 81 rrrVQMVFQIPNPIPNLSIFEnvALGLKLNRLVKSKKELQERVRWA-------------------LEKAQLWD------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 143 ildsfglrEYENRL---VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISH 214
Cdd:PRK14247 135 --------EVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFleLKKDMTIVLVTH 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-234 |
9.61e-12 |
|
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: 65.15 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDK----IILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisieMLAQSPKF 77
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV---------RLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 78 ndnlsvkdALNyelkEifDARdeyekvlAQISNEH-----------------DN---P-ELLHRQDelvkfieskdgwnI 136
Cdd:COG4181 78 --------ALD----E--DAR-------ARLRARHvgfvfqsfqllptltalENvmlPlELAGRRD-------------A 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 137 ENKIERILDSFGLREYENRLVNSLSGGEIRRVALG-ALILkKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVF 211
Cdd:COG4181 124 RARARALLERVGLGHRLDHYPAQLSGGEQQRVALArAFAT-EPAILFADEPTGNLDAATGEQIIDLLFELNRergtTLVL 202
|
250 260
....*....|....*....|...
gi 1196666485 212 ISHDRYFIDRlATRSVEIEDGAL 234
Cdd:COG4181 203 VTHDPALAAR-CDRVLRLRAGRL 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-224 |
1.02e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 67.92 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IR---QNSI--SIEMLAQSPK-FNDNlsvkd 85
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdIRdvtQASLraAIGIVPQDTVlFNDT----- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 alnyelkeIF--------DA-RDEYEKV--LAQIsneHDnpellhrqdelvkFIES-KDGWniENKI-ERildsfGLRey 152
Cdd:COG5265 448 --------IAyniaygrpDAsEEEVEAAarAAQI---HD-------------FIESlPDGY--DTRVgER-----GLK-- 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 153 enrlvnsLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVR-FLEEL-LLASNQTIVFISHdryfidRLAT 224
Cdd:COG5265 495 -------LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERaIQAALrEVARGRTTLVIAH------RLST 555
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-486 |
1.03e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGrvirqnsiSIEMLAQSPKFNDnl 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAG--------SILYLGKEVTFNG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 svkdalnyelkeifdARDEYEkvlAQISNEHDN----PEL-------LHRqdELVKFIESKDGWNIENKIERILDSFGLR 150
Cdd:PRK10762 73 ---------------PKSSQE---AGIGIIHQElnliPQLtiaenifLGR--EFVNRFGRIDWKKMYAEADKLLARLNLR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHL-DV---YMVRFLEELLlASNQTIVFISHdryfidRLaTRS 226
Cdd:PRK10762 133 FSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTeteSLFRVIRELK-SQGRGIVYISH------RL-KEI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 227 VEIEDG--ALRsfDGGYANyltkkEEILRSLakSHETLIKNL---KSEEEWLRrgvkarlkrnegrkqrilamreeakkn 301
Cdd:PRK10762 205 FEICDDvtVFR--DGQFIA-----EREVADL--TEDSLIEMMvgrKLEDQYPR--------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 302 pglirrvklelerasksfngggLNQNRKKMLFECKNLSKTIDNKVLFSdfnarVLQGERIGIVGRNGSGKSTMLKILLGE 381
Cdd:PRK10762 249 ----------------------LDKAPGEVRLKVDNLSGPGVNDVSFT-----LRKGEILGVSGLMGAGRTELMKVLYGA 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 382 LEADSGVI--NRGEIK-----------IGYFDQSRK--------SISDDKSLIEL-FCPNGGDHIMVRGRNYHVYGYLKN 439
Cdd:PRK10762 302 LPRTSGYVtlDGHEVVtrspqdglangIVYISEDRKrdglvlgmSVKENMSLTALrYFSRAGGSLKHADEQQAVSDFIRL 381
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1196666485 440 FLFPKEFLDKPVGVLSGGEKNRLALAL-LFTKEyDCLILDEPTNDLDI 486
Cdd:PRK10762 382 FNIKTPSMEQAIGLLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-187 |
1.19e-11 |
|
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: 64.76 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-------RQNSISI-EM-LAQSPK----FnDNLSVK 84
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditGLPPHERaRAgIGYVPEgrriF-PELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DalNYELKEIFDARDEYEKvlaqisnehdnpellhrqdelvkfieskdgwnienKIERILDSF-GLREYENRLVNSLSGG 163
Cdd:cd03224 94 E--NLLLGAYARRRAKRKA-----------------------------------RLERVYELFpRLKERRKQLAGTLSGG 136
|
170 180
....*....|....*....|....*
gi 1196666485 164 EIRRVALG-ALILKkPDVLLLDEPT 187
Cdd:cd03224 137 EQQMLAIArALMSR-PKLLLLDEPS 160
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
334-528 |
1.34e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.09 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeleaDSGV-INRGEIKIgyfdqsrksisDDKSL 412
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYeVTEGEILF-----------KGEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 IELfcpnggdHIMVRGRNyhvyGYLKNFLFP--------KEFLdKPVGV-LSGGEKNRLALALLFTKEYDCLILDEPTND 483
Cdd:cd03217 67 TDL-------PPEERARL----GIFLAFQYPpeipgvknADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1196666485 484 LDIATINILEE---YLLSFEGAILIVSHDRYFIDKI-TNKLWAYENGKI 528
Cdd:cd03217 135 LDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-232 |
1.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.45 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNsisIEMLAQSPKFND-NLSVKDALNYELKE 93
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG---VDITDKKVKLSDiRKKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 IFDarDEYEKVLAQisnehdNPELLHRQDElvkfieskdgwNIENKIERILDSFGL--REYENRLVNSLSGGEIRRVALG 171
Cdd:PRK13637 96 LFE--ETIEKDIAF------GPINLGLSEE-----------EIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 172 ALILKKPDVLLLDEPTNHLD-------VYMVRFLEElllASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-223 |
1.47e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 65.84 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMK-ILR--GECEIDSGRV-----------------IRQNSISieMLAQSPkfndnLS 82
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARaILGllPPPGITSGEIlfdgedllklsekelrkIRGREIQ--MIFQDP-----MT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vkdALN--YelkeifdardeyeKVLAQISnEhdnPELLHRqdelvkfIESKDgwNIENKIERILDSFGLREYENRLvNS- 159
Cdd:COG0444 98 ---SLNpvM-------------TVGDQIA-E---PLRIHG-------GLSKA--EARERAIELLERVGLPDPERRL-DRy 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 160 ---LSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDV--------YMVRFLEELllasNQTIVFISHD----RYFIDRLA 223
Cdd:COG0444 148 pheLSGGMRQRVMIArALALE-PKLLIADEPTTALDVtiqaqilnLLKDLQREL----GLAILFITHDlgvvAEIADRVA 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
335-531 |
1.54e-11 |
|
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: 66.29 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 335 CKNLSKTIDNKVLfsDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG--VINrGEI---------------KIG 397
Cdd:TIGR02142 2 SARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeiVLN-GRTlfdsrkgiflppekrRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 398 Y-FDQSRksisddkslieLFcpnggDHIMVRGrNYhVYGY------LKNFLFPK--------EFLDKPVGVLSGGEKNRL 462
Cdd:TIGR02142 79 YvFQEAR-----------LF-----PHLSVRG-NL-RYGMkrarpsERRISFERviellgigHLLGRLPGRLSGGEKQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 463 ALALLFTKEYDCLILDEPTNDLDIATINILEEYL----LSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:TIGR02142 141 AIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLerlhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
334-530 |
1.59e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIgyfDQSRkSISDDKSLI 413
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI---DTAR-SLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 elfcpnggdhimvRGRNYHVYGYLKNF-LFP---------------------------KEFLDKpVGV----------LS 455
Cdd:PRK11264 81 -------------RQLRQHVGFVFQNFnLFPhrtvleniiegpvivkgepkeeataraRELLAK-VGLagketsyprrLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 456 GGEKNRLALALLFTKEYDCLILDEPTNDLD-------IATINILEEYllsfEGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQE----KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
...
gi 1196666485 529 -EQ 530
Cdd:PRK11264 223 vEQ 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-215 |
1.87e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKIL------RGECEIDsGRVIRQnsISIEMLA---------QSPKFNdnLSVkdal 87
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMagllpgQGEILLN-GRPLSD--WSAAELArhraylsqqQSPPFA--MPV---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 88 nYELkeifdardeyekvLAqisnehdnpelLHRQDELVKFieskdgwNIENKIERILDSFGLREYENRLVNSLSGGEIRR 167
Cdd:COG4138 87 -FQY-------------LA-----------LHQPAGASSE-------AVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 168 VALGALILK-KPDV------LLLDEPTNHLDVY----MVRFLEELLLASNqTIVFISHD 215
Cdd:COG4138 135 VRLAAVLLQvWPTInpegqlLLLDEPMNSLDVAqqaaLDRLLRELCQQGI-TVVMSSHD 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-232 |
1.90e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILrGECEI-DSGrvirqnsiSIEMLAQSPKFNDNLS 82
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLETpDSG--------QLNIAGHQFDFSQKPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALnyELKEifdardeyeKVLAQISNEHDNPELLHRQDelvkFIE--------SKDGWNIenKIERILDSFGLREYEN 154
Cdd:COG4161 74 EKAIR--LLRQ---------KVGMVFQQYNLWPHLTVMEN----LIEapckvlglSKEQARE--KAMKLLARLRLTDKAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD-------VYMVRFLEElllaSNQTIVFISHDRYFIDRLATRSV 227
Cdd:COG4161 137 RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvVEIIRELSQ----TGITQVIVTHEVEFARKVASQVV 212
|
....*
gi 1196666485 228 EIEDG 232
Cdd:COG4161 213 YMEKG 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-216 |
1.93e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------------RQNsis 67
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfegedistlkpeiyRQQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 IEMLAQSPK-FNDnlSVKDALnyelkeIFDArdeyekvlaQISNEHDNPellhrqdelvkfieskdgwnieNKIERILDS 146
Cdd:PRK10247 83 VSYCAQTPTlFGD--TVYDNL------IFPW---------QIRNQQPDP----------------------AIFLDDLER 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 147 FGLREYE-NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTI--VFISHDR 216
Cdd:PRK10247 124 FALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIhrYVREQNIavLWVTHDK 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-216 |
2.05e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.12 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-------------RQnsisIE 69
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqdithvpaenRH----VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 70 MLAQSPKFNDNLSVKDALNYELKeifdardeYEKVLAQisnehdnpellhrqdelvkfieskdgwNIENKIERILDSFGL 149
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLR--------MQKTPAA---------------------------EITPRVMEALRMVQL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 150 REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDvYMVRFLEELLLASNQ-----TIVFISHDR 216
Cdd:PRK09452 135 EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD-YKLRKQMQNELKALQrklgiTFVFVTHDQ 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-531 |
2.49e-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: 63.43 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSISddksli 413
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 elfcpnggdhiMVRgRNYHVYGYL---KNFLFP------------------------KEFLDKPVGVLSGGEKNRLALAL 466
Cdd:cd03301 76 -----------MVF-QNYALYPHMtvyDNIAFGlklrkvpkdeidervrevaellqiEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 467 LFTKEYDCLILDEPTNDLD----IATINILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-507 |
2.62e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSIS------ 67
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILsgvyqpdSGEILLD-GEPVRFRSPRdaqaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 IEMLAQspKFN--DNLSVkdALNyelkeIFdardeyekvlaqISNEHDNPELLHRQDelvkfieskdgwnIENKIERILD 145
Cdd:COG1129 81 IAIIHQ--ELNlvPNLSV--AEN-----IF------------LGREPRRGGLIDWRA-------------MRRRARELLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 146 SFGLREYENRLVNSLSGG-----EIRRvalgALIlKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISHdry 217
Cdd:COG1129 127 RLGLDIDPDTPVGDLSVAqqqlvEIAR----ALS-RDARVLILDEPTASLTEREVERLFRIirrLKAQGVAIIYISH--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 218 FID---RLATR-SVeiedgaLRsfDGGYANYLTKKEEilrslakSHETLIKNLkseeewlrrgVkarlkrneGRKqrILA 293
Cdd:COG1129 199 RLDevfEIADRvTV------LR--DGRLVGTGPVAEL-------TEDELVRLM----------V--------GRE--LED 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 294 MREEAKKNPGlirrvklelerasksfnggglnqnrkKMLFECKNLSKtidnKVLFSDFNARVLQGERIGIVGRNGSGKST 373
Cdd:COG1129 244 LFPKRAAAPG--------------------------EVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 374 MLKILLGELEADSGVIN-RGE----------IK--IGYFDQSRK--------SISDDKSL--IELFCPNGgdhiMVRGRn 430
Cdd:COG1129 294 LARALFGADPADSGEIRlDGKpvrirsprdaIRagIAYVPEDRKgeglvldlSIRENITLasLDRLSRGG----LLDRR- 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 431 yhvygylknflfpKEF----------------LDKPVGVLSGGEKNRLALA-LLFTkEYDCLILDEPTNDLDIAT----I 489
Cdd:COG1129 369 -------------RERalaeeyikrlriktpsPEQPVGNLSGGNQQKVVLAkWLAT-DPKVLILDEPTRGIDVGAkaeiY 434
|
570
....*....|....*....
gi 1196666485 490 NILEEylLSFEG-AILIVS 507
Cdd:COG1129 435 RLIRE--LAAEGkAVIVIS 451
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-215 |
2.67e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.75 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFG---DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsISIEMLAQspkf 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII----IDGDLLTE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 78 nDNlsvkdalnyelkeIFDARDEYEKVLAQISNEHDNPELlhrQDELVKFIESKdGWNIENKIERI---LDSFGLREYEN 154
Cdd:PRK13650 74 -EN-------------VWDIRHKIGMVFQNPDNQFVGATV---EDDVAFGLENK-GIPHEEMKERVneaLELVGMQDFKE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHD 215
Cdd:PRK13650 136 REPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
331-528 |
2.98e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.72 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKV-----LFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgEIKIGYFDQSRKS 405
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG-----TIEWIFKDEKNKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 ISDDKSLI---------------------------------ELFCPNGGDHIMVRGRNYHV---------YGYLKNFLFP 443
Cdd:PRK13651 76 KTKEKEKVleklviqktrfkkikkikeirrrvgvvfqfaeyQLFEQTIEKDIIFGPVSMGVskeeakkraAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 444 KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD----IATINILEEylLSFEG-AILIVSHDRYFIDKITN 518
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN--LNKQGkTIILVTHDLDNVLEWTK 233
|
250
....*....|
gi 1196666485 519 KLWAYENGKI 528
Cdd:PRK13651 234 RTIFFKDGKI 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-215 |
3.50e-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: 63.51 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 10 SKKFGDKIILNEtNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-------------RQNSISIEMLAQSPk 76
Cdd:cd03299 7 SKDWKEFKLKNV-SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlppekRDISYVPQNYALFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 fndNLSVKDALNYELKEIFDARDEYEKVLAQISnehdnpELLHrqdelvkfieskdgwnienkIERILdsfglreyeNRL 156
Cdd:cd03299 85 ---HMTVYKNIAYGLKKRKVDKKEIERKVLEIA------EMLG--------------------IDHLL---------NRK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV-------YMVRFLEELllaSNQTIVFISHD 215
Cdd:cd03299 127 PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeklrEELKKIRKE---FGVTVLHVTHD 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-216 |
3.66e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.24 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEV---SKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQN-SIS--------IE 69
Cdd:PRK11607 15 ALTPLLEIrnlTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLShvppyqrpIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 70 MLAQSPKFNDNLSVKDALNYELKeifdardeyekvlaqisnehdnpellhrQDELVKFieskdgwNIENKIERILDSFGL 149
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLK----------------------------QDKLPKA-------EIASRVNEMLGLVHM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 150 REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD--------VYMVRFLEELllasNQTIVFISHDR 216
Cdd:PRK11607 140 QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQ 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-530 |
3.78e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 344 NKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSISDDKSLIELF----- 416
Cdd:PRK11160 353 QPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISVVSQRVHLFsatlr 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 417 ------CPNGGDHIMVR-----GrnyhvygyLKNFLFPKEFLDKPVG----VLSGGEKNRLALALLFTKEYDCLILDEPT 481
Cdd:PRK11160 432 dnlllaAPNASDEALIEvlqqvG--------LEKLLEDDKGLNAWLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 482 NDLDIAT-INILEEYLLSFEG-AILIVSHDRYFIDKItNKLWAYENGKI-EQ 530
Cdd:PRK11160 504 EGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQIiEQ 554
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
320-605 |
4.63e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.04 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 320 NGGGLNQNRKKMlfecKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLK---------------ILLGELEA 384
Cdd:PLN03073 169 NGGGPAIKDIHM----ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 385 ---DSGVIN---RGEIKIGYFDQSRKSISDDKSLIELFCPNGGDHIMVRG---------RNYHVY--------------- 434
Cdd:PLN03073 245 vgdDTTALQcvlNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDgvdkdavsqRLEEIYkrlelidaytaeara 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 435 -GYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFI 513
Cdd:PLN03073 325 aSILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 514 DKITNKLWAYENGKIEQIYMEYSEYLDIEEElnQLSDIEselgQSIETKEKQKT------SKVKLTYKQNQILQNHpalI 587
Cdd:PLN03073 405 NTVVTDILHLHGQKLVTYKGDYDTFERTREE--QLKNQQ----KAFESNERSRShmqafiDKFRYNAKRASLVQSR---I 475
|
330
....*....|....*...
gi 1196666485 588 EALEsRISELNHALSTPE 605
Cdd:PLN03073 476 KALD-RLGHVDAVVNDPD 492
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-191 |
4.75e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFG-----DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI----------------- 61
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdvtklpeykraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 62 ----RQN-------SISIE---MLAQSPKFNDNLSVkdALNYELKEIFDARdeyekvLAQISNehdnpellhrqdelvkf 127
Cdd:COG1101 82 igrvFQDpmmgtapSMTIEenlALAYRRGKRRGLRR--GLTKKRRELFREL------LATLGL----------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 128 ieskdgwnienkierildsfGLreyENRL---VNSLSGGEirRVALgALI---LKKPDVLLLDEPTNHLD 191
Cdd:COG1101 137 --------------------GL---ENRLdtkVGLLSGGQ--RQAL-SLLmatLTKPKLLLLDEHTAALD 180
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-223 |
4.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEV---SKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSgrvirqnsiSIEMLAQSPKFND 79
Cdd:PRK14258 4 LIPAIKVnnlSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES---------EVRVEGRVEFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 NlsvkdalnyelkeIFDARDEYEKVLAQISNEHDNPEL--LHRQDEL---VKFIeskdGWNIENKIERILDSfGLR---- 150
Cdd:PRK14258 75 N-------------IYERRVNLNRLRRQVSMVHPKPNLfpMSVYDNVaygVKIV----GWRPKLEIDDIVES-ALKdadl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 --EYENRLVNS---LSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDR 221
Cdd:PRK14258 137 wdEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
..
gi 1196666485 222 LA 223
Cdd:PRK14258 217 LS 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-235 |
5.09e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisiEMLAQspkfndNLSvkdALNYELKEIFDA 97
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEV--------SLVGQ------PLH---QMDEEARAKLRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 98 RDE----YEKVLAQISNEHDN---PELLHRQDELvkfiESKDGwnienkIERILDSFGLREYENRLVNSLSGGEIRRVAL 170
Cdd:PRK10584 88 KHVgfvfQSFMLIPTLNALENvelPALLRGESSR----QSRNG------AKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 171 GALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDryfiDRLAT---RSVEIEDGALR 235
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRehgtTLILVTHD----LQLAArcdRRLRLVNGQLQ 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-238 |
5.29e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 8 EVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRgeceidsgrviRQNSIsiemlaqspkfNDNLSVKDAL 87
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-----------RMNDL-----------NPEVTITGSI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 88 NYELKEIF-------DARDE---------------YEKVL--AQISNEHDNpellHRQDELVKfiESKDGWNIENKIERI 143
Cdd:PRK14239 68 VYNGHNIYsprtdtvDLRKEigmvfqqpnpfpmsiYENVVygLRLKGIKDK----QVLDEAVE--KSLKGASIWDEVKDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 144 LDSFGLreyenrlvnSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ--TIVFISHDRYFIDR 221
Cdd:PRK14239 142 LHDSAL---------GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASR 212
|
250
....*....|....*..
gi 1196666485 222 LATRSVEIEDGALRSFD 238
Cdd:PRK14239 213 ISDRTGFFLDGDLIEYN 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-260 |
5.47e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDsgrviRQNSISIEMLAQSPKFNDNLS 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-----KSAGSHIELLGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vkdalnyelKEIFDARDEYEKVLAQISnehdnpeLLHR----QDELVKFIESKDGWNI---------ENKIERILDSFGL 149
Cdd:PRK09984 79 ---------RDIRKSRANTGYIFQQFN-------LVNRlsvlENVLIGALGSTPFWRTcfswftreqKQRALQALTRVGM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 150 REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIVFISHDRYFIDRLATR 225
Cdd:PRK09984 143 VHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCER 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 1196666485 226 SVEIEDGALrSFDGGYANYLTKK-EEILRSLAKSHE 260
Cdd:PRK09984 223 IVALRQGHV-FYDGSSQQFDNERfDHLYRSINRVEE 257
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
333-487 |
5.51e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQsrKSISDDKSL 412
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS--KAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 IELFCPnGGDHIMVR-----GRnYHVYGYLKNF--------------LFPKEFLDKPVGVLSGGEKNRLALALLFTKEYD 473
Cdd:PRK10575 90 LPQQLP-AAEGMTVRelvaiGR-YPWHGALGRFgaadrekveeaislVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170
....*....|....
