|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-535 |
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: 727.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 6 VNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 86 EMLTVFTHLQQMETKLRRLEQEMgkeenfsneATYERLLADYDQLQLNYKDQGGYQYEADIRSILSGLGFPVETHQTTIS 165
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKL---------AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFV 245
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 246 GNYSKYLDLKSALYEQEMKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELLTRPLgDSKSASFHFDIEKQ 325
Cdd:COG0488 232 GNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPR-RDKTVEIRFPPPER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 326 SGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQANL 405
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 TSSKRVLNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEI 485
Cdd:COG0488 391 DPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446524801 486 LENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEK 535
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-536 |
3.14e-119 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 364.98 E-value: 3.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWDemlTVFt 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLD---TVI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 93 hlqqM-ETKLRRLEQEmgKEENFSN-EATYErllaDY---DQLQLNYKDQGGYQYEADIRSILSGLGFPVETHQTTISTL 167
Cdd:PRK15064 87 ----MgHTELWEVKQE--RDRIYALpEMSEE----DGmkvADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGN 247
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 248 YSKYLDLKSALYEQEMKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELltrplGDSKSAS-----FHFDI 322
Cdd:PRK15064 237 YDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKL-----EEVKPSSrqnpfIRFEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 323 EKQSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQ 402
Cdd:PRK15064 312 DKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 403 ANLTSSKRVLNELWDEY--PLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK15064 392 AYDFENDLTLFDWMSQWrqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 481 NSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEKK 536
Cdd:PRK15064 472 ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-639 |
1.47e-113 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 353.87 E-value: 1.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWD----------EMLTVFTHLqqmetkLRRLEQEMGkeenfsneatyERLLADYDQLQLNYKDQGGYQYEADIRSIL 150
Cdd:PRK11147 81 GTVYDfvaegieeqaEYLKRYHDI------SHLVETDPS-----------EKNLNELAKLQEQLDHHNLWQLENRINEVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFPVEThqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLV 230
Cdd:PRK11147 144 AQLGLDPDA---ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 231 TQVYEISNKESRRFVGNYSKYLDLKsalyeQEMKRYEKQQDE-----IAKLEDFVQKNIaRASTTK-----RA-----QS 295
Cdd:PRK11147 221 TRIVDLDRGKLVSYPGNYDQYLLEK-----EEALRVEELQNAefdrkLAQEEVWIRQGI-KARRTRnegrvRAlkalrRE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 296 RRKQLDRMelltrplgdsKSASFHFDIEKQSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKS 375
Cdd:PRK11147 295 RSERREVM----------GTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 376 IVNKLPLLNGDVSFGSNVSVGYYDQEQANLTSSKRVLNELWDEyplqpEKEI------RTILG---NFLFTGDDVLKPVS 446
Cdd:PRK11147 365 MLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEG-----KQEVmvngrpRHVLGylqDFLFHPKRAMTPVK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFI-NRVTTTVVELSTEGAQEY 525
Cdd:PRK11147 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 526 LGDY-DYYVEKKNEMIERAELEQQESDVPVQKVV----AQEKLNYLEEKErkqlerqrtrkIEELEQSIVELEEEIATLE 600
Cdd:PRK11147 520 VGGYhDARQQQAQYLALKQPAVKKKEEAAAPKAEtvkrSSKKLSYKLQRE-----------LEQLPQLLEDLEAEIEALQ 588
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 446524801 601 DQLCLPEIYA-DYEKASEITTKKQTLQEQLETCMAEWEEL 639
Cdd:PRK11147 589 AQVADADFFSqPHEQTQKVLADLADAEQELEVAFERWEEL 628
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-536 |
1.19e-108 |
|
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: 338.45 E-value: 1.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDemlTVFTHLQQMETKLRRLEQEMgkeENFSNE-ATYERLLADYDQLQLNYKDQGGYQYEADIRSILSGLGFPVEt 159
Cdd:TIGR03719 83 KTVRE---NVEEGVAEIKDALDRFNEIS---AKYAEPdADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 160 hQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNK 239
Cdd:TIGR03719 156 -DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 240 ESRRFVGNYSKYLDLKSALYEQEMKRYEKQQDEIAKLEDFVQKNI-ARASTTKRAQSRRKQLDRMELLTRPlgdsKSASF 318
Cdd:TIGR03719 235 RGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPkGRQAKSKARLARYEELLSQEFQKRN----ETAEI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 319 HFDIEKQSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYY 398
Cdd:TIGR03719 311 YIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQEQANLTSSKRVLNELWD--EYPLQPEKEI--RTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:TIGR03719 391 DQSRDALDPNKTVWEEISGglDIIKLGKREIpsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 475 TNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVveLSTEGAQE---YLGDYDYYVEKK 536
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFEGDSHvewFEGNFSEYEEDK 533
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-638 |
1.91e-106 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 335.60 E-value: 1.91e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNT-GLETSltiwdemltVFT 92
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpALPQP---------ALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 93 HLQQMETKLRRLEQEMGKEENFSNEATYERLLADYDQLQlnykdqgGYQYEADIRSILSGLGFPVETHQTTISTLSGGQK 172