gi 1196666485 474 CLILDEPTNDLDIA 487
Cdd:PRK10575 168 CLLLDEPTSALDIA 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
351-509 |
5.71e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 351 FNARVLQGERIGIVGRNGSGKSTMLKILLGELEADsgvinrGEIkigYFDQsrKSISDdKSLIELfcpnggdhimVRGRN 430
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS------GSI---QFAG--QPLEA-WSAAEL----------ARHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 431 Y-----------HVYGYLKNFLFPK--------------------EFLDKPVGVLSGGEKNRLALALLFTK-------EY 472
Cdd:PRK03695 73 YlsqqqtppfamPVFQYLTLHQPDKtrteavasalnevaealgldDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1196666485 473 DCLILDEPTNDLDIATINILEEYLLSFE---GAILIVSHD 509
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
350-528 |
5.96e-11 |
|
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: 62.74 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-RGEI----------KIGYFDQSRKSISDDKSLIELFcp 418
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvAGLVpwkrrkkflrRIGVVFGQKTQLWWDLPVIDSF-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 419 nggdhimvrGRNYHVYGyLKNFLFPK------------EFLDKPVGVLSGGEKNR--LALALLFTKEYdcLILDEPTNDL 484
Cdd:cd03267 117 ---------YLLAAIYD-LPPARFKKrldelselldleELLDTPVRQLSLGQRMRaeIAAALLHEPEI--LFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 485 DIATINILEEYLLSF----EGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:cd03267 185 DVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-242 |
6.59e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkFNDn 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV---------------FDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 lsvKDALNYE----LKEIFDARDEYEKVLAQISNEHDNpellhrqdELVKFIESKDGWniENKIERILDSFGlREYENRL 156
Cdd:PRK11614 67 ---KDITDWQtakiMREAVAIVPEGRRVFSRMTVEENL--------AMGGFFAERDQF--QERIKWVYELFP-RLHERRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 157 --VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHL-DVYMVRFLE--ELLLASNQTIVFISHDRYFIDRLATRSVEIED 231
Cdd:PRK11614 133 qrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLaPIIIQQIFDtiEQLREQGMTIFLVEQNANQALKLADRGYVLEN 212
|
250
....*....|.
gi 1196666485 232 GALRSFDGGYA 242
Cdd:PRK11614 213 GHVVLEDTGDA 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
154-238 |
6.78e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVR----FLEELLLASNQTIVFISHDRYFIDRLATRSVEI 229
Cdd:PRK11144 123 DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRellpYLERLAREINIPILYVSHSLDEILRLADRVVVL 202
|
....*....
gi 1196666485 230 EDGALRSFD 238
Cdd:PRK11144 203 EQGKVKAFG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
310-509 |
7.44e-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: 62.45 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 310 LELERASKSFngGGLnqnrkkmlfecknlsktidnKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:cd03219 1 LEVRGLTKRF--GGL--------------------VAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 390 nrgeikigYFDqsRKSISDDKS-------------LIELFcPNGG--DHIMVRGRNYHVYGYLKNFLFPKE--------- 445
Cdd:cd03219 58 --------LFD--GEDITGLPPheiarlgigrtfqIPRLF-PELTvlENVMVAAQARTGSGLLLARARREEreareraee 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 446 ---------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL--LSFEG-AILIVSHD 509
Cdd:cd03219 127 llervgladLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIreLRERGiTVLLVEHD 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
7.52e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSisiemlaqsPKFNDNLSvkdalnyelkeifDAR 98
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---------AITDDNFE-------------KLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DEYEKVLaqisnehDNPEllhrqDELVKFIESKD-GWNIEN----------KIERILDSFGLREYENRLVNSLSGGEIRR 167
Cdd:PRK13648 83 KHIGIVF-------QNPD-----NQFVGSIVKYDvAFGLENhavpydemhrRVSEALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 168 VALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHD 215
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDarqnLLDLVRKVKSEHNITIISITHD 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
343-488 |
8.89e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.80 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI----------NRGEI--KIGY-------FDQS- 402
Cdd:COG1132 352 DRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdlTLESLrrQIGVvpqdtflFSGTi 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 -------RKSISDDK-----------SLIELFcPNGGD-HIMVRGRNyhvygylknflfpkefldkpvgvLSGGEKNRLA 463
Cdd:COG1132 431 renirygRPDATDEEveeaakaaqahEFIEAL-PDGYDtVVGERGVN-----------------------LSGGQRQRIA 486
|
170 180
....*....|....*....|....*..
gi 1196666485 464 LA--LLftKEYDCLILDEPTNDLDIAT 488
Cdd:COG1132 487 IAraLL--KDPPILILDEATSALDTET 511
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-531 |
8.94e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQN------------SISIEM 70
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVkdalnyeLKEIFDARDEYEKVLAqisnehdnpellhrqdelVKFIESKDgwnIENKIERILDSFGLR 150
Cdd:PRK09700 85 IYQELSVIDELTV-------LENLYIGRHLTKKVCG------------------VNIIDWRE---MRVRAAMMLLRVGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVrflEELLLASNQ------TIVFISHDRYFIDRLAT 224
Cdd:PRK09700 137 VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEV---DYLFLIMNQlrkegtAIVYISHKLAEIRRICD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 225 RSVEIEDGAlrsfdggyanyltkkeeilrSLAKShetLIKNLkSEEEWLRRGVKARLkrnegrKQRILAMREEakknpgl 304
Cdd:PRK09700 214 RYTVMKDGS--------------------SVCSG---MVSDV-SNDDIVRLMVGREL------QNRFNAMKEN------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 305 irrvklelerasksfngggLNQNRKKMLFECKNLSKTIDNKVlfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEA 384
Cdd:PRK09700 257 -------------------VSNLAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 385 DSGVI--NRGEIK-----------IGYFDQSRK--------SISDDKSlIELFCPNGGdhimvrgrnyhvYGYLKNFLFP 443
Cdd:PRK09700 316 AGGEIrlNGKDISprspldavkkgMAYITESRRdngffpnfSIAQNMA-ISRSLKDGG------------YKGAMGLFHE 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 444 KE-----------------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL--LSFEG-AI 503
Cdd:PRK09700 383 VDeqrtaenqrellalkchSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMrqLADDGkVI 462
|
570 580
....*....|....*....|....*...
gi 1196666485 504 LIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:PRK09700 463 LMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-509 |
9.01e-11 |
|
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: 64.81 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSG----------VINR---------------GEI----KIGYFDQSRKSIS 407
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGdydeepswdeVLKRfrgtelqdyfkklanGEIkvahKPQYVDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 408 DD-KSLIElfcpnGGDHimvRGrnyhVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDI 486
Cdd:COG1245 178 GTvRELLE-----KVDE---RG----KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*..
gi 1196666485 487 ----ATINILEEyLLSFEGAILIVSHD 509
Cdd:COG1245 246 yqrlNVARLIRE-LAEEGKYVLVVEHD 271
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
322-485 |
9.12e-11 |
|
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: 64.74 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 322 GGLNQNRKKMLFECKNLSKTI---DNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG--VINRGEIKI 396
Cdd:TIGR02203 320 GTRAIERARGDVEFRNVTFRYpgrDRPAL-DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqiLLDGHDLAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 397 GYFDQSRKSISDDKSLIELF----CPN-----GGDHIMVRGRNYHVYGYLKNFL--FPKEfLDKPVGV----LSGGEKNR 461
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLFndtiANNiaygrTEQADRAEIERALAAAYAQDFVdkLPLG-LDTPIGEngvlLSGGQRQR 477
|
170 180
....*....|....*....|....
gi 1196666485 462 LALALLFTKEYDCLILDEPTNDLD 485
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALD 501
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
327-527 |
1.06e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.70 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 327 NRKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-RGEIKIGYFDQSRKS 405
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 I---SDDKSLIELFCPNggDHIMVRGRNYHVYGYLKNFLFPK--EF------LDKPVGVLSGGEKNRLALALLFTKEYDC 474
Cdd:PRK13536 116 IgvvPQFDNLDLEFTVR--ENLLVFGRYFGMSTREIEAVIPSllEFarleskADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 475 LILDEPTNDLDIATINILEEY---LLSFEGAILIVSHDRYFIDKITNKLWAYENGK 527
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERlrsLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
343-488 |
1.11e-10 |
|
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: 62.25 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSIS---DDKSL----- 412
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGvvpQDTVLfndti 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ---IELFCPNGGDHIMVRG-RNYHVYGYLKNFlfPKEFlDKPVG----VLSGGEKNRLALALLFTKEYDCLILDEPTNDL 484
Cdd:cd03253 92 gynIRYGRPDATDEEVIEAaKAAQIHDKIMRF--PDGY-DTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
....
gi 1196666485 485 DIAT 488
Cdd:cd03253 169 DTHT 172
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-214 |
1.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.80 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 16 KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRqnsisiemlaqspkfnDNLSVKDALNyelkeIF 95
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV----------------DGLDTSDEEN-----LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 96 DARDEYEKVLaqisNEHDNPELLHRQDELVKF------IESKDgwnIENKIERILDSFGLREYENRLVNSLSGGEIRRVA 169
Cdd:PRK13633 82 DIRNKAGMVF----QNPDNQIVATIVEEDVAFgpenlgIPPEE---IRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1196666485 170 LGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISH 214
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSgrreVVNTIKELNKKYGITIILITH 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
331-486 |
1.13e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFdqSRKSISDDK 410
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLI--ELFCPNGgdhIMVR-----GRNYHV--YGYLK-----------NFLFPKEFLDKPVGVLSGGEKNRLALALLFTK 470
Cdd:PRK11231 79 ALLpqHHLTPEG---ITVRelvayGRSPWLslWGRLSaednarvnqamEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170
....*....|....*.
gi 1196666485 471 EYDCLILDEPTNDLDI 486
Cdd:PRK11231 156 DTPVVLLDEPTTYLDI 171
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
7-232 |
1.18e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.58 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 7 IEVSKKFGDkIILnETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------RQNSIS-------IEML 71
Cdd:COG4148 5 VDFRLRRGG-FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdSARGIFlpphrrrIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 72 AQSPKFNDNLSVKDALNYELKEIFDARDEYEkvLAQISnehdnpELLHrqdelvkfieskdgwnienkIERILDsfglre 151
Cdd:COG4148 83 FQEARLFPHLSVRGNLLYGRKRAPRAERRIS--FDEVV------ELLG--------------------IGHLLD------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 yenRLVNSLSGGEIRRVALG-ALiLKKPDVLLLDEPTNHLDV--------YMVRFLEELLLAsnqtIVFISHDRYFIDRL 222
Cdd:COG4148 129 ---RRPATLSGGERQRVAIGrAL-LSSPRLLLMDEPLAALDLarkaeilpYLERLRDELDIP----ILYVSHSLDEVARL 200
|
250
....*....|
gi 1196666485 223 ATRSVEIEDG 232
Cdd:COG4148 201 ADHVVLLEQG 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-224 |
1.27e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 61.79 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMK-ILR------GECEIDsGRVIRQNSIS-----IEMLAQSPKFNDNlS 82
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSlLERfydptsGEILLD-GVDIRDLNLRwlrsqIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYELkeiFDARDEYEKVLAQISNEHDnpellhrqdelvkFIESkdgwnIENKIERILDSFGLReyenrlvnsLSG 162
Cdd:cd03249 93 IAENIRYGK---PDATDEEVEEAAKKANIHD-------------FIMS-----LPDGYDTLVGERGSQ---------LSG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT 224
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALdrAMKGRTTIVIAH------RLST 200
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
331-531 |
1.41e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 63.24 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigyfdqsrksisddk 410
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 slieLFcpNGGD---HIMVRGRNyhVyGYLknF----LFP--------------------------KEFLDKpVGV---- 453
Cdd:COG1118 60 ----VL--NGRDlftNLPPRERR--V-GFV--FqhyaLFPhmtvaeniafglrvrppskaeirarvEELLEL-VQLegla 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 454 ------LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLS----FEGAILIVSHDRyfidkitnkLWAY 523
Cdd:COG1118 128 drypsqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhdeLGGTTVFVTHDQ---------EEAL 198
|
250
....*....|....*..
gi 1196666485 524 E---------NGKIEQI 531
Cdd:COG1118 199 EladrvvvmnQGRIEQV 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-215 |
1.59e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 22 TNFNVNEKERIAIIGKNGGGKSTLMK----ILRGECEIDsgrvirqnsisiemlaqspkFNDnlsvKDALNYELKEIfdA 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLLPGSGSIQ--------------------FAG----QPLEAWSAAEL--A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 98 RdeYEKVLAQisneHDNPEL---------LHRQDELVKFieskdgwNIENKIERILDSFGLREYENRLVNSLSGGEIRRV 168
Cdd:PRK03695 69 R--HRAYLSQ----QQTPPFampvfqyltLHQPDKTRTE-------AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 169 ALGALILK-----KPD--VLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHD 215
Cdd:PRK03695 136 RLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD 192
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-232 |
1.61e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILrGECEI-DSGRV-IRQNSISiemLAQSPKfndnl 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMpRSGTLnIAGNHFD---FSKTPS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 svkdalnyeLKEIFDARDEYEKVLAQIsneHDNPELLHRQDelvkFIESK---DGWNIENKIER---ILDSFGLREYENR 155
Cdd:PRK11124 74 ---------DKAIRELRRNVGMVFQQY---NLWPHLTVQQN----LIEAPcrvLGLSKDQALARaekLLERLRLKPYADR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 156 LVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEElLLASNQTIVFISHDRYFIDRLATRSVEIED 231
Cdd:PRK11124 138 FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
.
gi 1196666485 232 G 232
Cdd:PRK11124 217 G 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-232 |
1.81e-10 |
|
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: 61.33 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSisiEMLAQSPkfnDNLSVKDalNYELKEIFDAR 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGP---DRMVVFQ--NYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DEYekVLAQISNEHDNPELLHRQdelvkfieskdgwnienKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKP 178
Cdd:TIGR01184 73 ENI--ALAVDRVLPDLSKSERRA-----------------IVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 179 DVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFISHDryfIDR---LATRSVEIEDG 232
Cdd:TIGR01184 134 KVLLLDEPFGALDALTRGNLQEELMqiweEHRVTVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-232 |
1.82e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRViRQNSISIEMLAQSPK----------FN 78
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV-SWRGEPLAKLNRAQRkafrrdiqmvFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLSvkdALNYElKEIFDARDEYEKVLAQISNEhdnpELLHRQDELvkfieskdgwnienkieriLDSFGLR-EYENRLV 157
Cdd:PRK10419 97 DSIS---AVNPR-KTVREIIREPLRHLLSLDKA----ERLARASEM-------------------LRAVDLDdSVLDKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 158 NSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK10419 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-224 |
2.05e-10 |
|
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: 61.09 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSIS-----IEMLAQSPK-FNDn 80
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILID-GIDIRDISRKslrsmIGVVLQDTFlFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 lSVKDALNYELKEifdARDEYEKVLAQISNEHDnpellhrqdelvkFIEskdgwNIENkierildsfGLREYENRLVNSL 160
Cdd:cd03254 92 -TIMENIRLGRPN---ATDEEVIEAAKEAGAHD-------------FIM-----KLPN---------GYDTVLGENGGNL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 161 SGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT 224
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH------RLST 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
2.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.93 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGD--KIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQNSIS----- 67
Cdd:PRK13632 6 VMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILtgllkpqSGEIKID-GITISKENLKeirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 IEMLAQSPkfnDN----LSVKDALNYELKeifdardeyekvlaqisNEHDNPEllhrqdelvkfieskdgwNIENKIERI 143
Cdd:PRK13632 85 IGIIFQNP---DNqfigATVEDDIAFGLE-----------------NKKVPPK------------------KMKDIIDDL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 144 LDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHD 215
Cdd:PRK13632 127 AKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKgkreIKKIMVDLRKTRKKTLISITHD 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
339-527 |
2.08e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 60.56 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 339 SKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEiKIGY-------------------- 398
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYvsqepwiqngtirenilfgk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 -FDQSR-KSISDDKSL---IELFCpnGGDHIMV--RGRNyhvygylknflfpkefldkpvgvLSGGEKNRLALALLFTKE 471
Cdd:cd03250 91 pFDEERyEKVIKACALepdLEILP--DGDLTEIgeKGIN-----------------------LSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 472 YDCLILDEPTNDLDIATIN-ILEEYL---LSFEGAILIVSHDRYFI---DKITnklwAYENGK 527
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRhIFENCIlglLLNNKTRILVTHQLQLLphaDQIV----VLDNGR 204
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
331-488 |
2.53e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLfECKNLSK-----TIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKS 405
Cdd:COG1101 1 ML-ELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 isddKSLIELF-------CPN-------------GGDHIMVRGRNYHVYGYLKNFLfpKEF-------LDKPVGVLSGGE 458
Cdd:COG1101 80 ----KYIGRVFqdpmmgtAPSmtieenlalayrrGKRRGLRRGLTKKRRELFRELL--ATLglglenrLDTKVGLLSGGQ 153
|
170 180 190
....*....|....*....|....*....|...
gi 1196666485 459 knRLALALL---FTKEyDCLILDEPTNDLDIAT 488
Cdd:COG1101 154 --RQALSLLmatLTKP-KLLLLDEHTAALDPKT 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
332-528 |
2.77e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTI-DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYfdqsrksisDDK 410
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY---------DKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLIE------LFCPNGGDHIMVRGRNYHV-YGYLkNFLFPKE-----------------FLDKPVGVLSGGEKNRLALAL 466
Cdd:PRK13639 72 SLLEvrktvgIVFQNPDDQLFAPTVEEDVaFGPL-NLGLSKEevekrvkealkavgmegFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 467 LFTKEYDCLILDEPTNDLD----IATINILeeYLLSFEGAILIVS-HDRYFIDKITNKLWAYENGKI 528
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDpmgaSQIMKLL--YDLNKEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-234 |
3.87e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 13 FGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDSGRVIRQNSIS----IEMLAQSPKFNDNL 81
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLsrlmtpaHGHVWLDGEHIQHYASKEvarrIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKDALnyelkeifdARDEYEkvlaqisneHDNPELLHRQDElvkfieskdgwniENKIERILDSFGLREYENRLVNSLS 161
Cdd:PRK10253 97 TVQELV---------ARGRYP---------HQPLFTRWRKED-------------EEAVTKAMQATGITHLADQSVDTLS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGAL 234
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShqidLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-234 |
4.48e-10 |
|
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: 60.18 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNS-IS----------IEMLAQSPKFNDNlSV 83
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpISqyehkylhskVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDALNYELKeifDARDEYEKVLAQISNEHDN-PELLHRQDELVkfieskdgwnienkierilDSFGlreyenrlvNSLSG 162
Cdd:cd03248 105 QDNIAYGLQ---SCSFECVKEAAQKAHAHSFiSELASGYDTEV-------------------GEKG---------SQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA--SNQTIVFISHDRYFIDRlATRSVEIEDGAL 234
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-509 |
4.60e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.80 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 355 VLQGERIGIVGRNGSGKSTMLKILLGELEADSGVinrgeIKIGYFDQSRKSISDDKSLIELFCPNgGDHIMVRG--RNYH 432
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT-----ITVGGMVLSEETVWDVRRQVGMVFQN-PDNQFVGAtvQDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 433 VYGyLKNFLFPKE-----------------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD-------IAT 488
Cdd:PRK13635 104 AFG-LENIGVPREemvervdqalrqvgmedFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLET 182
|
170 180
....*....|....*....|...
gi 1196666485 489 INILEEyllsfEGAILIVS--HD 509
Cdd:PRK13635 183 VRQLKE-----QKGITVLSitHD 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
310-531 |
4.73e-10 |
|
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: 60.39 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 310 LELERASKSFNGGglnqnrkkmlfecknlsktidnKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:cd03295 1 IEFENVTKRYGGG----------------------KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 390 NRGEI------------KIGYFDQS-----RKSISDDKSLIelfcP--NGGDHIMVRGRNYHVYGYLKnfLFPKEFLDKP 450
Cdd:cd03295 59 FIDGEdireqdpvelrrKIGYVIQQiglfpHMTVEENIALV----PklLKWPKEKIRERADELLALVG--LDPAEFADRY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 451 VGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGA----ILIVSHDryfID---KITNKLWAY 523
Cdd:cd03295 133 PHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgktIVFVTHD---IDeafRLADRIAIM 209
|
....*...
gi 1196666485 524 ENGKIEQI 531
Cdd:cd03295 210 KNGEIVQV 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-235 |
4.97e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS----------IEMLAQSPK-FNDNLsvKD 85
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIlLNGQPIAdyseaalrqaISVVSQRVHlFSATL--RD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 86 ALNYELKEIFDarDEYEKVLAQIsnehdnpellhrqdELVKFIESKDGwnienkieriLDSF---GLREyenrlvnsLSG 162
Cdd:PRK11160 433 NLLLAAPNASD--EALIEVLQQV--------------GLEKLLEDDKG----------LNAWlgeGGRQ--------LSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL--ASNQTIVFISHDRYFIDRLaTRSVEIEDGALR 235
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAehAQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
334-531 |
5.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.90 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLS---KTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI----------NRGEI--KIGY 398
Cdd:PRK13650 6 EVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteeNVWDIrhKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 FDQSRK------SISDDkslIELFCPNGG-DHIMVRGRNYHVYgylkNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKE 471
Cdd:PRK13650 86 VFQNPDnqfvgaTVEDD---VAFGLENKGiPHEEMKERVNEAL----ELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 472 YDCLILDEPTNDLD-------IATI-NILEEYLLSfegaILIVSHDryfIDKIT--NKLWAYENGKIEQI 531
Cdd:PRK13650 159 PKIIILDEATSMLDpegrlelIKTIkGIRDDYQMT----VISITHD---LDEVAlsDRVLVMKNGQVEST 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-271 |
5.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 16 KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGeceidsgrvirqnsisieMLAqsPKFNDNLSVK-DALNYELKEI 94
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLING------------------LLL--PDDNPNSKITvDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 FDARDEYEKVLaqisnehDNPEllhrqDELVKFIESKD-GWNIENK----------IERILDSFGLREYENRLVNSLSGG 163
Cdd:PRK13640 80 WDIREKVGIVF-------QNPD-----NQFVGATVGDDvAFGLENRavprpemikiVRDVLADVGMLDYIDSEPANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDryfIDR--LATRSVEIEDGALrsF 237
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD---IDEanMADQVLVLDDGKL--L 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1196666485 238 DGGYANYLTKKEEILRS--------------LAKSHETLIKNLKSEEE 271
Cdd:PRK13640 223 AQGSPVEIFSKVEMLKEigldipfvyklknkLKEKGISVPQEINTEEK 270
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
334-531 |
5.67e-10 |
|
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: 60.04 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSIS---DDK 410
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISyvpQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLIelfcPNggdhiMVRGRNYhVYGyLKNFLFPK-----------------EFLDKPVGVLSGGEKNRLALALLFTKEYD 473
Cdd:cd03299 81 ALF----PH-----MTVYKNI-AYG-LKKRKVDKkeierkvleiaemlgidHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 474 CLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:cd03299 150 ILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-215 |
6.88e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.01 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKI-ILNETNFNVNEKERIAIIGKNGGGKSTLMK-------ILRGECEIDsGRVIrqNSIS----- 67
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRmvaglerITSGEIWIG-GRVV--NELEpadrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 68 IEMLAQSPKFNDNLSVKDALNYELKEIFDARDEyekvlaqisnehdnpellhrqdelvkfieskdgwnIENKIERILDSF 147
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAE-----------------------------------IEERVAEAARIL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 148 GLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHD 215
Cdd:PRK11650 123 ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
334-509 |
7.26e-10 |
|
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: 59.75 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNK----VLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeLEADSGvinrGEIKIgyFDQSRKSISDD 409
Cdd:COG4181 10 ELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDRPTS----GTVRL--AGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 410 KslielfcpnggdhiMVRGRNYHVyGY-------------LKNFLFP-------------KEFLDKpVGV---------- 453
Cdd:COG4181 83 A--------------RARLRARHV-GFvfqsfqllptltaLENVMLPlelagrrdararaRALLER-VGLghrldhypaq 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 454 LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT-INILEeyLLsFE-----GAILI-VSHD 509
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgEQIID--LL-FElnrerGTTLVlVTHD 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-214 |
7.86e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.05 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILR-------GECEIDSGRVIRQNSISIE----MLAQSPKFNdNLSV 83
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGVPLVQYDHHYLHrqvaLVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDALNYELKeifDARDEYEKVLAQISNEHDnpellhrqdelvkFIEskdgwNIENKIERILDSFGlreyenrlvNSLSGG 163
Cdd:TIGR00958 572 RENIAYGLT---DTPDEEIMAAAKAANAHD-------------FIM-----EFPNGYDTEVGEKG---------SQLSGG 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISH 214
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-251 |
8.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 5 DLIEVSKKF---GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIdsgrvirqnsisiemlaqspkFNDNL 81
Cdd:PRK14246 9 DVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEI---------------------YDSKI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKDALNYELKEIF--DA---RDEYEKVLAQisnehDNP-ELLHRQDELVKFIES---KDGWNIENKIERILDSFGL-RE 151
Cdd:PRK14246 68 KVDGKVLYFGKDIFqiDAiklRKEVGMVFQQ-----PNPfPHLSIYDNIAYPLKShgiKEKREIKKIVEECLRKVGLwKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 152 YENRL---VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHDRYFIDRLATRS 226
Cdd:PRK14246 143 VYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVADYV 222
|
250 260
....*....|....*....|....*
gi 1196666485 227 VEIEDGALRSFDGGYANYLTKKEEI 251
Cdd:PRK14246 223 AFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-215 |
8.33e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNDNLs 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vkdalnyelkeifdardeyekvlaqisnehdnPELLHRQDELVKFIESKDgwnIENKIERILDSFGLreyeNRLVNSLSG 162
Cdd:PRK09544 83 --------------------------------PLTVNRFLRLRPGTKKED---ILPALKRVQAGHLI----DAPMQKLSG 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 163 GEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHD 215
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVngqvALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-528 |
1.05e-09 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 59.75 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDN--KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-----------NRGEI--KIGY 398
Cdd:TIGR04520 2 EVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldtldeeNLWEIrkKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 399 FDQS------RKSISDDKSlielFCP--NGGDHIMVRGRnyhVYGYLKnFLFPKEFLDKPVGVLSGGEKNRLALALLFTK 470
Cdd:TIGR04520 82 VFQNpdnqfvGATVEDDVA----FGLenLGVPREEMRKR---VDEALK-LVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 471 EYDCLILDEPTNDLD-------IATINILEEyllsfEGAILIVS--HDryfIDKITN--KLWAYENGKI 528
Cdd:TIGR04520 154 RPDIIILDEATSMLDpkgrkevLETIRKLNK-----EEGITVISitHD---MEEAVLadRVIVMNKGKI 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-214 |
1.10e-09 |
|
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: 61.68 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIiLNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIEMLaqspkfnDNLSV 83
Cdd:TIGR01193 476 INDVSYSYGYGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE-ILLNGFSLKDI-------DRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDALNYELKE--IFDArDEYEKVLAQiSNEHDNPELLhrqDELVKFIESKDgwnienKIERILDSFGLREYENRlvNSLS 161
Cdd:TIGR01193 547 RQFINYLPQEpyIFSG-SILENLLLG-AKENVSQDEI---WAACEIAEIKD------DIENMPLGYQTELSEEG--SSIS 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVYMV-RFLEELLLASNQTIVFISH 214
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLNLQDKTIIFVAH 667
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-234 |
1.17e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKF-GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMLAQSPKFNDN 80
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 81 LsvkdALNYELKEIFDARDEYEKVLAQIsnehdnpellhrqdelvkFIESKDGWNIENKIERILDSFGLREYENRLVNSL 160
Cdd:PRK10908 81 I----GMIFQDHHLLMDRTVYDNVAIPL------------------IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 161 SGGEIRRVALGALILKKPDVLLLDEPTNHLDVYM----VRFLEELllasNQ---TIVFISHDRYFIDRLATRSVEIEDGA 233
Cdd:PRK10908 139 SGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALsegiLRLFEEF----NRvgvTVLMATHDIGLISRRSYRMLTLSDGH 214
|
.
gi 1196666485 234 L 234
Cdd:PRK10908 215 L 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
1.46e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKI-----ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-------------RQNS 65
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 66 ISIEMLAQSPKFNDNLSVKD-------ALNYELKEIFDARDEYEKVLAQISNEHDNPELLHRQDELVKFIeskdgwnien 138
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEirrrvgvVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELV---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 139 kierildsfGLRE-YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLaSNQTIVFIS 213
Cdd:PRK13651 153 ---------GLDEsYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNK-QGKTIILVT 222
|
250 260
....*....|....*....|.
gi 1196666485 214 HDRYFIDRLATRSVEIEDGAL 234
Cdd:PRK13651 223 HDLDNVLEWTKRTIFFKDGKI 243
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
10-186 |
1.57e-09 |
|
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: 58.82 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 10 SKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS-----------IEMLAQSPKF 77
Cdd:TIGR04406 8 IKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlIDGQDIThlpmherarlgIGYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 78 NDNLSVKDALnyelkeifdardeyeKVLAQISNEHDNPELLHRQDELVKfieskdgwniENKIERILDSFGLreyenrlv 157
Cdd:TIGR04406 88 FRKLTVEENI---------------MAVLEIRKDLDRAEREERLEALLE----------EFQISHLRDNKAM-------- 134
|
170 180
....*....|....*....|....*....
gi 1196666485 158 nSLSGGEIRRVALGALILKKPDVLLLDEP 186
Cdd:TIGR04406 135 -SLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-187 |
1.83e-09 |
|
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: 58.46 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-RQNSIS-------IEM-L 71
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITglpphriARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 72 AQSPK----FnDNLSVKDALnyelkeifdardeyekVLAQISnehdnpellhrqdelvkfieSKDGWNIENKIERILDSF 147
Cdd:COG0410 81 GYVPEgrriF-PSLTVEENL----------------LLGAYA--------------------RRDRAEVRADLERVYELF 123
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196666485 148 -GLREYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPT 187
Cdd:COG0410 124 pRLKERRRQRAGTLSGGEQQMLAIGrALMSR-PKLLLLDEPS 164
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
336-516 |
1.88e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLG-------------------ELEAD----------- 385
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedilELSPDeraragiflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 386 ------SGVINRGEIKIGYFDQSRKSISDDKSLIElfcpnggdhimvrgrnyhVYGYLKNFLFPKEFLDKPVGV-LSGGE 458
Cdd:COG0396 84 qypveiPGVSVSNFLRTALNARRGEELSAREFLKL------------------LKEKMKELGLDEDFLDRYVNEgFSGGE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 459 KNR---LALALLFTKeydCLILDEPTNDLDIATINILEEY---LLSFEGAILIVSHDRYFIDKI 516
Cdd:COG0396 146 KKRneiLQMLLLEPK---LAILDETDSGLDIDALRIVAEGvnkLRSPDRGILIITHYQRILDYI 206
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
357-531 |
2.16e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 58.66 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-RGEIKIGYFDQSRKSISDDKSLIELFCPNGGDHIMVRG------- 428
Cdd:TIGR02769 36 EGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRqiigepl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 429 RNY----------HVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDI----ATINILEE 494
Cdd:TIGR02769 116 RHLtsldeseqkaRIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRK 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196666485 495 YLLSFEGAILIVSHDRYFIDKITNKLWAYENGKI-EQI 531
Cdd:TIGR02769 196 LQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEEC 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-191 |
2.59e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.49 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 6 LIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEID---SGRV-IRQNSIS--------IEMLAQ 73
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVlLNGRRLTalpaeqrrIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 SPKFNDNLSVKDALNYELkeifdardeyekvlaqisnehdnPELLHRQDElvkfieskdgwniENKIERILDSFGLREYE 153
Cdd:COG4136 84 DDLLFPHLSVGENLAFAL-----------------------PPTIGRAQR-------------RARVEQALEEAGLAGFA 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:COG4136 128 DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-224 |
3.67e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.59 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSI-----SIEMLAQSPK-FN----DNLSV--K 84
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdIRTVTRaslrrNIAVVFQDAGlFNrsieDNIRVgrP 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DALNYELKEIfdardeyekvlAQISNEHDnpellhrqdelvkFIESKdgwniENKIERILDSFGlreyenrlvNSLSGGE 164
Cdd:PRK13657 435 DATDEEMRAA-----------AERAQAHD-------------FIERK-----PDGYDTVVGERG---------RQLSGGE 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 165 IRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT 224
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdeLMKGRTTFIIAH------RLST 532
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-213 |
3.73e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 16 KIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL----RGECEIDSGRVIRQNSISIEMLA-------QSPKFNDNLSVK 84
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAKEMRaisayvqQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DALNY--ELKeifdardeyekvlaqisnehdnpelLHRQdelvkfiESKDGwnienKIER---ILDSFGLREYENRL--- 156
Cdd:TIGR00955 118 EHLMFqaHLR-------------------------MPRR-------VTKKE-----KRERvdeVLQALGLRKCANTRigv 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 157 ---VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYM----VRFLEEllLASNQTIVFIS 213
Cdd:TIGR00955 161 pgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMaysvVQVLKG--LAQKGKTIICT 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
350-509 |
4.04e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.32 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYfdqSRKSISDDKSLIELFCPNGgDHIMVRGR 429
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY---SRKGLMKLRESVGMVFQDP-DNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 430 NYH--VYGYLkNFLFPKE-----------------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATIN 490
Cdd:PRK13636 100 VYQdvSFGAV-NLKLPEDevrkrvdnalkrtgiehLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180
....*....|....*....|...
gi 1196666485 491 ILEEYLLSFEG----AILIVSHD 509
Cdd:PRK13636 179 EIMKLLVEMQKelglTIIIATHD 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
334-528 |
4.27e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKIlLGELEadsgVINRGEIKIGyfDQSRKSISDDKSLI 413
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-INKLE----EITSGDLIVD--GLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELfcpNGGdhiMVRgRNYHVYGY---LKNFLF----------------PKEFLDKpVGV----------LSGGEKNRLAL 464
Cdd:PRK09493 76 RQ---EAG---MVF-QQFYLFPHltaLENVMFgplrvrgaskeeaekqARELLAK-VGLaerahhypseLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLDiatINILEEYL-----LSFEG-AILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALD---PELRHEVLkvmqdLAEEGmTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
4.63e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.58 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKF----GDKIILNETNFNVNEKERIAIIGKNGGGKS----TLMKILRGeceidSGRVirqnsisiemlA 72
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRI-----------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPKFNDnlsvKDALNYELKEIFDARDEYEKVLAQISNEHDNP-----ELLHRQDELVKFIESKDGWniENKIeRILDSF 147
Cdd:PRK09473 74 GSATFNG----REILNLPEKELNKLRAEQISMIFQDPMTSLNPymrvgEQLMEVLMLHKGMSKAEAF--EESV-RMLDAV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 148 GLREYENRLV---NSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHD 215
Cdd:PRK09473 147 KMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-239 |
5.03e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnsisiemlaqspkFNDNLSVKDALNYELKEIFDA--RDE 100
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----------------LLDGKPVTAEQPEDYRKLFSAvfTDF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 101 Y--EKVLaqisnehdNPELLHRQDELVkfieskDGWnienkIERILDSFGLREYENRLVN-SLSGGEIRRVALGALILKK 177
Cdd:PRK10522 407 HlfDQLL--------GPEGKPANPALV------EKW-----LERLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 178 PDVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFISH-DRYFIdrLATRSVEIEDGALRSFDG 239
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLpllqEMGKTIFAISHdDHYFI--HADRLLEMRNGQLSELTG 532
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
141-227 |
5.18e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 57.56 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 141 ERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFISHDr 216
Cdd:COG4525 116 EELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLdvwqRTGKGVFLITHS- 194
|
90
....*....|....
gi 1196666485 217 yfIDR---LATRSV 227
Cdd:COG4525 195 --VEEalfLATRLV 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
327-517 |
5.20e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 327 NRKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI--NRGEIKIGYFDQSRK 404
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 405 SISDDKSLIELFCPNGGDHIM----VRGRN---YHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALA--LLFTKEydCL 475
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIfpwqIRNQQpdpAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIrnLQFMPK--VL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1196666485 476 ILDEPTNDLDIAT---IN-ILEEYLLSFEGAILIVSHDRyfiDKIT 517
Cdd:PRK10247 160 LLDEITSALDESNkhnVNeIIHRYVREQNIAVLWVTHDK---DEIN 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-214 |
5.30e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.82 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRViRQNSISIEMLAQSPKFND-NLSVKDALNYELKEIFDa 97
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDIVVSSTSKQKEIKPvRKKVGVVFQFPESQLFE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 98 rdeyEKVLAQISNEHDNPELlhRQDELVKFIESKdgwnienkieriLDSFGL-REYENRLVNSLSGGEIRRVALGALILK 176
Cdd:PRK13643 100 ----ETVLKDVAFGPQNFGI--PKEKAEKIAAEK------------LEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196666485 177 KPDVLLLDEPTNHLD----VYMVRFLEElLLASNQTIVFISH 214
Cdd:PRK13643 162 EPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-232 |
5.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSisiemlaqspKFNDNLSvkdalnyELKEIFDAR 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDY----------AIPANLK-------KIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DEYEKVLaqisnehDNPELLHRQDELVKFIE------SKDGWNIENKIERILDSFGL-REYENRLVNSLSGGEIRRVALG 171
Cdd:PRK13645 90 KEIGLVF-------QFPEYQLFQETIEKDIAfgpvnlGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 172 ALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKgeedFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
349-528 |
5.52e-09 |
|
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: 59.37 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 349 SDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFD--QSRKSISD--------DKSLIE--LF 416
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINYlpqepyifSGSILEnlLL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 417 CPNGG---DHIMVRGRNYHVYGYLKNFlfPKEF---LDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT-I 489
Cdd:TIGR01193 571 GAKENvsqDEIWAACEIAEIKDDIENM--PLGYqteLSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITeK 648
|
170 180 190
....*....|....*....|....*....|....*....
gi 1196666485 490 NILEEYLLSFEGAILIVSHdRYFIDKITNKLWAYENGKI 528
Cdd:TIGR01193 649 KIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
345-485 |
6.69e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 345 KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVinrgeikiGYFDQSRKSISDDKSLIELFCPNGGDHI 424
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA--------GCVDVPDNQFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 425 MVRGRNyhVYGYLKNFLFPkefldKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD 485
Cdd:COG2401 115 AVELLN--AVGLSDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-186 |
7.35e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.58 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS-----------I 68
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfLDGEDIThlpmhkrarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 69 EMLAQSPKFNDNLSVKDalNYELkeifdardeyekVLaqisnehdnpellhrqdELVKFieSKDGwnIENKIERILDSFG 148
Cdd:COG1137 81 GYLPQEASIFRKLTVED--NILA------------VL-----------------ELRKL--SKKE--REERLEELLEEFG 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 1196666485 149 LREYENRLVNSLSGGEIRRVALG-ALILkKPDVLLLDEP 186
Cdd:COG1137 126 ITHLRKSKAYSLSGGERRRVEIArALAT-NPKFILLDEP 163
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-270 |
7.55e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.30 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKI-ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIrqnsisiemlaqspkfndnL 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-------------------V 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 82 SVKDALNY-ELKEIfdardeyEKVLAQIsneHDNPEllhrQDELVKFIESKDGWNIEN----------KIERILDSFGLR 150
Cdd:PRK13644 62 SGIDTGDFsKLQGI-------RKLVGIV---FQNPE----TQFVGRTVEEDLAFGPENlclppieirkRVDRALAEIGLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYM-VRFLEEL--LLASNQTIVFISHDryfIDRL--ATR 225
Cdd:PRK13644 128 KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHN---LEELhdADR 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1196666485 226 SVEIEDGALRsFDGGYANYLTKKEeiLRSLAKSHETLI---KNLKSEE 270
Cdd:PRK13644 205 IIVMDRGKIV-LEGEPENVLSDVS--LQTLGLTPPSLIelaENLKMHG 249
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-514 |
7.86e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 358 GERIGIVGRNGSGKSTMLKILLGELEADSG----------VIN--RGEIKIGYFDQSRksisdDKSLIELFCPNGGDHI- 424
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeILDefRGSELQNYFTKLL-----EGDVKVIVKPQYVDLIp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 425 -MVRGR---------NYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA---TINI 491
Cdd:cd03236 101 kAVKGKvgellkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAAR 180
|
170 180
....*....|....*....|...
gi 1196666485 492 LEEYLLSFEGAILIVSHDRYFID 514
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLAVLD 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-214 |
8.31e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 13 FGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-R-----------GECEIDsGRVIRQNSISIE-------MLAQ 73
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnRmndlipgarveGEILLD-GEDIYDPDVDVVelrrrvgMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 SPkfndN---LSVKDALNYELKeifdardeyekvlaqISNEHDNPELlhrqDELVkfieskdgwnienkiERILDSFGL- 149
Cdd:COG1117 100 KP----NpfpKSIYDNVAYGLR---------------LHGIKSKSEL----DEIV---------------EESLRKAALw 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 150 REYENRL---VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISH 214
Cdd:COG1117 142 DEVKDRLkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIleLKKDYTIVIVTH 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-204 |
9.53e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIEMlAQSPKFNDNLSVKDALNYELKEI 94
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ-IQIDGKTATR-GDRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 fdardeyekvlaqisnehdnpELLHrqdelvkFIESKDGWNIENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALI 174
Cdd:PRK13543 101 ---------------------ENLH-------FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170 180 190
....*....|....*....|....*....|
gi 1196666485 175 LKKPDVLLLDEPTNHLDVYMVRFLEELLLA 204
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
343-508 |
1.00e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRgeikigyfdqsrksisddkslielfcPNGGD 422
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------------------------PAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 423 HIMVRGRNYHVYGYLKNFL-FP-----------KEFLDKpVG----------------VLSGGEKNRLALA-LLFTKEyD 473
Cdd:COG4178 428 VLFLPQRPYLPLGTLREALlYPataeafsdaelREALEA-VGlghlaerldeeadwdqVLSLGEQQRLAFArLLLHKP-D 505
|
170 180 190
....*....|....*....|....*....|....*..