Cdd:PRK10636 83 YVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAID-------AWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 173 TRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGNYSKYL 252
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 253 DLKSALYEQEMKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELLTRPLGDSksaSFHFDIEKQSG--NDV 330
Cdd:PRK10636 236 VQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDN---PFHFSFRAPESlpNPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQAN-LTSSK 409
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLRADE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENA 489
Cdd:PRK10636 393 SPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 490 LIDYPGTLLFVSHDRYFInRVTTTVVELSTEGAQE-YLGDYDYYvekKNEMIERAELEQQESDVPVQKVV--AQEKlnyl 566
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEpFDGDLEDY---QQWLSDVQKQENQTDEAPKENNAnsAQAR---- 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 567 EEKERKQLE-RQRT----RKIEELEQSIVELEEEIATLEDQLCLPEIYADYEKA--SEITTKKQTLQEQLETCMAEWEE 638
Cdd:PRK10636 545 KDQKRREAElRTQTqplrKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAelTACLQQQASAKSGLEECEMAWLE 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-512 |
9.08e-101 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 318.22 E-value: 9.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 7 NALSKLYGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWD 85
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 86 EmltVFTHLQQMETKLRRLEQEMgkeENFSNE-ATYERLLADYDQLQLNYKDQGGYQYEADIRSILSGLGFPVEthQTTI 164
Cdd:PRK11819 90 N---VEEGVAEVKAALDRFNEIY---AAYAEPdADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPW--DAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 165 STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRF 244
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 245 VGNYSKYLDLKSALYEQEMKRYEKQQDEIAKLEDFVQKNiARASTTK-----------RAQSRRKQLDRMELLTrPLGDs 313
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQS-PKARQAKskarlaryeelLSEEYQKRNETNEIFI-PPGP- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 314 ksasfhfdiekQSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNV 393
Cdd:PRK11819 319 -----------RLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 394 SVGYYDQEQANLTSSKRVLNELWD--EYPLQPEKEI--RTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK11819 388 KLAYVDQSRDALDPNKTVWEEISGglDIIKVGNREIpsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446524801 470 ILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTT 512
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIAT 510
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-508 |
9.86e-76 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 256.33 E-value: 9.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 31 RIALVGRNGAGKSTLLKIIAGElSHDGgeiiKPKDVSIGYLAQ--------------NTGLETSLTIWDEmltVFTHLQQ 96
Cdd:PLN03073 205 HYGLVGRNGTGKTTFLRYMAMH-AIDG----IPKNCQILHVEQevvgddttalqcvlNTDIERTQLLEEE---AQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 97 METKLRRLEQEMGKEEN--FSNEATYERLLADYDQLQLnykdQGGYQYEADIRSILSGLGFPVETHQTTISTLSGGQKTR 174
Cdd:PLN03073 277 RELEFETETGKGKGANKdgVDKDAVSQRLEEIYKRLEL----IDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 175 LALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGNYSKYLDL 254
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERT 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 255 KSALYEQEMKRYEKQQDEIAKLEDFVQK---NIARASTTkraQSRRKQLDRMELLTRPLGDSkSASFHFDI-EKQSGNDV 330
Cdd:PLN03073 433 REEQLKNQQKAFESNERSRSHMQAFIDKfryNAKRASLV---QSRIKALDRLGHVDAVVNDP-DYKFEFPTpDDRPGPPI 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPII-EHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQAN-LTSS 408
Cdd:PLN03073 509 ISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDgLDLS 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILEN 488
Cdd:PLN03073 589 SNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
490 500
....*....|....*....|
gi 446524801 489 ALIDYPGTLLFVSHDRYFIN 508
Cdd:PLN03073 669 GLVLFQGGVLMVSHDEHLIS 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-253 |
8.67e-73 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 243.43 E-value: 8.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQ-NTGLETS 80
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQhQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDEMltvfthlqqmetklRRLEQEMGkeenfsneatyerlladydqlqlnykdqggyqyEADIRSILSGLGFPVETH 160
Cdd:COG0488 394 KTVLDEL--------------RDGAPGGT---------------------------------EQEVRGYLGRFLFSGDDA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKE 240
Cdd:COG0488 427 FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG 506
|
250
....*....|...
gi 446524801 241 SRRFVGNYSKYLD 253
Cdd:COG0488 507 VREYPGGYDDYLE 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-586 |
1.08e-62 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 216.47 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 333 VNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQaNLTSSKRVL 412
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP-PLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 413 N-------ELW-------------DEYPLQPEK------------------EIRTILGNFLFTGDDVLKPVSSLSGGQKA 454
Cdd:COG0488 80 DtvldgdaELRaleaeleeleaklAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVE 534
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 535 KKNEMIERAELEQQESdvpvQKVVAQEK--LNYLEEKERKQleRQ---RTRKIEELE 586
Cdd:COG0488 240 QRAERLEQEAAAYAKQ----QKKIAKEEefIRRFRAKARKA--KQaqsRIKALEKLE 290
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
331-518 |
7.80e-57 |
|
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: 188.43 E-value: 7.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQeqanltsskr 410
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 vlnelwdeyplqpekeirtilgnflftgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180
....*....|....*....|....*...