gi 1196666485 474 CLILDEPTNDLDIATINILEEYLLS-FEGAILI-VSH 508
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREeLPGTTVIsVGH 542
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
312-488 |
1.01e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.79 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 312 LERASKSFNGGGLNQNRKKMLFEckNLSKTIdNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINR 391
Cdd:cd03291 21 LEKAKQENNDRKHSSDDNNLFFS--NLCLVG-APVL-KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 392 geikigyfdQSRKSISDDKSLIelfCPNGGDHIMVRGRNYHVYGYLKNF----------LFPKEflDKPV----GV-LSG 456
Cdd:cd03291 97 ---------SGRISFSSQFSWI---MPGTIKENIIFGVSYDEYRYKSVVkacqleeditKFPEK--DNTVlgegGItLSG 162
|
170 180 190
....*....|....*....|....*....|..
gi 1196666485 457 GEKNRLALALLFTKEYDCLILDEPTNDLDIAT 488
Cdd:cd03291 163 GQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-232 |
1.12e-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: 55.55 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 10 SKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIemLAQSPkFNDNLSVKDalNY 89
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAY--VSQEP-WIQNGTIRE--NI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 90 ELKEIFDArDEYEKVLA--------QISNEHDNPELlhrqdelvkfieskdGwniENKIerildsfglreyenrlvnSLS 161
Cdd:cd03250 87 LFGKPFDE-ERYEKVIKacalepdlEILPDGDLTEI---------------G---EKGI------------------NLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFL-EELL---LASNQTIVFISHDRYFIDRlATRSVEIEDG 232
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-232 |
1.37e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.01 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDK----IILNETNFNVNEKERIAIIGKNGGGKSTLmkiLRgeC-----EIDSGRVIrqnsIS-IEMLAQ 73
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTL---IR--CinlleRPTSGSVL----VDgVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 74 SPKfndnlsvkdalnyELKE-------IFdardeyekvlaqisnEHDNpeLLHRQD---------ELVKFieSKDgwNIE 137
Cdd:COG1135 73 SER-------------ELRAarrkigmIF---------------QHFN--LLSSRTvaenvalplEIAGV--PKA--EIR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 138 NKIERILDSFGLREYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLD------VymvrfLeELLLASNQ--- 207
Cdd:COG1135 119 KRVAELLELVGLSDKADAYPSQLSGGQKQRVGIArALANN-PKVLLCDEATSALDpettrsI-----L-DLLKDINRelg 191
|
250 260
....*....|....*....|....*.
gi 1196666485 208 -TIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:COG1135 192 lTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
334-508 |
1.43e-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: 55.36 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI--------NRGEIKIGYFDQSRKS 405
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkpldIAARNRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 ISDDK---SLIELFCPNGGDHIMVRGRnyhVYGYLKNF-LFPKEflDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPT 481
Cdd:cd03269 82 YPKMKvidQLVYLAQLKGLKKEEARRR---IDEWLERLeLSEYA--NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190
....*....|....*....|....*....|
gi 1196666485 482 NDLDIATINILEEYLLSFEGA---ILIVSH 508
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-229 |
1.53e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.66 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 24 FNVNEKERIAIIGKNGGGKSTLMK-ILRGEcEIDSGRVIrqnsisiemlaqspkFN-DNLSVKDALnyELKE-------I 94
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRlLLRLE-EPTSGEIL---------------FDgQDITGLSGR--ELRPlrrrmqmV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 FdaRDEYE-----KVLAQISNEhdnPELLHRqdelvkfIESKDGwnIENKIERILDSFGLR-EYENRLVNSLSGGEIRRV 168
Cdd:COG4608 101 F--QDPYAslnprMTVGDIIAE---PLRIHG-------LASKAE--RRERVAELLELVGLRpEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 169 ALG-ALILKkPDVLLLDEPTNHLDVYM----VRFLEELLLASNQTIVFISHD----RYFIDRLAT----RSVEI 229
Cdd:COG4608 167 GIArALALN-PKLIVCDEPVSALDVSIqaqvLNLLEDLQDELGLTYLFISHDlsvvRHISDRVAVmylgKIVEI 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-235 |
1.63e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 26 VNEKERIAIIGKNGGGKSTLMKILRGECEIDSG-RVIRQNSI--SIEMLAQS----PKFndnlsvkDALNyelkEIFDAR 98
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGKSIltNISDVHQNmgycPQF-------DAID----DLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DE---YEKVLAQISNEhdnpellhrqdelvkfIESKDGWNIEnkierildSFGLREYENRLVNSLSGGEIRRVALGALIL 175
Cdd:TIGR01257 2031 EHlylYARLRGVPAEE----------------IEKVANWSIQ--------SLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 176 KKPDVLLLDEPTNHLDVYMVRFLEELLLA---SNQTIVFISHDRYFIDRLATRSVEIEDGALR 235
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSiirEGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
357-524 |
1.78e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.50 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQsrksisddkslielfcpnggdhimvrgrnyhvygY 436
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ----------------------------------Y 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 437 LKnflfpkefldkpvgvLSGGEKNRLALALLFTKEYDCLILDEPTNDLDI----ATINILEEYLLSFEGAILIVSHDRYF 512
Cdd:cd03222 70 ID---------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVVEHDLAV 134
|
170
....*....|..
gi 1196666485 513 IDKITNKLWAYE 524
Cdd:cd03222 135 LDYLSDRIHVFE 146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
350-507 |
1.86e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN------RGEIK---IGYFDQSRKSISDDKSLIElfcpng 420
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptRQALQknlVAYVPQSEEVDWSFPVLVE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 421 gDHIMVrGRnyhvYGYLKNFLFPK-----------------EFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTND 483
Cdd:PRK15056 99 -DVVMM-GR----YGHMGWLRRAKkrdrqivtaalarvdmvEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180
....*....|....*....|....*...
gi 1196666485 484 LDIAT----INILEEylLSFEGAILIVS 507
Cdd:PRK15056 173 VDVKTeariISLLRE--LRDEGKTMLVS 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-214 |
1.93e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNS------------ISIEMLAQSPKFNDNlS 82
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYELKEIFDAR---DEYEK---------------------VLAQISNEHDNPELLHRQDELvKFIESKDGWNIEN 138
Cdd:PTZ00265 476 IKNNIKYSLYSLKDLEalsNYYNEdgndsqenknkrnscrakcagDLNDMSNTTDSNELIEMRKNY-QTIKDSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 139 KIerILDSF--GLREYENRLVNS----LSGGEIRRVALGALILKKPDVLLLDEPTNHLD---VYMV-RFLEELLLASNQT 208
Cdd:PTZ00265 555 KV--LIHDFvsALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVqKTINNLKGNENRI 632
|
....*.
gi 1196666485 209 IVFISH 214
Cdd:PTZ00265 633 TIIIAH 638
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-531 |
2.08e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKS----TLMKILR---GECEIDSGRVIRQNSISIEMLAQSPKFNDNLSVKDaLNYELKEIF 95
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGAD-MAMIFQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 96 DARDEYEKVLAQISNEHDNPELLHRQDELVkfiESKdgwnienkieRILDSFGLREYE---NRLVNSLSGGEIRRVALGA 172
Cdd:PRK10261 115 TSLNPVFTVGEQIAESIRLHQGASREEAMV---EAK----------RMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 173 LILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQT----IVFISHDRYFIDRLATRSVEIEDGalRSFDGGYAnyltkk 248
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmsmgVIFITHDMGVVAEIADRVLVMYQG--EAVETGSV------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 249 EEILRSLAKSH-ETLIKNLK-----SEEEWLRR----GVKARLKRNEGRKQR-------ILAMREEAKKNP---GLIRRV 308
Cdd:PRK10261 254 EQIFHAPQHPYtRALLAAVPqlgamKGLDYPRRfpliSLEHPAKQEPPIEQDtvvdgepILQVRNLVTRFPlrsGLLNRV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 309 KLELERASK-SFNggglnqnrkkmlfecknlsktidnkvlfsdfnarVLQGERIGIVGRNGSGKSTMLKILLGELEADSG 387
Cdd:PRK10261 334 TREVHAVEKvSFD----------------------------------LWPGETLSLVGESGSGKSTTGRALLRLVESQGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 388 VINRGEIKIGYFDQSR-KSISDDKSLI-----ELFCPNG--GDHIMVRGRnyhVYGYLKNFLFPKE--FLDKPVGVL--- 454
Cdd:PRK10261 380 EIIFNGQRIDTLSPGKlQALRRDIQFIfqdpyASLDPRQtvGDSIMEPLR---VHGLLPGKAAAARvaWLLERVGLLpeh 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 455 --------SGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT----INILEEYLLSFEGAILIVSHDRYFIDKITNKLWA 522
Cdd:PRK10261 457 awryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIrgqiINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
....*....
gi 1196666485 523 YENGKIEQI 531
Cdd:PRK10261 537 MYLGQIVEI 545
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-229 |
2.26e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.56 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 33 AIIGKNGGGKSTLMKILrgeceidsGRvirqnsisiemlAQSPKFNDNLsvkdaLNYELKEIFDARDEYEKVlAQIsneh 112
Cdd:PRK10575 41 GLIGHNGSGKSTLLKML--------GR------------HQPPSEGEIL-----LDAQPLESWSSKAFARKV-AYL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 113 dnPELLHRQD-----ELVKFIE-------SKDGWNIENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDV 180
Cdd:PRK10575 91 --PQQLPAAEgmtvrELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 181 LLLDEPTNHLDV-YMVRFLEELLLASNQ---TIVFISHD-----RYFIDRLATRSVEI 229
Cdd:PRK10575 169 LLLDEPTSALDIaHQVDVLALVHRLSQErglTVIAVLHDinmaaRYCDYLVALRGGEM 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-215 |
2.27e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.38 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 6 LIEVSK---KFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIEMLAqSPKFNDNLS 82
Cdd:PRK11300 5 LLSVSGlmmRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQHIEGLP-GHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYELkeiFDARDEYEKVL-AQisNEHDNPELLH--------RQDElVKFIESKDGWnienkieriLDSFGLREYE 153
Cdd:PRK11300 83 VRTFQHVRL---FREMTVIENLLvAQ--HQQLKTGLFSgllktpafRRAE-SEALDRAATW---------LERVGLLEHA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA----SNQTIVFISHD 215
Cdd:PRK11300 148 NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHD 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
327-528 |
2.31e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 327 NRKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGEleaDSGVINRGEIKigYFDQSRKSI 406
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH---PAYKILEGDIL--FKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 S-DDKSLIELFCP----------NGGDHIMVRGRNYHVYgYLKNFLFPKEFLD------KPVGV------------LSGG 457
Cdd:CHL00131 77 EpEERAHLGIFLAfqypieipgvSNADFLRLAYNSKRKF-QGLPELDPLEFLEiineklKLVGMdpsflsrnvnegFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 458 EKNR---LALALLFTKeydCLILDEPTNDLDIATINILEEYLLSF---EGAILIVSHDRYFIDKIT-NKLWAYENGKI 528
Cdd:CHL00131 156 EKKRneiLQMALLDSE---LAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-220 |
2.37e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.46 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG--ECEIDSGRVIRQNsisiemlaqspkfndnlsvKDALNYEL 91
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG-------------------EDITDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 92 keifdardeYEKVLAQISNEHDNPEllhrqdelvkfieskdgwnienKIERILDSFGLREyenrlVN-SLSGGEIRRVAL 170
Cdd:cd03217 72 ---------EERARLGIFLAFQYPP----------------------EIPGVKNADFLRY-----VNeGFSGGEKKRNEI 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 171 GALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISHDRYFID 220
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLD 168
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
347-507 |
2.48e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 54.97 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 347 LFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEAD---SGVI--NRGEIKIgyfDQSRKSIS----DDKSLielfc 417
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfNGQPRKP---DQFQKCVAyvrqDDILL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 418 pnggDHIMVRgrnYHVYgYLKNFLFPKEFLDK-----------------PVG-----VLSGGEKNRLALALLFTKEYDCL 475
Cdd:cd03234 94 ----PGLTVR---ETLT-YTAILRLPRKSSDAirkkrvedvllrdlaltRIGgnlvkGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....
gi 1196666485 476 ILDEPTNDLDIATINILEEYL--LSFEGAILIVS 507
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLsqLARRNRIVILT 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-528 |
2.62e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDSGRVIRQN-----SISIEM 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIagivppdSGTLEIGGNPCARLTpakahQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 71 LAQSPKFNDNLSVKDALNYELKEIFDARDEYEKVLAQIsNEHDNPELlhrqdelvkfieskdgwnienkierildSFGLR 150
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAAL-GCQLDLDS----------------------------SAGSL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENR-LVNSLSGgeirrvalgalILKKPDVLLLDEPTNHLDVYMV-RFLEEL--LLASNQTIVFISHDRYFIDRLATRS 226
Cdd:PRK15439 142 EVADRqIVEILRG-----------LMRDSRILILDEPTASLTPAETeRLFSRIreLLAQGVGIVFISHKLPEIRQLADRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 227 VEIEDGALrSFDGGYANYltkkeeilrslakSHETLIKnlkseeewlrrgvkarlkrnegrkqrilAMREEAkKNPGLIR 306
Cdd:PRK15439 211 SVMRDGTI-ALSGKTADL-------------STDDIIQ----------------------------AITPAA-REKSLSA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 307 RVKLELErasksfngggLNQNRKkmlfecknlSKTIDNKVL---------FSDFNARVLQGERIGIVGRNGSGKSTMLKI 377
Cdd:PRK15439 248 SQKLWLE----------LPGNRR---------QQAAGAPVLtvedltgegFRNISLEVRAGEILGLAGVVGAGRTELAET 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 378 LLGeLEADSGvinrGEIKIGYFDQSRKSISD--DKSLIELfcPnggDHIMVRGRN------YHVYGYLKN----FLFPK- 444
Cdd:PRK15439 309 LYG-LRPARG----GRIMLNGKEINALSTAQrlARGLVYL--P---EDRQSSGLYldaplaWNVCALTHNrrgfWIKPAr 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 445 ----------------EFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEG---AILI 505
Cdd:PRK15439 379 enavleryrralnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqnvAVLF 458
|
570 580
....*....|....*....|...
gi 1196666485 506 VSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK15439 459 ISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-236 |
2.93e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKF--GDKII--LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSG--RVIRQNSISIEmlaqsp 75
Cdd:PRK10535 3 ALLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVATLD------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 76 kfndnlsvKDALNYELKEIFDARDEYEKVLAQISNEHdNPEL------LHRQDELVKFIEskdgwnienkierILDSFGL 149
Cdd:PRK10535 77 --------ADALAQLRREHFGFIFQRYHLLSHLTAAQ-NVEVpavyagLERKQRLLRAQE-------------LLQRLGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 150 REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYM---VRFLEELLLASNQTIVFISHDRYfIDRLATRS 226
Cdd:PRK10535 135 EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERV 213
|
250
....*....|
gi 1196666485 227 VEIEDGALRS 236
Cdd:PRK10535 214 IEIRDGEIVR 223
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
336-517 |
3.37e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 54.96 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGEleaDSGVINRGEIKIGYFDQSRKSIsDDKSLIEL 415
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH---PSYEVTSGTILFKGQDLLELEP-DERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 416 F--------------------------CPNGGDHIMVRGRNYHVYGYLKNFLFPKEFLDKPVGV-LSGGEKNRLALALLF 468
Cdd:TIGR01978 80 FlafqypeeipgvsnleflrsalnarrSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 469 TKEYDCLILDEPTNDLDIATINILEEYLLSF---EGAILIVSHDRYFIDKIT 517
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIK 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
331-508 |
3.43e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLfECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-RGEiKIGyfdQSRKS---- 405
Cdd:PRK13538 1 ML-EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGE-PIR---RQRDEyhqd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 ---------ISDDKSLIE-------LFCPNGGDHIMV-------RGrnyhvygylknflfpkeFLDKPVGVLSGGEKNRL 462
Cdd:PRK13538 76 llylghqpgIKTELTALEnlrfyqrLHGPGDDEALWEalaqvglAG-----------------FEDVPVRQLSAGQQRRV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1196666485 463 ALALLFTKEYDCLILDEPTNDLDIATINILEEYL---LSFEGAILIVSH 508
Cdd:PRK13538 139 ALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhAEQGGMVILTTH 187
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-242 |
3.78e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV------IRQNSIS-----IEMLAQSPK-FNDnlS 82
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghdLRDYTLAslrnqVALVSQNVHlFND--T 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALNYELKEIFdARDEYEKVlaqisnehdnPELLHRQDelvkFIEskdgwnienKIERILDS-FGlreyENRLvnSLS 161
Cdd:PRK11176 433 IANNIAYARTEQY-SREQIEEA----------ARMAYAMD----FIN---------KMDNGLDTvIG----ENGV--LLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT--RSVEI---EDG-- 232
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH------RLSTieKADEIlvvEDGei 556
|
250
....*....|....*..
gi 1196666485 233 -------ALRSFDGGYA 242
Cdd:PRK11176 557 vergthaELLAQNGVYA 573
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
345-529 |
3.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.05 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 345 KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgEIKIGYFDQSRKSI--SDDKSLIEL------- 415
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSG-----KIIIDGVDITDKKVklSDIRKKVGLvfqypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 416 ------------FCP-NGG---DHIMVRgrnyhVYGYLKNFLFPKE-FLDKPVGVLSGGEKNRLALALLFTKEYDCLILD 478
Cdd:PRK13637 95 qlfeetiekdiaFGPiNLGlseEEIENR-----VKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 479 EPTNDLD-------IATI-NILEEYLLSfegaILIVSHDRYFIDKITNKLWAYENGKIE 529
Cdd:PRK13637 170 EPTAGLDpkgrdeiLNKIkELHKEYNMT----IILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
346-481 |
3.95e-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: 54.60 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 346 VLFsDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN----------------RGeikIGYFDQSRKSISDd 409
Cdd:COG0410 18 VLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglpphriarLG---IGYVPEGRRIFPS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 410 ksL-----IELFCPNGGDHIMVRGRNYHVYGylknfLFP--KEFLDKPVGVLSGGEKNRLAL--ALLftKEYDCLILDEP 480
Cdd:COG0410 93 --LtveenLLLGAYARRDRAEVRADLERVYE-----LFPrlKERRRQRAGTLSGGEQQMLAIgrALM--SRPKLLLLDEP 163
|
.
gi 1196666485 481 T 481
Cdd:COG0410 164 S 164
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-214 |
4.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILrgeceidsGRVIRQNSISiEMLAQSPKFNDNLSV 83
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF--------NRLLELNEEA-RVEGEVRLFGRNIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDALNYELKEIFDARDEYEKVLAQISnEHDNPELLHRQDELVKfieSKDgwNIENKIERILDSFGL-REYENRLVN---S 159
Cdd:PRK14267 76 PDVDPIEVRREVGMVFQYPNPFPHLT-IYDNVAIGVKLNGLVK---SKK--ELDERVEWALKKAALwDEVKDRLNDypsN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISH 214
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfeLKKEYTIVLVTH 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
316-510 |
4.28e-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: 56.84 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 316 SKSFNGGGLNQNRKKMLFECKNLSK-----------------TIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKIL 378
Cdd:TIGR01271 1186 PRPSGGGGKYQLSTVLVIENPHAQKcwpsggqmdvqgltakyTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 379 L------GELEADS---------------GVINR------GEIKIG------YFDQSRKSISDD---KSLIELFcPNGGD 422
Cdd:TIGR01271 1266 LrllsteGEIQIDGvswnsvtlqtwrkafGVIPQkvfifsGTFRKNldpyeqWSDEEIWKVAEEvglKSVIEQF-PDKLD 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 423 HIMVRGrnyhvyGYlknflfpkefldkpvgVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL-LSFEG 501
Cdd:TIGR01271 1345 FVLVDG------GY----------------VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSN 1402
|
....*....
gi 1196666485 502 AILIVSHDR 510
Cdd:TIGR01271 1403 CTVILSEHR 1411
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-234 |
4.29e-08 |
|
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: 53.37 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRqnsisiemlaqspkfnDNLSVKDAlnyelkeifdA 97
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL----------------DGADISQW----------D 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 98 RDEYEK---VLAQisnehdnpellhrQDELVkfieskDGwnienkieRILDsfglreyenrlvNSLSGGEIRRVALGALI 174
Cdd:cd03246 71 PNELGDhvgYLPQ-------------DDELF------SG--------SIAE------------NILSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 175 LKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHDRYFIdRLATRSVEIEDGAL 234
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAalkAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
349-509 |
4.91e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 349 SDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKI------GYFDQSRKSIS-----DDKSLIE--- 414
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRPVRKRIGmvfqfPESQLFEdtv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 415 ----LFCPNGGDHIMVRGRNYhVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD----I 486
Cdd:PRK13646 104 ereiIFGPKNFKMNLDEVKNY-AHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskR 182
|
170 180
....*....|....*....|...
gi 1196666485 487 ATINILEEYLLSFEGAILIVSHD 509
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHD 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-234 |
5.33e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKF--GDKII--LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------------RQNS 65
Cdd:PRK11153 2 IELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdltalsekelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 66 ISIEMLAQspKFN--------DNLsvkdALNYELkeifdardeyekvlaqisnehdnpellhrqdelvkfieskDGWN-- 135
Cdd:PRK11153 82 RQIGMIFQ--HFNllssrtvfDNV----ALPLEL----------------------------------------AGTPka 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 136 -IENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ----TIV 210
Cdd:PRK11153 116 eIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIV 195
|
250 260
....*....|....*....|....
gi 1196666485 211 FISHDRYFIDRLATRSVEIEDGAL 234
Cdd:PRK11153 196 LITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-191 |
5.88e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.13 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGR-VIRQNSISIEMLAQspkfnd 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiIIDDEDISLLPLHA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 nlSVKDALNYELKE--IFDARDEYEKVLAQISNEHDnpelLHRQDElvkfieskdgwniENKIERILDSFGLREYENRLV 157
Cdd:PRK10895 75 --RARRGIGYLPQEasIFRRLSVYDNLMAVLQIRDD----LSAEQR-------------EDRANELMEEFHIEHLRDSMG 135
|
170 180 190
....*....|....*....|....*....|....
gi 1196666485 158 NSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:PRK10895 136 QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-518 |
6.43e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKIL--LGELEADSGVinrgEIKIGYFDQS----------- 402
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRV----EGRVEFFNQNiyerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 RKSISDDKSLIELFCPNGGDHIM--VRGRNYH----VYGYLKNFLFPKEFLD-------KPVGVLSGGEKNRLALALLFT 469
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAygVKIVGWRpkleIDDIVESALKDADLWDeikhkihKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 470 KEYDCLILDEPTNDLD-IATINI---LEEYLLSFEGAILIVSHDRYFIDKITN 518
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDpIASMKVeslIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
336-508 |
6.63e-08 |
|
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: 53.82 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-------------NRGEIKIGYFDQS 402
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmhERARLGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 ----RK-SISDD-KSLIELFCPNGGDHIMVRgrnyhvygyLKNFLfpKEF-----LDKPVGVLSGGEKNRLALALLFTKE 471
Cdd:TIGR04406 85 asifRKlTVEENiMAVLEIRKDLDRAEREER---------LEALL--EEFqishlRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1196666485 472 YDCLILDEPTNDLD-IATINI--LEEYLLSFEGAILIVSH 508
Cdd:TIGR04406 154 PKFILLDEPFAGVDpIAVGDIkkIIKHLKERGIGVLITDH 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
332-511 |
6.73e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-------RGEIK--IGYFDQS 402
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgktatRGDRSrfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 RKSISDDKSLIELFCPNGgdhimVRGRN-YHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPT 481
Cdd:PRK13543 91 PGLKADLSTLENLHFLCG-----LHGRRaKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190
....*....|....*....|....*....|...
gi 1196666485 482 NDLDIATINILEEYL---LSFEGAILIVSHDRY 511
Cdd:PRK13543 166 ANLDLEGITLVNRMIsahLRGGGAALVTTHGAY 198
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
336-487 |
6.82e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.93 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgEIKIGYFDQSRKSiSDD--KSLI 413
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSG-----EVLVDGLDVATTP-SRElaKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELFCPNggdHIMVR---------GRNYHVYGYLK-----------NFL----FPKEFLDKpvgvLSGGEKNRLALALLFT 469
Cdd:COG4604 79 ILRQEN---HINSRltvrelvafGRFPYSKGRLTaedreiideaiAYLdledLADRYLDE----LSGGQRQRAFIAMVLA 151
|
170
....*....|....*...
gi 1196666485 470 KEYDCLILDEPTNDLDIA 487
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMK 169
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
7.20e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 2 ALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL------------------RGECEI--DSGRVI 61
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlfgrrRGSGETiwDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 62 RQNSISIEMlaqspKFNDNLSVKDALnyeLKEIFDARDEYEkvlaQISNehdnpellhRQDELVkfieskDGWnienkie 141
Cdd:PRK10938 339 GYVSSSLHL-----DYRVSTSVRNVI---LSGFFDSIGIYQ----AVSD---------RQQKLA------QQW------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 142 riLDSFGLreyENRLVN----SLSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFIS 213
Cdd:PRK10938 385 --LDILGI---DKRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrQLVRRFVDVLISEGETQLLFVS 459
|
.
gi 1196666485 214 H 214
Cdd:PRK10938 460 H 460
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-529 |
8.17e-08 |
|
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: 53.35 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNK----VLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeLEADSgvinRGEIKIGYFDQSRKSisdD 409
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERPT----SGSVLVDGTDLTLLS---G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 410 KSLielfcPNGGDHI-MVRgRNYH------VYGylkNFLFPKEFLDKP--------------VGV----------LSGGE 458
Cdd:cd03258 75 KEL-----RKARRRIgMIF-QHFNllssrtVFE---NVALPLEIAGVPkaeieervlellelVGLedkadaypaqLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 459 KNRLALALLFTKEYDCLILDEPTNDLDIATI-NILEeyLLS-----FEGAILIVSHDRYFIDKITNKLWAYENGKIE 529
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTqSILA--LLRdinreLGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
337-508 |
8.54e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 53.18 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 337 NLSKTIDNkVLFsdfnaRVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-----NRGEIKIGYFDQSRKSISDDKS 411
Cdd:cd03369 19 DLPPVLKN-VSF-----KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeidgiDISTIPLEDLRSSLTIIPQDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 412 LIElfcpnggdhimvrgrnyhvyGYLKNFLFP-KEFLDKPV---------GV-LSGGEKNRLALALLFTKEYDCLILDEP 480
Cdd:cd03369 93 LFS--------------------GTIRSNLDPfDEYSDEEIygalrvsegGLnLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190
....*....|....*....|....*....|
gi 1196666485 481 TNDLDIATINILEEYLL-SFEGA-ILIVSH 508
Cdd:cd03369 153 TASIDYATDALIQKTIReEFTNStILTIAH 182
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-509 |
8.73e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.32 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIGYFDQSR------KSISD----------DKSLI 413
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS-----GEVRVLGYVPFKrrkefaRRIGVvfgqrsqlwwDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELFCPNGgdhimvrgrnyHVYG-----YLKNF------LFPKEFLDKPVGVLSGGEKNR--LALALLFTKEydCLILDEP 480
Cdd:COG4586 115 DSFRLLK-----------AIYRipdaeYKKRLdelvelLDLGELLDTPVRQLSLGQRMRceLAAALLHRPK--ILFLDEP 181
|
170 180 190
....*....|....*....|....*....|...
gi 1196666485 481 TNDLDIAT----INILEEYLLSFEGAILIVSHD 509
Cdd:COG4586 182 TIGLDVVSkeaiREFLKEYNRERGTTILLTSHD 214
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
363-509 |
9.09e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 363 IVGRNGSGKSTMLK-ILLGELEADSGVINRGEIKIGYFdqsrksisddKSLIELFcpnggdhimvrgrnyhvygylknFL 441
Cdd:cd03227 26 ITGPNGSGKSTILDaIGLALGGAQSATRRRSGVKAGCI----------VAAVSAE-----------------------LI 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 442 FpkeFLDKpvgvLSGGEKNRLALALLF----TKEYDCLILDEPTNDLDIATINILEEYLLSF--EGAILIV-SHD 509
Cdd:cd03227 73 F---TRLQ----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQVIViTHL 140
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-389 |
9.88e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKS----TLMKILRGECEIDSGRV-----------------IRQNSISieMLA 72
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlfdgqdllglserelrrIRGNRIA--MIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 73 QSPkfndnLSvkdALNyELKEIfdardeyEKvlaQISnehdnpE--LLHRqdelvkfieSKDGWNIENKIERILDSFGLR 150
Cdd:COG4172 99 QEP-----MT---SLN-PLHTI-------GK---QIA------EvlRLHR---------GLSGAAARARALELLERVGIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 151 EYENRLvNS----LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVyMVR--FLEelLLASNQT-----IVFISHD---- 215
Cdd:COG4172 145 DPERRL-DAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQaqILD--LLKDLQRelgmaLLLITHDlgvv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 216 RYFIDRLAT-RSVEI-EDGAlrsfdggyanyltkKEEILRslAKSHE-TliknlkseeewlRRGVKARLKRnegrkqril 292
Cdd:COG4172 221 RRFADRVAVmRQGEIvEQGP--------------TAELFA--APQHPyT------------RKLLAAEPRG--------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 293 AMREEAKKNPGLirrvkLELERASKSFnggglnqNRKKMLFecknlSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKS 372
Cdd:COG4172 264 DPRPVPPDAPPL-----LEARDLKVWF-------PIKRGLF-----RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKS 326
|
410
....*....|....*..
gi 1196666485 373 TMLKILLGeLEADSGVI 389
Cdd:COG4172 327 TLGLALLR-LIPSEGEI 342
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-234 |
9.97e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 5 DLIEVSKKFGdKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI---RQNSISIEMLAQS----PKF 77
Cdd:TIGR01257 933 NLVKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLvggKDIETNLDAVRQSlgmcPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 78 N---DNLSVKDALNYelkeifdardeyekvLAQISNEhdnpellhrqdelvkfieSKDGWNIEnkIERILDSFGLREYEN 154
Cdd:TIGR01257 1012 NilfHHLTVAEHILF---------------YAQLKGR------------------SWEEAQLE--MEAMLEDTGLHHKRN 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 155 RLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA--SNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKyrSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
..
gi 1196666485 233 AL 234
Cdd:TIGR01257 1137 RL 1138
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-215 |
1.10e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 23 NFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI--------------RQNSISIEMLAQSP--KFNDNLSVKDA 86
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmkddewRAVRSDIQMIFQDPlaSLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 87 LNYELKEIFdardeyekvlaqisnehdnPELlHRQDelvkfieskdgwnIENKIERILDSFGLREYE-NRLVNSLSGGEI 165
Cdd:PRK15079 121 IAEPLRTYH-------------------PKL-SRQE-------------VKDRVKAMMLKVGLLPNLiNRYPHEFSGGQC 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 166 RRVALG-ALILKkPDVLLLDEPTNHLDVYM----VRFLEELLLASNQTIVFISHD 215
Cdd:PRK15079 168 QRIGIArALILE-PKLIICDEPVSALDVSIqaqvVNLLQQLQREMGLSLIFIAHD 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
332-528 |
1.11e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTID-NKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG-VINRGE-IKIGYFDQSRKSI-- 406
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsVLIRGEpITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 ----SDDksliELFCPN------------GGDHIMVRGRnyhVYGYLKnFLFPKEFLDKPVGVLSGGEKNRLALALLFTK 470
Cdd:PRK13652 83 vfqnPDD----QIFSPTveqdiafgpinlGLDEETVAHR---VSSALH-MLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 471 EYDCLILDEPTNDLD-------IATINIL-EEYLLSfegaILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK13652 155 EPQVLVLDEPTAGLDpqgvkelIDFLNDLpETYGMT----VIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-528 |
1.17e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.51 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEA-DSGVINRGeiKIGYFDQSRKSISDDK 410
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDG--KVLYFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLIELFC----PNGGDHIMV----------------RGRNYHVYGYLKNFLFPKEFLDK---PVGVLSGGEKNRLALALL 467
Cdd:PRK14246 88 LRKEVGMvfqqPNPFPHLSIydniayplkshgikekREIKKIVEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 468 FTKEYDCLILDEPTNDLDIATINILEEYL--LSFEGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-215 |
1.18e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.56 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnSISIEMLAQSPKFNdnlsvkdaLNYELKEIFDAR 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV----KIDGELLTAENVWN--------LRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DEyEKVLAQISNEhdnpellhrqdelVKFIESKDGWNIENKIERI---LDSFGLREYENRLVNSLSGGEIRRVALGALIL 175
Cdd:PRK13642 91 DN-QFVGATVEDD-------------VAFGMENQGIPREEMIKRVdeaLLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1196666485 176 KKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHD 215
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-234 |
1.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.63 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 33 AIIGKNGGGKSTLMKILRGECEIDSGrvirqnSISIEMLAQSPKFNDnlsvkdalnyelKEIFDARDEYEKVLaQIsneh 112
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTG------TVTVDDITITHKTKD------------KYIRPVRKRIGMVF-QF---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 113 dnPELLHRQDELVKFIE--SKD-GWNIE---NKIERILDSFGL-REYENRLVNSLSGGEIRRVALGALILKKPDVLLLDE 185
Cdd:PRK13646 94 --PESQLFEDTVEREIIfgPKNfKMNLDevkNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 186 PTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGAL 234
Cdd:PRK13646 172 PTAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-214 |
1.20e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.85 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILrgeceidSGRVIRQNSISIEmlaqspkfndnlsvkdalNYELKEI 94
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-------LGFLPYQGSLKIN------------------GIELREL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 fdARDEYEKVLAQISNehdNPELLH---RQDELVKFIESKDGwnienKIERILDSFGLREYENRLVN-----------SL 160
Cdd:PRK11174 417 --DPESWRKHLSWVGQ---NPQLPHgtlRDNVLLGNPDASDE-----QLQQALENAWVSEFLPLLPQgldtpigdqaaGL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 161 SGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVR-FLEELLLASN-QTIVFISH 214
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQlVMQALNAASRrQTTLMVTH 542
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
357-513 |
1.26e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigyfdqsrKSISDDKSLIELFcpnggdhimvrgrnyhvygy 436
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------IYIDGEDILEEVL-------------------- 46
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 437 lknFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGAILIVSHDRYFI 513
Cdd:smart00382 47 ---DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
331-509 |
1.49e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.83 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLfECKNLSKTIDNKVLfsDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgEIKIGYFDQSRKSISDDK 410
Cdd:COG3840 1 ML-RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG-----RILWNGQDLTALPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 -SLI----ELFcpnggDHIMVR-----GRN-------------------YHVYGYLKNflfpkefldKPvGVLSGGEKNR 461
Cdd:COG3840 73 vSMLfqenNLF-----PHLTVAqniglGLRpglkltaeqraqveqalerVGLAGLLDR---------LP-GQLSGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 462 LALALLFTKEYDCLILDEPTNDLDIA----TINILEEYLLSFEGAILIVSHD 509
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGLTVLMVTHD 189
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
363-542 |
1.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 363 IVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSISDDKSLIEL-------------------FCPnggdh 423
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLvfqfpeyqlfqetiekdiaFGP----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 424 IMVRGRNYHVYGYLKNFL----FPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT----INILEEY 495
Cdd:PRK13645 117 VNLGENKQEAYKKVPELLklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1196666485 496 LLSFEGAILIVSHDRYFIDKITNKLWAYENGKIEQIYMEYSEYLDIE 542
Cdd:PRK13645 197 NKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
344-485 |
1.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 344 NKVLFsDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSR--KSISDDKSLI------EL 415
Cdd:PRK13643 19 SRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeiKPVRKKVGVVfqfpesQL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 416 FCPNGGDHIMVRGRNYHVYG---------YLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD 485
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKekaekiaaeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-214 |
1.64e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.70 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 28 EKERI-AIIGKNGGGKSTLMKILRGEceIDSgrviRQNSISIEMLAQSPKFNDNLSVKDALNYELKEifdardeYEKVLA 106
Cdd:PRK13631 50 EKNKIyFIIGNSGSGKSTLVTHFNGL--IKS----KYGTIQVGDIYIGDKKNNHELITNPYSKKIKN-------FKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 107 QISNEHDNPELLHRQDELVKFI--------ESKDgwNIENKIERILDSFGLRE-YENRLVNSLSGGEIRRVALGALILKK 177
Cdd:PRK13631 117 RVSMVFQFPEYQLFKDTIEKDImfgpvalgVKKS--EAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1196666485 178 PDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISH 214
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILdakANNKTVFVITH 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-232 |
1.77e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqNSISIEMLAQSPKFndnLSVKDALNYElkeifdar 98
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---KVMGREVNAENEKW---VRSKVGLVFQ-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DEYEKVLAQiSNEHD------NPELlhRQDElvkfieskdgwnIENKIERILDSFGLREYENRLVNSLSGGEIRRVALGA 172
Cdd:PRK13647 87 DPDDQVFSS-TVWDDvafgpvNMGL--DKDE------------VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 173 LILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-214 |
1.83e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 16 KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVirqnSISIEMLaQSPKFNDNLSV---KDALNYELK 92
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV----TIGERVI-TAGKKNKKLKPlrkKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 93 E--IFDardeyEKVLAQISNEHDNpellhrqdelvkFIESKDgwNIENKIERILDSFGLRE-YENRLVNSLSGGEIRRVA 169
Cdd:PRK13634 95 EhqLFE-----ETVEKDICFGPMN------------FGVSEE--DAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1196666485 170 LGALILKKPDVLLLDEPTNHLDVY----MVRFLEELLLASNQTIVFISH 214
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKgrkeMMEMFYKLHKEKGLTTVLVTH 204
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-234 |
1.93e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.66 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGeCEIDSGRVIRQNSISIEMLAQSpkfNDNLSV 83
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINF-LEKPSEGSIVVNGQTINLVRDK---DGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 84 KDA-----LNYELKEIFDARDEYEKVLAqISNEHDNP-ELLHRQDELVKfieskdgwnieNKIERILDSFGLREY-ENRL 156
Cdd:PRK10619 82 ADKnqlrlLRTRLTMVFQHFNLWSHMTV-LENVMEAPiQVLGLSKQEAR-----------ERAVKYLAKVGIDERaQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMV----RFLEElLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgevlRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
..
gi 1196666485 233 AL 234
Cdd:PRK10619 229 KI 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
351-508 |
1.93e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 52.28 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 351 FNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIGYFDQSRKSISdDKSLIELFCPNG-GDHIMVR-- 427
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS-----GSLTLNGQDHTTTPPS-RRPVSMLFQENNlFSHLTVAqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 428 -GRNYH----VYGYLKNFL-------FPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA----TINI 491
Cdd:PRK10771 92 iGLGLNpglkLNAAQREKLhaiarqmGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAlrqeMLTL 171
|
170
....*....|....*..
gi 1196666485 492 LEEYLLSFEGAILIVSH 508
Cdd:PRK10771 172 VSQVCQERQLTLLMVSH 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
137-223 |
1.98e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.92 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 137 ENKIERILDSFGL-REYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDVyMVRF--LEelLLASNQ----- 207
Cdd:COG4172 402 RARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIArALILE-PKLLVLDEPTSALDV-SVQAqiLD--LLRDLQrehgl 477
|
90 100
....*....|....*....|
gi 1196666485 208 TIVFISHD----RYFIDRLA 223
Cdd:COG4172 478 AYLFISHDlavvRALAHRVM 497
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
331-531 |
2.01e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.55 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeLEADSGvinrGEIKIGYFDQSRKSISDDK 410
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQTS----GHIRFHGTDVSRLHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 -----SLIELFcpnggDHIMV-------------RGR-NYHV-------------YGYLKNfLFPKEfldkpvgvLSGGE 458
Cdd:PRK10851 76 vgfvfQHYALF-----RHMTVfdniafgltvlprRERpNAAAikakvtqllemvqLAHLAD-RYPAQ--------LSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 459 KNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL------LSFEGaiLIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlheeLKFTS--VFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
343-528 |
2.06e-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: 52.49 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG--VINRGEI----------KIGYFDQS----RKSI 406
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvLVDGHDLaladpawlrrQVGVVLQEnvlfNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDDKSLielfcpngGDHIMVRGRNYHVYGYLKNFLFPKEF---LDKPVGV----LSGGEKNRLALALLFTKEYDCLILDE 479
Cdd:cd03252 93 RDNIAL--------ADPGMSMERVIEAAKLAGAHDFISELpegYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 480 PTNDLDIATINILEEYL--LSFEGAILIVSHdRYFIDKITNKLWAYENGKI 528
Cdd:cd03252 165 ATSALDYESEHAIMRNMhdICAGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-234 |
2.12e-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: 52.49 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI---------------RQNSIsieMLAQSPKFN---- 78
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdghdlaladpawlrRQVGV---VLQENVLFNrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLSVKDAlNYELKEIFDArdeyekvlAQISNEHDnpellhrqdelvkFI-ESKDGWNienkieRILDSFGLreyenrlv 157
Cdd:cd03252 94 DNIALADP-GMSMERVIEA--------AKLAGAHD-------------FIsELPEGYD------TIVGEQGA-------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 158 nSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdRYFIDRLATRSVEIEDGAL 234
Cdd:cd03252 138 -GLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMhdICAGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
159-225 |
2.24e-07 |
|
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: 51.42 E-value: 2.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV----YMVRFLEELLLASNQTIVFISHDRYFIDRLATR 225
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDR 141
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
331-528 |
2.64e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKIL-LGELeADSGVINrgeIKIGYFDQSRKSisDD 409
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLET-PDSGQLN---IAGHQFDFSQKP--SE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 410 KSLIELFCPNGgdhiMVRgRNYHVYGYLK---NFL--------FPKE-----------------FLDKPVGVLSGGEKNR 461
Cdd:COG4161 75 KAIRLLRQKVG----MVF-QQYNLWPHLTvmeNLIeapckvlgLSKEqarekamkllarlrltdKADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 462 LALALLFTKEYDCLILDEPTNDLD------IATInILEeylLSFEGAI-LIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDpeitaqVVEI-IRE---LSQTGITqVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
355-509 |
2.73e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 355 VLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-------------RGEIK---IGYFDQSRKSISDDKSLIELFCP 418
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeeaRAKLRakhVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 419 nggdhIMVRGRNYH-----VYGYLKNFLFPKEFLDKPVGvLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILE 493
Cdd:PRK10584 113 -----ALLRGESSRqsrngAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180
....*....|....*....|
gi 1196666485 494 EYLLS----FEGAILIVSHD 509
Cdd:PRK10584 187 DLLFSlnreHGTTLILVTHD 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-234 |
2.76e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 15 DKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSISIEMLAQSPKfndNLSVKDALNYELKE 93
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHITPETGNKNLK---KLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 94 --IFDardeyEKVLAQISNEHDNpellhrqdelVKFIESKdgwnIENKIERILDSFGLRE-YENRLVNSLSGGEIRRVAL 170
Cdd:PRK13641 96 aqLFE-----NTVLKDVEFGPKN----------FGFSEDE----AKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 171 GALILKKPDVLLLDEPTNHLDVYMVRFLEELLL---ASNQTIVFISHDRYFIDRLATRSVEIEDGAL 234
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKdyqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-214 |
2.87e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQnsiSIEMLAQSpKFNDNLSV--KDALNYELKE--I 94
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD---DTLITSTS-KNKDIKQIrkKVGLVFQFPEsqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 95 FDardeyEKVLAQISNEHDNPELlhRQDELVKFIESKdgwnienkieriLDSFGLRE-YENRLVNSLSGGEIRRVALGAL 173
Cdd:PRK13649 99 FE-----ETVLKDVAFGPQNFGV--SQEEAEALAREK------------LALVGISEsLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1196666485 174 ILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISH 214
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVTH 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-215 |
3.03e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIEmlaqSPK------ 76
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGKPVE----GPGaergvv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 FNDN-----LSVKDALNYELKeifdardeyekvLAQISNEhdnpELLHRQDELVKFIeskdgwnienkierildsfGLRE 151
Cdd:PRK11248 76 FQNEgllpwRNVQDNVAFGLQ------------LAGVEKM----QRLEIAHQMLKKV-------------------GLEG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 152 YENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA----SNQTIVFISHD 215
Cdd:PRK11248 121 AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwqeTGKQVLLITHD 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
332-531 |
3.15e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.92 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSISDDKS 411
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 412 LIELFcpnggDHIMVRgRNYhVYGyLKNFLFPK-----------------EFLDKPVGVLSGGEKNRLALALLFTKEYDC 474
Cdd:PRK11607 99 SYALF-----PHMTVE-QNI-AFG-LKQDKLPKaeiasrvnemlglvhmqEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 475 LILDEPTNDLD--------IATINILEEYllsfeGAI-LIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:PRK11607 171 LLLDEPMGALDkklrdrmqLEVVDILERV-----GVTcVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
350-508 |
3.65e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 51.34 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEI---KIGYFDQsRKSISddkslielFCPNggDHIMV 426
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdisKIGLHDL-RSRIS--------IIPQ--DPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 427 RG--------RNYH----VYGYLKNFLFpKEFLDKPVG-----------VLSGGEKNRLALALLFTKEYDCLILDEPTND 483
Cdd:cd03244 91 SGtirsnldpFGEYsdeeLWQALERVGL-KEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180
....*....|....*....|....*..
gi 1196666485 484 LDIATINILEEYLLS-FEGA-ILIVSH 508
Cdd:cd03244 170 VDPETDALIQKTIREaFKDCtVLTIAH 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-192 |
3.86e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGrvirqnsiSIEMLAQSpkfndnlsVKDALNYELKEIFDAR 98
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG--------KISILGQP--------TRQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 DEYE---KVLAQ---ISNEHDNPELLHRQdelvkfiESKDGWNIENKIERIldsfGLREYENRLVNSLSGGEIRRVALGA 172
Cdd:PRK15056 87 EEVDwsfPVLVEdvvMMGRYGHMGWLRRA-------KKRDRQIVTAALARV----DMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180
....*....|....*....|
gi 1196666485 173 LILKKPDVLLLDEPTNHLDV 192
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDV 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
331-530 |
3.99e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTI-DNKVLFsDFNARVLQGERIGIVGRNGSGKSTMLKIL-LGELeADSGVINrgeIKIGYFDQSRKSisD 408
Cdd:PRK11124 1 MSIQLNGINCFYgAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEM-PRSGTLN---IAGNHFDFSKTP--S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 409 DKSLIELFCPNGgdhiMVRgRNYHVYGYL---KNF-------------------------LFPKEFLDKPVGVLSGGEKN 460
Cdd:PRK11124 74 DKAIRELRRNVG----MVF-QQYNLWPHLtvqQNLieapcrvlglskdqalaraekllerLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 461 RLALALLFTKEYDCLILDEPTNDLD--IAT--INILEEylLSFEGAI-LIVSHDRYFIDKITNKLWAYENGKI-EQ 530
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDpeITAqiVSIIRE--LAETGITqVIVTHEVEVARKTASRVVYMENGHIvEQ 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-214 |
4.12e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIIlNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFNdNLSVKDALNY-ELK 92
Cdd:TIGR00954 464 GDVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMT-LGTLRDQIIYpDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 93 EIFDARDEYEKVLAQISnehDNPELLHrqdelvkFIESKDGWNIenkierildsfgLREYEnrlvNSLSGGEIRRVALGA 172
Cdd:TIGR00954 542 EDMKRRGLSDKDLEQIL---DNVQLTH-------ILEREGGWSA------------VQDWM----DVLSGGEKQRIAMAR 595
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196666485 173 LILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQTIVFISH 214
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-222 |
4.42e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGEceidsgRVIRQNSISIEMlaQSPKFNDNLSVKDAlnyelkeIFDA 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------LKGTPVAGCVDV--PDNQFGREASLIDA-------IGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 98 RDEYEKVlaqisnehdnpELLHRQdelvkfieskdGWNienkierilDSFGLReyenRLVNSLSGGEIRRVALGALILKK 177
Cdd:COG2401 110 GDFKDAV-----------ELLNAV-----------GLS---------DAVLWL----RRFKELSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1196666485 178 PDVLLLDEPTNHLDVYMVRF----LEELLLASNQTIVFISHDRYFIDRL 222
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRvarnLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-214 |
4.50e-07 |
|
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: 52.90 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG-------ECEID-SGRVIRQNSIS------I 68
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwDGEIYwSGSPLKASNIRdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 69 EMLAQSPKFNDNLSVkdalnyeLKEIFDARDeyekvLAQISNEHDNPELLHRQDELVKfieskdgwniENKIERILDSfg 148
Cdd:TIGR02633 81 VIIHQELTLVPELSV-------AENIFLGNE-----ITLPGGRMAYNAMYLRAKNLLR----------ELQLDADNVT-- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 149 lreyenRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEEL---LLASNQTIVFISH 214
Cdd:TIGR02633 137 ------RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISH 199
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-215 |
4.83e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKII----LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGEceID-SGRVIrqnsisiemlAQSP 75
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVM----------AEKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 76 KFNDNlsvkdalnyELKEIfDARDEYEKVLAQISNEHDNPELLHRQDELVKF-----IESKDGWNIENKIERILDSF--- 147
Cdd:PRK11022 69 EFNGQ---------DLQRI-SEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFqimeaIKVHQGGNKKTRRQRAIDLLnqv 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 148 GLREYENRL---VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA----SNQTIVFISHD 215
Cdd:PRK11022 139 GIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElqqkENMALVLITHD 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
357-541 |
5.18e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigYFDQSR---KSISDDKSLIELFCPNGGDHIMVRGRNYHV 433
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI--------FYNNQAitdDNFEKLRKHIGIVFQNPDNQFVGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 434 YGYLKNFLFPKEFLDKPVG-----------------VLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT----INIL 492
Cdd:PRK13648 106 AFGLENHAVPYDEMHRRVSealkqvdmleradyepnALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 493 EEYLLSFEGAILIVSHD-------RYFIdkITNKLWAYENGKIEQIYMEYSEYLDI 541
Cdd:PRK13648 186 RKVKSEHNITIISITHDlseameaDHVI--VMNKGTVYKEGTPTEIFDHAEELTRI 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
331-398 |
5.26e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 51.65 E-value: 5.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 331 MLfECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-------NRGEI-KIGY 398
Cdd:COG4152 1 ML-ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgeplDPEDRrRIGY 75
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
350-509 |
5.35e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 50.93 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLG-ELEADSGVINRGEiKIGYFDQSRKSISDDKSLIE--------LFCPNG 420
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGK-QITEPGPDRMVVFQNYSLLPwltvreniALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 421 GDHIMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSF- 499
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIw 161
|
170
....*....|...
gi 1196666485 500 ---EGAILIVSHD 509
Cdd:TIGR01184 162 eehRVTVLMVTHD 174
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
139-215 |
5.62e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 139 KIERILDSFGLR-EYENRLVNSLSGGEIRRVALG-ALILKkPDVLLLDEPTNHLDV--------YMVRFLEELLLAsnqt 208
Cdd:PRK11308 133 KALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIArALMLD-PDVVVADEPVSALDVsvqaqvlnLMMDLQQELGLS---- 207
|
....*..
gi 1196666485 209 IVFISHD 215
Cdd:PRK11308 208 YVFISHD 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
330-520 |
5.67e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 330 KMLFECKNLSKTIDNKVLFSDFNARVL----QGERIGIVGRNGSGKSTMLKILLGELEADSG-VINRGEI---------- 394
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSfsigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFNGQPmsklssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 395 -----KIGYFDQSRKSISDDKSLIELFCPnggdhIMVRGRNyhvygylknflfPKEFLDK------PVGV---------- 453
Cdd:PRK11629 83 elrnqKLGFIYQFHHLLPDFTALENVAMP-----LLIGKKK------------PAEINSRalemlaAVGLehranhrpse 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 454 LSGGEKNRLALALLFTKEYDCLILDEPTNDLDI----ATINILEEYLLSFEGAILIVSHDRYFIDKITNKL 520
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDArnadSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-191 |
5.98e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 3 LIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGeceidsgrVIRQNSISIEMLAQSPKfndnls 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--------LLNPEKGEILFERQSIK------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 vKDalnyelkeifdaRDEYEKVLAQISNEHD-NPELLHRQDELVKFIESKDgwNIEnkIERILDSFGLREYENRLVNSLS 161
Cdd:PRK13540 67 -KD------------LCTYQKQLCFVGHRSGiNPYLTLRENCLYDIHFSPG--AVG--ITELCRLFSLEHLIDYPCGLLS 129
|
170 180 190
....*....|....*....|....*....|
gi 1196666485 162 GGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:PRK13540 130 SGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-234 |
6.99e-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: 52.41 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 19 LNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRqnsisiemlaqspkfnDNLSVKDalnYELKeifDAR 98
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL----------------DGHDLAD---YTLA---SLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 99 deyekvlAQISNEHDNPELLhrQDELVKFIESKDGWNI-ENKIERILDSFGLREYENRLVNS-----------LSGGEIR 166
Cdd:TIGR02203 406 -------RQVALVSQDVVLF--NDTIANNIAYGRTEQAdRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 167 RVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT-----RSVEIEDGAL 234
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALerLMQGRTTLVIAH------RLSTiekadRIVVMDDGRI 545
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-318 |
8.35e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 16 KIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISieMLAQSPKFNdNLSVKDALNYelkeiF 95
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIA--YVPQQAWIM-NATVRGNILF-----F 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 96 DARDE--YEKVLAQISNEHDNPELlhrqdelvkfieskdGWNIENKIERildsfglreyenRLVNsLSGGEIRRVALGAL 173
Cdd:PTZ00243 745 DEEDAarLADAVRVSQLEADLAQL---------------GGGLETEIGE------------KGVN-LSGGQKARVSLARA 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 174 ILKKPDVLLLDEPTNHLDVYM-VRFLEELLLA--SNQTIVFISHDRYFIDRlATRSVEIEDGALRsFDGGYANYL-TKKE 249
Cdd:PTZ00243 797 VYANRDVYLLDDPLSALDAHVgERVVEECFLGalAGKTRVLATHQVHVVPR-ADYVVALGDGRVE-FSGSSADFMrTSLY 874
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 250 EILRSLAKSHETLiKNLKSEEEWLR----RGVKARLKRNEGrKQRILAMREEAKKNPGLIRRVKLELERASKS 318
Cdd:PTZ00243 875 ATLAAELKENKDS-KEGDADAEVAEvdaaPGGAVDHEPPVA-KQEGNAEGGDGAALDAAAGRLMTREEKASGS 945
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
350-488 |
8.68e-07 |
|
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: 52.61 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRgeikigyfdQSRKSISDDKSLIelfCPNGGDHIMVRGR 429
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH---------SGRISFSPQTSWI---MPGTIKDNIIFGL 511
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 430 NYHVYGYLKNF----------LFPKEflDKPV----GV-LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIAT 488
Cdd:TIGR01271 512 SYDEYRYTSVIkacqleediaLFPEK--DKTVlgegGItLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
329-485 |
9.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 329 KKMLFECKNLS-KTIDN-----KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELeadsgVINRGEIKIGYFDQS 402
Cdd:PRK13633 1 MNEMIKCKNVSyKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL-----IPSEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 -RKSISDDKSLIELFCPNGGDHIM---------------------VRGRnyhVYGYLKNFLFpKEFLDKPVGVLSGGEKN 460
Cdd:PRK13633 76 dEENLWDIRNKAGMVFQNPDNQIVativeedvafgpenlgippeeIRER---VDESLKKVGM-YEYRRHAPHLLSGGQKQ 151
|
170 180
....*....|....*....|....*
gi 1196666485 461 RLALALLFTKEYDCLILDEPTNDLD 485
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
350-485 |
1.04e-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: 50.31 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQS--RKSISDDKSLIELFCPNGGDHIM-- 425
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslRRQIGLVSQDVFLFNDTVAENIAyg 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 426 --------VR--GRNYHVYGYLKNFlfpKEFLDKPVGV----LSGGEKNRLALALLFTKEYDCLILDEPTNDLD 485
Cdd:cd03251 100 rpgatreeVEeaARAANAHEFIMEL---PEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
336-528 |
1.05e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFdqSRKSISDDKSLIEL 415
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY--ASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 416 FCPNGGD----HIMVRGRnyhvygYLKNFLFPK-------------------EFLDKPVGVLSGGEKNRLALALLFTKEY 472
Cdd:PRK10253 89 NATTPGDitvqELVARGR------YPHQPLFTRwrkedeeavtkamqatgitHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 473 DCLILDEPTNDLDIA-TINILEeyLLS----FEGAIL-IVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK10253 163 AIMLLDEPTTWLDIShQIDLLE--LLSelnrEKGYTLaAVLHDLNQACRYASHLIALREGKI 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
332-492 |
1.07e-06 |
|
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: 51.75 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLG----------------ELEAdSGVINRGEIK 395
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKA-SNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 396 IGYFDQSRKSISDDKSLIELFCpngGDHIMVRGRNYH-------VYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLF 468
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFL---GNEITLPGGRMAynamylrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180
....*....|....*....|....
gi 1196666485 469 TKEYDCLILDEPTNDLDIATINIL 492
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEIL 180
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-191 |
1.21e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 8 EVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECE---------IDSGRVIRQNSISIEMLAQSPKFN 78
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnftgtilANNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLSVKDALnyelkeIFDArdeyekvLAQIsnehdnPELLHRQDELVKfieskdgwnienkIERILDSFGLREYENRLV- 157
Cdd:PLN03211 153 PHLTVRETL------VFCS-------LLRL------PKSLTKQEKILV-------------AESVISELGLTKCENTIIg 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196666485 158 NS----LSGGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:PLN03211 201 NSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-214 |
1.40e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGE--CEIDSGRVIRQNSiSIemLAQSPKFNDNLSVKDALNYEL 91
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGE-SI--LDLEPEERAHLGIFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 92 kEIfdardeyekvlAQISNEhDNPELLHRQDELVKFIESKDGWNIENKIERILDSFGLRE-YENRLVNS-LSGGEIRRVA 169
Cdd:CHL00131 95 -EI-----------PGVSNA-DFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196666485 170 LGALILKKPDVLLLDEPTNHLDVYMVRFLEE---LLLASNQTIVFISH 214
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEginKLMTSENSIILITH 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
332-389 |
1.68e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 1.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-215 |
1.92e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 14 GDKIILNETNFNVNEKERIAIIGKNGGGKST----LMKILRGECEID-SGRVIRQNSISiEMLAQSPK----FNDNLSvk 84
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWfDGQPLHNLNRR-QLLPVRHRiqvvFQDPNS-- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 dALNyelkeifdARDEYEKVLAQISNEHdNPELLHRQDElvkfieskdgwnieNKIERILDSFGLR-EYENRLVNSLSGG 163
Cdd:PRK15134 374 -SLN--------PRLNVLQIIEEGLRVH-QPTLSAAQRE--------------QQVIAVMEEVGLDpETRHRYPAEFSGG 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 164 EIRRVALG-ALILKkPDVLLLDEPTNHLDVYMVRFLEELLLASNQT----IVFISHD 215
Cdd:PRK15134 430 QRQRIAIArALILK-PSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHD 485
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-485 |
1.94e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.99 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 325 NQNRKKMlFECKNL--SKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIGYFDQS 402
Cdd:PRK13632 1 IKNKSVM-IKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS-----GEIKIDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 RKSISDDKSLIELFCPNGGDH-IMVRGRNYHVYGyLKNFLFP-----------------KEFLDKPVGVLSGGEKNRLAL 464
Cdd:PRK13632 75 KENLKEIRKKIGIIFQNPDNQfIGATVEDDIAFG-LENKKVPpkkmkdiiddlakkvgmEDYLDKEPQNLSGGQKQRVAI 153
|
170 180
....*....|....*....|.
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLD 485
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLD 174
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
350-485 |
2.00e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIgyfdQSRKSISDDKSL------------IELFC 417
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI----TAGKKNKKLKPLrkkvgivfqfpeHQLFE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 418 PNGGDHIMVRGRNYHV---------YGYLKNFLFPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLD 485
Cdd:PRK13634 101 ETVEKDICFGPMNFGVseedakqkaREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-530 |
2.03e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.00 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEAdsgvinRGEIKI-GY------FDQSRKSIS---DDKSL 412
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY------QGSLKInGIelreldPESWRKHLSwvgQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 IE--------LFCPNGGDHimvrgrnyHVYGYLKNfLFPKEFLDK-PVGV----------LSGGEKNRLALALLFTKEYD 473
Cdd:PRK11174 435 PHgtlrdnvlLGNPDASDE--------QLQQALEN-AWVSEFLPLlPQGLdtpigdqaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 474 CLILDEPTNDLDI----ATINILEEYllSFEGAILIVSHDryfIDKITN--KLWAYENGKIEQ 530
Cdd:PRK11174 506 LLLLDEPTASLDAhseqLVMQALNAA--SRRQTTLMVTHQ---LEDLAQwdQIWVMQDGQIVQ 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
355-510 |
2.04e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.73 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 355 VLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGyfDQSRKSISDDKSLI----ELFCPNGGDHIMVrGR- 429
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR--TVTRASLRRNIAVVfqdaGLFNRSIEDNIRV-GRp 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 430 ---NYHVYGYLK-----NFLFPKEF-LDKPVG----VLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATinilEEYL 496
Cdd:PRK13657 435 datDEEMRAAAEraqahDFIERKPDgYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKV 510
|
170
....*....|....
gi 1196666485 497 lsfEGAILIVSHDR 510
Cdd:PRK13657 511 ---KAALDELMKGR 521
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-221 |
2.12e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-----RQNSISIEMLAQSPKfNDNLSVKDALNYEL- 91
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneHTNDMTNEQDYQGDE-EQNVGMKNVNEFSLt 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 92 KEIFDARD-----------------------EYEKVLAQISNEhdnPELLHRQ-DELVKFieSKDGWNIENkIERILDSF 147
Cdd:PTZ00265 1262 KEGGSGEDstvfknsgkilldgvdicdynlkDLRNLFSIVSQE---PMLFNMSiYENIKF--GKEDATRED-VKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 148 GLREYENRLVN-----------SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLL----ASNQTIVFI 212
Cdd:PTZ00265 1336 AIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADKTIITI 1415
|
....*....
gi 1196666485 213 SHDRYFIDR 221
Cdd:PTZ00265 1416 AHRIASIKR 1424
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
343-485 |
2.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.60 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG-VINRGeIKIGYFDQsrksISDDKSLIELFCPNGG 421
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkVLVSG-IDTGDFSK----LQGIRKLVGIVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 422 DHIMVRGRNYHVYGYLKNFLFP----KEFLDKPVG-------------VLSGGEKNRLALALLFTKEYDCLILDEPTNDL 484
Cdd:PRK13644 88 TQFVGRTVEEDLAFGPENLCLPpieiRKRVDRALAeiglekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
.
gi 1196666485 485 D 485
Cdd:PRK13644 168 D 168
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-531 |
2.53e-06 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 49.16 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIgyfdqsrksisDDKSLI 413
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS-----GEILL-----------DGKDIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELfcPNGGDHIMVRGRNYHVYGYL---KNFLFP------------------------KEFLDKPVGVLSGGEKNRLALAL 466
Cdd:cd03300 66 NL--PPHKRPVNTVFQNYALFPHLtvfENIAFGlrlkklpkaeikervaealdlvqlEGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 467 LFTKEYDCLILDEPTNDLD--------IATINILEEYLLSFegaiLIVSHDRYFIDKITNKLWAYENGKIEQI 531
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDlklrkdmqLELKRLQKELGITF----VFVTHDQEEALTMSDRIAVMNKGKIQQI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-232 |
2.63e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.03 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 8 EVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRqnsisiemlaqspkfnDNLSVKDAL 87
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI----------------DGVDIAKIS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 88 NYELKEIfdardEYEKVLAQISNEHDNPELLHRQDelVKFIESKDGWNIENKIERILDSF---GLREYENRLVNSLSGGE 164
Cdd:PRK10070 97 DAELREV-----RRKKIAMVFQSFALMPHMTVLDN--TAFGMELAGINAEERREKALDALrqvGLENYAHSYPDELSGGM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 165 IRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDG 232
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
325-389 |
2.64e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.95 E-value: 2.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 325 NQNRKKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
331-531 |
2.76e-06 |
|
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: 48.87 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIGYFDQSRKSISDdk 410
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS-----GTILFGGEDATDVPVQE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 slielfcpnggdhimvRG-----RNYHVYGYL---KNFLF-----------PKEFLDKPV-----------------GVL 454
Cdd:cd03296 74 ----------------RNvgfvfQHYALFRHMtvfDNVAFglrvkprserpPEAEIRAKVhellklvqldwladrypAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 455 SGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGAI----LIVSHDRYFIDKITNKLWAYENGKIEQ 530
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
.
gi 1196666485 531 I 531
Cdd:cd03296 218 V 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
336-509 |
2.90e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeLEADSGvinrGEIKIG-------------YFDQS 402
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSA----GELLAGtaplaearedtrlMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 R----KSISDDKSLielfcpnGgdhimvrgrnyhvygyLKNFLFPK--EFLDKpVGV----------LSGGEKNRLALAL 466
Cdd:PRK11247 91 RllpwKKVIDNVGL-------G----------------LKGQWRDAalQALAA-VGLadranewpaaLSGGQKQRVALAR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1196666485 467 LFTKEYDCLILDEPTNDLDIAT---INILEEYLLSFEG-AILIVSHD 509
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTrieMQDLIESLWQQHGfTVLLVTHD 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-203 |
3.28e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 24 FNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI-----------RQNSISIEMLAQSPkfndnlsvKDALNyelk 92
Cdd:PRK15112 34 FTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhfgdySYRSQRIRMIFQDP--------STSLN---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 93 eifdARDEYEKVLaqisnehDNPELLHrqDELvkfieskDGWNIENKIERILDSFGLR-EYENRLVNSLSGGEIRRVALG 171
Cdd:PRK15112 102 ----PRQRISQIL-------DFPLRLN--TDL-------EPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190
....*....|....*....|....*....|...
gi 1196666485 172 -ALILkKPDVLLLDEPTNHLDVYMVRFLEELLL 203
Cdd:PRK15112 162 rALIL-RPKVIIADEALASLDMSMRSQLINLML 193
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
355-508 |
3.65e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 355 VLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIgyfdqsRKSISDDKSLIElFCPNgGDHI--MVRGRNyH 432
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTNISDVHQNMG-YCPQ-FDAIddLLTGRE-H 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 433 VYGYLKNFLFPKE-----------------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEY 495
Cdd:TIGR01257 2033 LYLYARLRGVPAEeiekvanwsiqslglslYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170
....*....|....*.
gi 1196666485 496 LLSF---EGAILIVSH 508
Cdd:TIGR01257 2113 IVSIireGRAVVLTSH 2128
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-240 |
3.82e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.80 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 34 IIGKNGGGKSTLMKILRGECEIDSGRvIRQNSISIEMLAQ-------SPKFNDnlsvkdalnYELkeiFDArdeyekvLA 106
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGE-ILLDGQPVTADNReayrqlfSAVFSD---------FHL---FDR-------LL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 107 QISNEHDnPELLhrQDELVKFieskdgwNIENKierildsfgLREYENRLVN-SLSGGEIRRVALGALILKKPDVLLLDE 185
Cdd:COG4615 423 GLDGEAD-PARA--RELLERL-------ELDHK---------VSVEDGRFSTtDLSQGQRKRLALLVALLEDRPILVFDE 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 186 ------PTNhldvymvR--FLEELL--L-ASNQTIVFISHD-RYFIdrLATRSVEIEDGALRSFDGG 240
Cdd:COG4615 484 waadqdPEF-------RrvFYTELLpeLkARGKTVIAISHDdRYFD--LADRVLKMDYGKLVELTGP 541
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-191 |
3.91e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 1 MALIDLIEVSKKFGDKI-ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGeceidsgrvIRQNSISIEmlaQSPKFNd 79
Cdd:cd03233 4 LSWRNISFTTGKGRSKIpILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---------RTEGNVSVE---GDIHYN- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 80 nlsvkdalNYELKEIFdardEYEKVLAQISNEHDN--PELLHRQdelvkfieskdgwnienkierILDsFGLREYENRLV 157
Cdd:cd03233 71 --------GIPYKEFA----EKYPGEIIYVSEEDVhfPTLTVRE---------------------TLD-FALRCKGNEFV 116
|
170 180 190
....*....|....*....|....*....|....
gi 1196666485 158 NSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:cd03233 117 RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-213 |
4.36e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 10 SKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIdSGRVIRQNSISIEM----LAQSPKFN 78
Cdd:NF033858 273 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtgllpasEGEAWL-FGQPVDAGDIATRRrvgyMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLSVKDalNYELkeifDARdeyekvLAQISNEHdnpellhrqdelvkfieskdgwnIENKIERILDSFGLREYENRLVN 158
Cdd:NF033858 352 GELTVRQ--NLEL----HAR------LFHLPAAE-----------------------IAARVAEMLERFDLADVADALPD 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 159 SLSGGeIR-RVALGALILKKPDVLLLDEPTNHLD-VYMVRFLEELL-LASNQ--TIvFIS 213
Cdd:NF033858 397 SLPLG-IRqRLSLAVAVIHKPELLILDEPTSGVDpVARDMFWRLLIeLSREDgvTI-FIS 454
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-234 |
5.34e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 7 IEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRgeceidsgrvirqnsisiemlaqspKFNDNLS---- 82
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLN-------------------------RMNDKVSgyry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 83 VKDALnYELKEIFDARD--EYEKVLAQISnEHDNPELLHRQDELV------KFIESKDgwnIENKIERILDSFGLRE-YE 153
Cdd:PRK14271 80 SGDVL-LGGRSIFNYRDvlEFRRRVGMLF-QRPNPFPMSIMDNVLagvrahKLVPRKE---FRGVAQARLTEVGLWDaVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 154 NRLVNS---LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHDRYFIDRLATRSVE 228
Cdd:PRK14271 155 DRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIrsLADRLTVIIVTHNLAQAARISDRAAL 234
|
....*.
gi 1196666485 229 IEDGAL 234
Cdd:PRK14271 235 FFDGRL 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
362-528 |
5.40e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 362 GIVGRNGSGKSTMLKILLGELEADSG-VINRGEIkigyFDQSRKSISDDKSLIELFCPNGGDHIMVRGRNYHVYGYLKNF 440
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGaVLWQGKP----LDYSKRGLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 441 LFPKE-----------------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA----TINILEEyLLSF 499
Cdd:PRK13638 107 GVPEAeitrrvdealtlvdaqhFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAgrtqMIAIIRR-IVAQ 185
|
170 180
....*....|....*....|....*....
gi 1196666485 500 EGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK13638 186 GNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
327-532 |
6.01e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.55 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 327 NRKKMLFECKNLS---KTIDNKVLF----------SDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG-VINRG 392
Cdd:PRK15079 3 EGKKVLLEVADLKvhfDIKDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 393 EIKIGYFDQSRKSISDDKSLI---ELFCPNG----GDHIMVRGRNYHVY-----------------GYLKNFL--FPKEF 446
Cdd:PRK15079 83 KDLLGMKDDEWRAVRSDIQMIfqdPLASLNPrmtiGEIIAEPLRTYHPKlsrqevkdrvkammlkvGLLPNLInrYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 447 ldkpvgvlSGGEKNRLALALLFTKEYDCLILDEPTNDLDIA----TINILEEylLSFE-GAILI-VSHDRYFIDKITNKL 520
Cdd:PRK15079 163 --------SGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaqVVNLLQQ--LQREmGLSLIfIAHDLAVVKHISDRV 232
|
250
....*....|....*...
gi 1196666485 521 W------AYENGKIEQIY 532
Cdd:PRK15079 233 LvmylghAVELGTYDEVY 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
324-544 |
6.81e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 324 LNQNRKKMLFECKNLS---KTIDNKVL-FSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELeADSGVI------NRGE 393
Cdd:PRK09473 4 LAQQQADALLDVKDLRvtfSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsatfNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 394 IKIGYFDQSRKSISDDKSLI---ELFCPNG----GDHIMVRGRNYHVYGYLKNF--------------------LFPKEF 446
Cdd:PRK09473 83 ILNLPEKELNKLRAEQISMIfqdPMTSLNPymrvGEQLMEVLMLHKGMSKAEAFeesvrmldavkmpearkrmkMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 447 ldkpvgvlSGGEKNR--LALALLftkeydC----LILDEPTNDLDI---ATI-NILEEYLLSFEGAILIVSHDRYFIDKI 516
Cdd:PRK09473 163 --------SGGMRQRvmIAMALL------CrpklLIADEPTTALDVtvqAQImTLLNELKREFNTAIIMITHDLGVVAGI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1196666485 517 TNK-LWAY-----ENGKIEQIYME----YSE-------YLDIEEE 544
Cdd:PRK09473 229 CDKvLVMYagrtmEYGNARDVFYQpshpYSIgllnavpRLDAEGE 273
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
333-491 |
1.16e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 47.15 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-------------NRGEIKIGYF 399
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 400 DQ-----SRKSISDDKSLIELFCPNGGDHIMVRgrnyhvygyLKNFLfpKEF-----LDKPVGVLSGGEKNRLALALLFT 469
Cdd:cd03218 81 PQeasifRKLTVEENILAVLEIRGLSKKEREEK---------LEELL--EEFhithlRKSKASSLSGGERRRVEIARALA 149
|
170 180
....*....|....*....|...
gi 1196666485 470 KEYDCLILDEPTNDLD-IATINI 491
Cdd:cd03218 150 TNPKFLLLDEPFAGVDpIAVQDI 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
343-485 |
1.28e-05 |
|
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: 47.15 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 343 DNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILL-------GELEADSGVINRGEI-----KIGYFDQS----RKSI 406
Cdd:cd03249 15 DVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEILLDGVDIRDLNLrwlrsQIGLVSQEpvlfDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDDkslIeLFCPNGGDHIMV----RGRNYHvygylkNFL--FPKEFlDKPVG----VLSGGEKNRLALALLFTKEYDCLI 476
Cdd:cd03249 94 AEN---I-RYGKPDATDEEVeeaaKKANIH------DFImsLPDGY-DTLVGergsQLSGGQKQRIAIARALLRNPKILL 162
|
....*....
gi 1196666485 477 LDEPTNDLD 485
Cdd:cd03249 163 LDEATSALD 171
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
350-528 |
1.36e-05 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 47.79 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 350 DFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVIN-RGEI---------------KIGY-FDQSRksisddksl 412
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlGGEVlqdsargiflpphrrRIGYvFQEAR--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 413 ieLFcpnggDHIMVRGrNYHvYGY------LKNFLFPK--------EFLDKPVGVLSGGEKNRLAL--ALLftKEYDCLI 476
Cdd:COG4148 88 --LF-----PHLSVRG-NLL-YGRkrapraERRISFDEvvellgigHLLDRRPATLSGGERQRVAIgrALL--SSPRLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 477 LDEPTNDLDIATIN-ILeEYLLS----FEGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:COG4148 157 MDEPLAALDLARKAeIL-PYLERlrdeLDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
227-283 |
1.42e-05 |
|
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: 43.72 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196666485 227 VEIEDGALRSFDGGYANYLTKKEEILRSLAKSHETLIKNLKSEEEWLRRG---------VKARLKR 283
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFrakaskakqAQSRIKA 66
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
332-509 |
1.57e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInrgeikigYFDqsrksisddks 411
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI--------LFD----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 412 lielfcpngGDHI--MVRGRNYHV---------YGYL-------KNFLFP-KEFLDKP--------------VGV----- 453
Cdd:PRK11831 68 ---------GENIpaMSRSRLYTVrkrmsmlfqSGALftdmnvfDNVAYPlREHTQLPapllhstvmmkleaVGLrgaak 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 454 -----LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGAI----LIVSHD 509
Cdd:PRK11831 139 lmpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-241 |
1.62e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 136 IENKIErILDSFGLREYE-NRLVNSLSGGEIRRVALGALIL---KKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---T 208
Cdd:PRK00635 786 IHEKIH-ALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHqghT 864
|
90 100 110
....*....|....*....|....*....|....*
gi 1196666485 209 IVFISHDRYFIdRLATRSVEI--EDGALrsfdGGY 241
Cdd:PRK00635 865 VVIIEHNMHVV-KVADYVLELgpEGGNL----GGY 894
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-508 |
1.67e-05 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 46.45 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 333 FECKNLSKTIDNKVLfSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEI------------KIGYFD 400
Cdd:cd03254 5 FENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 401 Q---------------SRKSISDDKSLIELFCPNGGDHIMVRGRNYHVYgylknflfpkefLDKPVGVLSGGEKNRLALA 465
Cdd:cd03254 84 QdtflfsgtimenirlGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTV------------LGENGGNLSQGERQLLAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1196666485 466 LLFTKEYDCLILDEPTNDLDIATINILEEYLLS-FEG-AILIVSH 508
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-508 |
1.74e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.76 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 329 KKMLFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKIL--LGELEADSGVinRGEIKI---GYFDQSR 403
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEARV--EGEVRLfgrNIYSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 404 KSISDDKSLIELF-CPNGGDHIMVRgRNYHVYGYLKNFLFPKEFLDKPV---------------------GVLSGGEKNR 461
Cdd:PRK14267 79 DPIEVRREVGMVFqYPNPFPHLTIY-DNVAIGVKLNGLVKSKKELDERVewalkkaalwdevkdrlndypSNLSGGQRQR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1196666485 462 LALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSF--EGAILIVSH 508
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-509 |
1.85e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGrvirqnSISIEmlAQSPKFNdnlSVKDALN 88
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAG------SILID--GQEMRFA---STTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 89 YElkeifdardeyekvLAQISNE-HDNPELLHRQDELVKFIESKDGW-NIENKIER---ILDSFGLREYENRLVNSLSGG 163
Cdd:PRK11288 79 AG--------------VAIIYQElHLVPEMTVAENLYLGQLPHKGGIvNRRLLNYEareQLEHLGVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 164 EIRRVALGALILKKPDVLLLDEPTNHLDvymVRFLEEL------LLASNQTIVFISHDRYFIDRLATRSVEIEDGAL-RS 236
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLS---AREIEQLfrvireLRAEGRVILYVSHRMEEIFALCDAITVFKDGRYvAT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 237 FDggyanyltkkeeilrSLAK-SHETLIKNLKseeewlrrgvkarlkrneGRK-QRILAMREEAkknpglIRRVKLELER 314
Cdd:PRK11288 222 FD---------------DMAQvDRDQLVQAMV------------------GREiGDIYGYRPRP------LGEVRLRLDG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 315 ASksfnGGGLNQNrkkmlfecknlsktidnkvlfSDFNARvlQGERIGIVGRNGSGKSTMLKILLGeleADSgvINRGEI 394
Cdd:PRK11288 263 LK----GPGLREP---------------------ISFSVR--AGEIVGLFGLVGAGRSELMKLLYG---ATR--RTAGQV 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 395 KIgyfDQSRKSISDDKSLIE---LFCPNG------------GDHIMVRGRNYHV-YGYLKNFLFPKEFLDK--------- 449
Cdd:PRK11288 311 YL---DGKPIDIRSPRDAIRagiMLCPEDrkaegiipvhsvADNINISARRHHLrAGCLINNRWEAENADRfirslnikt 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 450 -----PVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDI---ATI-NILeeYLLSFEG-AILIVSHD 509
Cdd:PRK11288 388 psreqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgakHEIyNVI--YELAAQGvAVLFVSSD 455
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-508 |
1.87e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 1.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196666485 444 KEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSF--EGAILIVSH 508
Cdd:PRK14247 137 KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
357-389 |
1.87e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.87 E-value: 1.87e-05
10 20 30
....*....|....*....|....*....|...
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-51 |
1.95e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1196666485 1 MALIDLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG 51
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
152-215 |
2.11e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.50 E-value: 2.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 152 YENRLVNS-LSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ---TIVFISHD 215
Cdd:cd03215 96 AENIALSSlLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADagkAVLLISSE 163
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-238 |
2.27e-05 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 45.87 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRV-IRQNSIS----------IEMLAQSPKFndnlsvkda 86
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDIStipledlrssLTIIPQDPTL--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 87 LNYELKEIFDARDEYEkvlaqisnehdnpellhrQDELVKFIESKDGWNienkierildsfglreyenrlvnSLSGGEIR 166
Cdd:cd03369 94 FSGTIRSNLDPFDEYS------------------DEEIYGALRVSEGGL-----------------------NLSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 167 RVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHdryfidRLAT-----RSVEIEDGALRSFD 238
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIreEFTNSTILTIAH------RLRTiidydKILVMDAGEVKEYD 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
334-531 |
2.64e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 46.63 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 334 ECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSgvinrGEIKIgyfdqsrksisDDKSLI 413
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDS-----GRILL-----------DGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 414 ELfcPNGGDHI-MVRgRNY----H--V-----YGyLKNFLFPKE-----------------FLDKPVGVLSGGEKNRLAL 464
Cdd:COG3842 71 GL--PPEKRNVgMVF-QDYalfpHltVaenvaFG-LRMRGVPKAeirarvaellelvglegLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLD--------IATINILEEYLLSFegaiLIVSHDRY----FIDKItnklwA-YENGKIEQI 531
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDaklreemrEELRRLQRELGITF----IYVTHDQEealaLADRI-----AvMNDGRIEQV 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
335-485 |
3.40e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 335 CKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIG-YFDQSR-------KSI 406
Cdd:PRK13631 29 CVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdKKNNHElitnpysKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 407 SDDKSL------------IELFCPNGGDHIM----------VRGRNYHVYgYLKNFLFPKEFLDKPVGVLSGGEKNRLAL 464
Cdd:PRK13631 109 KNFKELrrrvsmvfqfpeYQLFKDTIEKDIMfgpvalgvkkSEAKKLAKF-YLNKMGLDDSYLERSPFGLSGGQKRRVAI 187
|
170 180
....*....|....*....|.
gi 1196666485 465 ALLFTKEYDCLILDEPTNDLD 485
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLD 208
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
33-227 |
3.47e-05 |
|
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: 46.53 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 33 AIIGKNGGGKSTLMKILRGECEIDSGRVIRQN-----------SISIEM-----LAQSPKFNDNLSVKDALNYELKEIfd 96
Cdd:COG3593 27 VLVGENNSGKSSILEALRLLLGPSSSRKFDEEdfylgddpdlpEIEIELtfgslLSRLLRLLLKEEDKEELEEALEEL-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 97 aRDEYEKVLAQISNE-HDNPELLHRQDELVKFIESKDGWNIENKIerildSFGLREYENRLVNSLSGGEIRRVALGALIL 175
Cdd:COG3593 105 -NEELKEALKALNELlSEYLKELLDGLDLELELSLDELEDLLKSL-----SLRIEDGKELPLDRLGSGFQRLILLALLSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196666485 176 -------KKPDVLLLDEPTNHLDVYMVR----FLEELLLASNQtiVFIS-HDRYFIDRLATRSV 227
Cdd:COG3593 179 laelkraPANPILLIEEPEAHLHPQAQRrllkLLKELSEKPNQ--VIITtHSPHLLSEVPLENI 240
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-221 |
3.60e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 3.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 154 NRLVNSLSGGEIRRVALGALILK--KPDVLLLDEPTNHLDVYMV-RFLEEL--LLASNQTIVFISHDRYFIDR 221
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDInQLLEVIkgLIDLGNTVILIEHNLDVLSS 154
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
159-215 |
3.98e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 3.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 159 SLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELL--LASNQTIVFISHD 215
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMheLKEQYTIIIVTHN 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
337-515 |
4.44e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 337 NLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGvinrgeiKIGYFDQSRKSisDDKSLIELF 416
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG-------EILFERQSIKK--DLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 417 CPNG-----GDHIMVRGRNYHVYGYLKNFLFPKE---------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTN 482
Cdd:PRK13540 77 CFVGhrsgiNPYLTLRENCLYDIHFSPGAVGITElcrlfslehLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1196666485 483 DLDIATINILEEYLLSFE---GAILIVSHDRYFIDK 515
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
116-225 |
4.54e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 116 ELLHRqdelVKFIESKDgwnienkierILDSFglrEYEnrlvnsLSGGEIRRVALGALILKKPDVLLLDEPTNHLD---- 191
Cdd:PRK15093 138 ELLHR----VGIKDHKD----------AMRSF---PYE------LTEGECQKVMIAIALANQPRLLIADEPTNAMEpttq 194
|
90 100 110
....*....|....*....|....*....|....
gi 1196666485 192 VYMVRFLEELLLASNQTIVFISHDRYFIDRLATR 225
Cdd:PRK15093 195 AQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-193 |
4.57e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.62 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIemlaqSPKFNDNL--SVKDALNYELkeif 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISF-----SSQFSWIMpgTIKENIIFGV---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 96 dARDE--YEKVLAQISNEHDnpellhrqdeLVKFIEskdgwnienKIERILDSFGLreyenrlvnSLSGGEIRRVALGAL 173
Cdd:cd03291 123 -SYDEyrYKSVVKACQLEED----------ITKFPE---------KDNTVLGEGGI---------TLSGGQRARISLARA 173
|
170 180
....*....|....*....|
gi 1196666485 174 ILKKPDVLLLDEPTNHLDVY 193
Cdd:cd03291 174 VYKDADLYLLDSPFGYLDVF 193
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
159-222 |
5.99e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 5.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 159 SLSGGE------IRRVALGALILKKPDVLLLDEPTNHLD-----VYMVRFLEELLLASNQTIVFISHDRYFIDRL 222
Cdd:cd03240 115 RCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-396 |
6.22e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 6.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGEL---EADSGVINRGEIKI 396
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTL 68
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-224 |
6.44e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.86 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 4 IDLIEVSKKF-GDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEID-------SGRVIRQnsiSI 68
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLmgyypltEGEIRLDgrplsslSHSVLRQ---GV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 69 EMLAQSP-----KFNDNLSvkdaLNYELKEifdarDEYEKVLAQIsnehdnpellhrqdELVKFIES-KDGwnienkIER 142
Cdd:PRK10790 418 AMVQQDPvvladTFLANVT----LGRDISE-----EQVWQALETV--------------QLAELARSlPDG------LYT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 143 ILDSFGlreyenrlvNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLASNQ--TIVFISHdryfid 220
Cdd:PRK10790 469 PLGEQG---------NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREhtTLVVIAH------ 533
|
....
gi 1196666485 221 RLAT 224
Cdd:PRK10790 534 RLST 537
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
328-389 |
6.46e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 6.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 328 RKKMLFECKNLSKTidnkvlFSDFNA------RVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI 389
Cdd:COG3845 1 MMPPALELRGITKR------FGGVVAnddvslTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEI 62
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
336-509 |
8.38e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.50 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVI-------------NRGEIKIGYFDQS 402
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 403 -----RKSISDD-KSLIELfcpngGDHIMVRGRNYHVYGYLKNFLFpkEFLDKPVG-VLSGGEKNRLALALLFTKEYDCL 475
Cdd:PRK10895 87 asifrRLSVYDNlMAVLQI-----RDDLSAEQREDRANELMEEFHI--EHLRDSMGqSLSGGERRRVEIARALAANPKFI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1196666485 476 ILDEPTNDLD-IATINI--LEEYLLSFEGAILIVSHD 509
Cdd:PRK10895 160 LLDEPFAGVDpISVIDIkrIIEHLRDSGLGVLITDHN 196
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-278 |
9.30e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 5 DLIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIemLAQSPKFNDNLSVK 84
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV--IAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 85 DALNYELKEIFDARDEYEKVLAQIsnehdnpellhrqdelVKFIEskdgwnienkierildsfgLREYENRLVNSLSGGE 164
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKI----------------IEFSE-------------------LGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 165 IRRVALGALILKKPDVLLLDEPTNHLD-VYMVRFLEEL--LLASNQTIVFISHDRYFIDRLATRSVEIEDGALRSFdGGY 241
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDqTFAQKCLDKIyeFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GEL 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 1196666485 242 ANYLTKKEEILRSLAKSHETLIKNLKSEEEWLRRGVK 278
Cdd:PRK13546 228 DDVLPKYEAFLNDFKKKSKAEQKEFRNKLDESRFVIK 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
336-485 |
1.09e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.83 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVL-FSDFNARVLQGERIGIVGRNGSGKSTMLKILLGeLEAdsgvINRGEIKIGyfdqsRKSISDdkslIE 414
Cdd:PRK11650 7 QAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LER----ITSGEIWIG-----GRVVNE----LE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 415 lfcPNGGDHIMVRgRNYHVY---------GY-LKNFLFPKE-----------------FLD-KPVGvLSGGEKNRLALAL 466
Cdd:PRK11650 73 ---PADRDIAMVF-QNYALYphmsvrenmAYgLKIRGMPKAeieervaeaarilelepLLDrKPRE-LSGGQRQRVAMGR 147
|
170
....*....|....*....
gi 1196666485 467 LFTKEYDCLILDEPTNDLD 485
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLD 166
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
138-226 |
1.15e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 138 NKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV---------YMVRFLEELLLASNQT 208
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealllllEELRLLLLLKSEKNLT 118
|
90
....*....|....*...
gi 1196666485 209 IVFISHDRYFIDRLATRS 226
Cdd:smart00382 119 VILTTNDEKDLGPALLRR 136
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-51 |
1.23e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 1.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRG 51
Cdd:NF040905 7 ITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
345-485 |
1.29e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 345 KVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVInRGEIKIGYFDQSRksisddkslielfcpnggdHI 424
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQA-------------------WI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 425 M---VRGrnyhvygylkNFLFPKE----FLDKPVGV------------------------LSGGEKNRLALALLFTKEYD 473
Cdd:PTZ00243 733 MnatVRG----------NILFFDEedaaRLADAVRVsqleadlaqlgggleteigekgvnLSGGQKARVSLARAVYANRD 802
|
170
....*....|..
gi 1196666485 474 CLILDEPTNDLD 485
Cdd:PTZ00243 803 VYLLDDPLSALD 814
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
332-492 |
1.82e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 332 LFECKNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILlgeleadSGVIN----RGEIKIGYFDQSRKSIS 407
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPhgtyEGEIIFEGEELQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 408 D-----------------DKSLIE-LFCpngGDHIMVRGRnyhvYGYLKNFLFPKEFLDK---------PVGVLSGGEKN 460
Cdd:PRK13549 78 DteragiaiihqelalvkELSVLEnIFL---GNEITPGGI----MDYDAMYLRAQKLLAQlkldinpatPVGNLGLGQQQ 150
|
170 180 190
....*....|....*....|....*....|..
gi 1196666485 461 RLALALLFTKEYDCLILDEPTNDLDIATINIL 492
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVL 182
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
139-191 |
1.95e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 139 KIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLD 191
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
358-530 |
2.14e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.42 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 358 GERIGIVGRNGSGKSTMLKIL--LGELEADSGVINRGEIKIGYFDQSRKSISDDKSLIELFCP--------NGGDHIM-- 425
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCInfLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRTRltmvfqhfNLWSHMTvl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 426 --VRGRNYHVYGYLKNFLFPK--EFLDKpVGV-----------LSGGEKNRLALALLFTKEYDCLILDEPTNDLDI---- 486
Cdd:PRK10619 111 enVMEAPIQVLGLSKQEARERavKYLAK-VGIderaqgkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvg 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1196666485 487 ATINILEEylLSFEG-AILIVSHDRYFIDKITNKLWAYENGKIEQ 530
Cdd:PRK10619 190 EVLRIMQQ--LAEEGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-61 |
2.35e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.38 E-value: 2.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 9 VSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVI 61
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
336-487 |
2.57e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.86 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 336 KNLSKTIDNKVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIK----------IGYFDQSRK- 404
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaergVGMVFQSYAl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 405 ----SISDDKSL-IELfcpNGGDHIMVRGRNYHVYGYLKnflfPKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLILDE 479
Cdd:PRK11000 87 yphlSVAENMSFgLKL---AGAKKEEINQRVNQVAEVLQ----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
....*...
gi 1196666485 480 PTNDLDIA 487
Cdd:PRK11000 160 PLSNLDAA 167
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
362-514 |
2.66e-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: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 362 GIVGRNGSGKSTmlkiLLGELEADSGVINRGEIKIGYFDQSRKSISDDKSLIELFcpnggdhimvrgrnyhvYGYLKnfl 441
Cdd:cd03238 25 VVTGVSGSGKST----LVNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVG-----------------LGYLT--- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196666485 442 fpkefLDKPVGVLSGGEKNRLALA--LLFTKEYDCLILDEPTNDLDIATINILEEY---LLSFEGAILIVSHDRYFID 514
Cdd:cd03238 81 -----LGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLDVLS 153
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-532 |
3.29e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.16 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 454 LSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYLLSFEG--AILIVSHDRYFIDKITNKLWAY------EN 525
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFfdgrlvEE 243
|
....*..
gi 1196666485 526 GKIEQIY 532
Cdd:PRK14271 244 GPTEQLF 250
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
441-481 |
3.59e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 3.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1196666485 441 LFPkeFLDKPVGVLSGGEKNRLAL--ALLftKEYDCLILDEPT 481
Cdd:NF033858 126 LAP--FADRPAGKLSGGMKQKLGLccALI--HDPDLLILDEPT 164
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
357-509 |
3.94e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.80 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 357 QGERIGIVGRNGSGKSTMLKILLGeleadsgvIN---RGEIKIGYFDQSRKSISDDKSLIELFCPNGGDHIMVRGRNYHV 433
Cdd:PRK13647 30 EGSKTALLGPNGAGKSTLLLHLNG--------IYlpqRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVFSSTVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 434 -YGYLKNFLFPKE----------------FLDKPVGVLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINILEEYL 496
Cdd:PRK13647 102 aFGPVNMGLDKDEverrveealkavrmwdFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL 181
|
170
....*....|....*.
gi 1196666485 497 --LSFEGAILIVS-HD 509
Cdd:PRK13647 182 drLHNQGKTVIVAtHD 197
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
571-608 |
4.99e-04 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 38.99 E-value: 4.99e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1196666485 571 KLTYKQNQILQNHPALIEALESRISELNHALSTPEIYQ 608
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYS 38
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
363-486 |
5.03e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 41.52 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 363 IVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSRKSIsdDKSLIELFCPNGgdhimvrgrnyhvygylkNFLF 442
Cdd:cd03239 27 IVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGI--NSASVEITFDKS------------------YFLV 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1196666485 443 PKEFLDKpvgVLSGGEKNRLALALLFT----KEYDCLILDEPTNDLDI 486
Cdd:cd03239 87 LQGKVEQ---ILSGGEKSLSALALIFAlqeiKPSPFYVLDEIDAALDP 131
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
331-485 |
7.24e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.04 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 331 MLFECKNLSKT------IDNKVLFsDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYFDQSR- 403
Cdd:PRK13649 1 MGINLQNVSYTyqagtpFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 404 -KSISDDKSLI------ELFCPNGGDHIMVRGRNYHVYG---------YLKNFLFPKEFLDKPVGVLSGGEKNRLALALL 467
Cdd:PRK13649 80 iKQIRKKVGLVfqfpesQLFEETVLKDVAFGPQNFGVSQeeaealareKLALVGISESLFEKNPFELSGGQMRRVAIAGI 159
|
170
....*....|....*...
gi 1196666485 468 FTKEYDCLILDEPTNDLD 485
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLD 177
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
454-528 |
8.38e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.61 E-value: 8.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 454 LSGGEKNRLALALLFTKEYDCLILDEPTNDLD-IATINILE--EYLLSFEG-AILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDvVAQARILDllESIVQKRAlGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-238 |
9.08e-04 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 41.33 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 18 ILNETNFNVNEKERIAIIGKNGGGKSTLMKIL-------RGECEIDsGRVIRQ-------NSISIemLAQSPK-FN---- 78
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlvelsSGSILID-GVDISKiglhdlrSRISI--IPQDPVlFSgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 79 DNLsvkDALN-YELKEIFDArdeyekvLAQISnehdnpellhrqdeLVKFIESKDGwnienKIERILDSFGlreyenrlv 157
Cdd:cd03244 96 SNL---DPFGeYSDEELWQA-------LERVG--------------LKEFVESLPG-----GLDTVVEEGG--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 158 NSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDVYMVRFLEELLLA--SNQTIVFISHdryfidRLAT-----RSVEIE 230
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH------RLDTiidsdRILVLD 211
|
....*...
gi 1196666485 231 DGALRSFD 238
Cdd:cd03244 212 KGRVVEFD 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
355-516 |
1.11e-03 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 41.58 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 355 VLQGERIGIVGRNGSGKSTMLKILLGeLEADSGVInRGEI---------------------KIGY-FdQS-------RKS 405
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILG-LLPPPGIT-SGEIlfdgedllklsekelrkirgrEIQMiF-QDpmtslnpVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 406 ISDdkSLIE-LFCPNGGDHIMVRGRnyhVYGYLK--NFLFPKEFLDK-PvGVLSGGEKNR--LALALLftkeydC----L 475
Cdd:COG0444 105 VGD--QIAEpLRIHGGLSKAEARER---AIELLErvGLPDPERRLDRyP-HELSGGMRQRvmIARALA------LepklL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1196666485 476 ILDEPTNDLDiATI--NILEeyLL-----SFEGAILIVSHD----RYFIDKI 516
Cdd:COG0444 173 IADEPTTALD-VTIqaQILN--LLkdlqrELGLAILFITHDlgvvAEIADRV 221
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
77-220 |
1.16e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 77 FNDNLSVKDALNYELKEIFDARDEYEKVLAQISNEHDNPELLHRQDELVKFIESKDGWNIENKIERILDSFGLREYENRL 156
Cdd:pfam13304 151 LSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGG 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 157 ---VNSLSGGEIRRVALGALIL---KKPDVLLLDEPTNHLDVYMVR-FLEELLLASNQT--IVFISHDRYFID 220
Cdd:pfam13304 231 elpAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRrLLELLKELSRNGaqLILTTHSPLLLD 303
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
330-405 |
1.52e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.93 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 330 KMLFECKNLSKTIDNKV-LFS----------DFNARvlQGERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGY 398
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgWFRrqtveavkplSFTLR--EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 79
|
....*..
gi 1196666485 399 FDQSRKS 405
Cdd:PRK15112 80 GDYSYRS 86
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
363-528 |
1.54e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.01 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 363 IVGRNGSGKSTMLKILLGELEADSGVINRGE---------I-------KIGY-FDQSRksisddkslieLFcPnggdHIM 425
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgIclppekrRIGYvFQDAR-----------LF-P----HYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 426 VRGrNYHvYGYLKnflFPKEFLDKPVGVL-------------SGGEKNRLAL--ALLfTKEyDCLILDEPTNDLDIATIN 490
Cdd:PRK11144 93 VRG-NLR-YGMAK---SMVAQFDKIVALLgieplldrypgslSGGEKQRVAIgrALL-TAP-ELLLMDEPLASLDLPRKR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196666485 491 ILEEYL--LS--FEGAILIVSHDRYFIDKITNKLWAYENGKI 528
Cdd:PRK11144 166 ELLPYLerLAreINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
157-252 |
2.64e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV---YMVRFLEELLLASNQTIVFISHDRYFIDRLATRSVEIEDGA 233
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVgakYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
90
....*....|....*....
gi 1196666485 234 LRsfdGGYANYLTKKEEIL 252
Cdd:TIGR02633 481 LK---GDFVNHALTQEQVL 496
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
359-399 |
2.96e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1196666485 359 ERIGIVGRNGSGKSTMLKILLGELEADSGVINRGEIKIGYF 399
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-192 |
2.98e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.98e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV 192
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
355-508 |
3.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.73 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 355 VLQGERIGIVGRNGSGKSTMLKILLGELEadsgvINRGEIKIGYFDQSRKSISDDKSLIEL------------------F 416
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVE-----LEKGRIMIDDCDVAKFGLTDLRRVLSIipqspvlfsgtvrfnidpF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 417 CPNGGDHIMVRGRNYHVYGYLKNFLFPkefLDKPVG----VLSGGEKNRLALALLFTKEYDCLILDEPTNDLDIATINIL 492
Cdd:PLN03232 1334 SEHNDADLWEALERAHIKDVIDRNPFG---LDAEVSeggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170
....*....|....*...
gi 1196666485 493 EEYLL-SFEG-AILIVSH 508
Cdd:PLN03232 1411 QRTIReEFKScTMLVIAH 1428
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
348-481 |
3.49e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 348 FSDFNA------RVLQGERIGIVGRNGSGKSTMLKILLGELEADSG-------VINRGEI----KIGYFDQSRksisddk 410
Cdd:NF033858 276 FGDFTAvdhvsfRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqPVDAGDIatrrRVGYMSQAF------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 411 SLIE-------------LFcpnggdHIMVRGRNYHVYGYLKNF-LfpKEFLDKPVGVLSGGEKNRLALALLFTKEYDCLI 476
Cdd:NF033858 349 SLYGeltvrqnlelharLF------HLPAAEIAARVAEMLERFdL--ADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
....*
gi 1196666485 477 LDEPT 481
Cdd:NF033858 421 LDEPT 425
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
157-192 |
3.51e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV 192
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-64 |
4.66e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 4.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196666485 6 LIEVSKKFGDKIILNETNFNVNEKERIAIIGKNGGGKSTLMKILRGECEIDSGRVIRQN 64
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-197 |
4.97e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 33 AIIGKNGGGKSTLMKILRGECEIDSGRVIRQNSISIEMLAQSPKFN-DNLSVKDALNYELKEIFDARDEYEKVLAQISNE 111
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLlNGIDPKEPIEFEISEFLEDGVRYRYGLDLERED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 112 HDNPELLHRQDELVKFIESKDGW-NIENKIERILDSFGLREYENRLVNSLSGGEIRRVALGALILKKPDVLLLDEPTNHL 190
Cdd:pfam13304 83 VEEKLSSKPTLLEKRLLLREDSEeREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLL 162
|
....*..
gi 1196666485 191 DVYMVRF 197
Cdd:pfam13304 163 LEDWAVL 169
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
447-513 |
5.92e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196666485 447 LDKPVGVLSGGEKNRLALA--LLFTKEYDCL-ILDEPTNDLDIATINILEEYLLS--FEG-AILIVSHDRYFI 513
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAyeLLAPSKKPTLyVLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNMHVV 875
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
160-210 |
6.52e-03 |
|
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: 38.38 E-value: 6.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1196666485 160 LSGGEIRRVALGALILKKPDVLLLDEPTNHLD----VYMVRFLEElLLASNQTIV 210
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDsqaaYNIVRFLKK-LADSGQAIL 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
139-187 |
6.67e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 6.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1196666485 139 KIERILDSFGLREYENRLVNSLSGGEIRRVAL-GALIlKKPDVLLLDEPT 187
Cdd:NF033858 116 RIDELLRATGLAPFADRPAGKLSGGMKQKLGLcCALI-HDPDLLILDEPT 164
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
308-572 |
8.36e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 308 VKLELERASKSFNGGGLNQNRKKMLFECKNLSKTIdnkVLFSDFNARVLQGERIGIVGRNGSGKSTMLKILLGELEADSG 387
Cdd:PRK13546 3 VSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 388 VINR-GEIKIGYFDQSRKSISDDKSLIELFCPNGGdhiMVRGRNYHVYGYLKNFLFPKEFLDKPVGVLSGGEKNRLALAL 466
Cdd:PRK13546 80 KVDRnGEVSVIAISAGLSGQLTGIENIEFKMLCMG---FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196666485 467 LFTKEYDCLILDEPTNDLDIATINILEEYLLSFEGA---ILIVSHDRYFIDKITNKLWAYENGKIEqiymeysEYLDIEE 543
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQFCTKIAWIEGGKLK-------DYGELDD 229
|
250 260
....*....|....*....|....*....
gi 1196666485 544 ELNQLSDIESELGQsiETKEKQKTSKVKL 572
Cdd:PRK13546 230 VLPKYEAFLNDFKK--KSKAEQKEFRNKL 256
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
157-192 |
8.85e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.14 E-value: 8.85e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1196666485 157 VNSLSGGEIRRVALGALILKKPDVLLLDEPTNHLDV 192
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-375 |
9.74e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 9.74e-03
|
| |