gi 446524801 491 IDYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:cd03221 114 KEYPGTVILVSHDRYFLDQVATKIIELE 141
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-240 |
1.02e-53 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 180.34 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQntgletslti 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 wdemltvfthlqqmetklrrleqemgkeenfsneatyerlladydqlqlnykdqggyqyeadirsilsglgfpvethqtt 163
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 164 istLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKE 240
Cdd:cd03221 71 ---LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-252 |
7.34e-39 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 150.43 E-value: 7.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLEtslti 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYD----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMLTVFTHLQQMetklrrleqemgkeenfsneatyeRLLADYDQLqlnykdqggyqyeadIRSILSGLGFPVETHQTT 163
Cdd:PRK15064 395 FENDLTLFDWMSQW------------------------RQEGDDEQA---------------VRGTLGRLLFSQDDIKKS 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRR 243
Cdd:PRK15064 436 VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
....*....
gi 446524801 244 FVGNYSKYL 252
Cdd:PRK15064 516 FSGTYEEYL 524
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-510 |
3.80e-34 |
|
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: 136.57 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG---GEI-IKPKDV---------- 66
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVlLDGRDLlelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 67 SIGYLAQNTglETSLTiwdeMLTVfthLQQMETKLRRLeqemgkeeNFSNEATYERLLADYDQLQLnykDQGGYQYeadi 146
Cdd:COG1123 84 RIGMVFQDP--MTQLN----PVTV---GDQIAEALENL--------GLSRAEARARVLELLEAVGL---ERRLDRY---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 147 rsilsglgfpveTHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:COG1123 140 ------------PHQ-----LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 223 ryfldklvtqvyeisnkesrrfvgnyskyLDLKSALyeqemkryekqQDEIAKLEDFVqknIARASTTKRAQSRRKQLDR 302
Cdd:COG1123 203 -----------------------------LGVVAEI-----------ADRVVVMDDGR---IVEDGPPEEILAAPQALAA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 303 MELLTRPLGDSKSASfhfdiekQSGNDVLQVNDATIGY-----DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIV 377
Cdd:COG1123 240 VPRLGAARGRAAPAA-------AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 378 NKLPLLNGDVSF-GSNVS-------------VGY-----YDQeqanLTSSKRVLNELwdEYPLQ-----PEKEIRTILGN 433
Cdd:COG1123 313 GLLRPTSGSILFdGKDLTklsrrslrelrrrVQMvfqdpYSS----LNPRMTVGDII--AEPLRlhgllSRAERRERVAE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 434 FLftgDDV-LKP------VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILeNALIDY---PG-TLLFVS 501
Cdd:COG1123 387 LL---ERVgLPPdladryPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVsVQAQIL-NLLRDLqreLGlTYLFIS 462
|
570
....*....|...
gi 446524801 502 HD----RYFINRV 510
Cdd:COG1123 463 HDlavvRYIADRV 475
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-238 |
1.53e-33 |
|
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: 127.21 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS----IGYLA 72
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepIRDAREDyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLETSLTIWdEMLTVFTHLQQMETKLRRLEQEMgkeenfsneatyERL-LADYdqlqlnykdqggyqyeADIRsils 151
Cdd:COG4133 82 HADGLKPELTVR-ENLRFWAALYGLRADREAIDEAL------------EAVgLAGL----------------ADLP---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 glgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP---GAILIVSHDRYFLDK 228
Cdd:COG4133 129 ------------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA 196
|
250
....*....|
gi 446524801 229 lvTQVYEISN 238
Cdd:COG4133 197 --ARVLDLGD 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-240 |
5.47e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 5.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS----------IGYLA 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYlDGKPLSampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLetsltiWDEmlTVfthlqqmetklrrleqemgkEENFSNEATYERLLADYDQLqlnykdqggyqyeadiRSILSG 152
Cdd:COG4619 81 QEPAL------WGG--TV--------------------RDNLPFPFQLRERKFDRERA----------------LELLER 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 153 LGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVSHDRYFLDK 228
Cdd:COG4619 117 LGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIER 196
|
250
....*....|..
gi 446524801 229 LVTQVYEISNKE 240
Cdd:COG4619 197 VADRVLTLEAGR 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-304 |
3.50e-31 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 129.13 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTgLEtslt 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ-LE---- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 iwdemltvftHLQQMETKLRRLEQEMGKEenfsneatYERLLADYdqlqlnykdqggyqyeadirsiLSGLGFPVETHQT 162
Cdd:PRK10636 387 ----------FLRADESPLQHLARLAPQE--------LEQKLRDY----------------------LGGFGFQGDKVTE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESR 242
Cdd:PRK10636 427 ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 243 RFVGNYSKYLDLKSALYEQEMKRYEKQQDEIAKLEDfVQKNIARASTTKRAQSR--RKQLDRME 304
Cdd:PRK10636 507 PFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSAQ-ARKDQKRREAELRTQTQplRKEIARLE 569
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-240 |
5.98e-31 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 121.12 E-value: 5.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI--------IKPKDV--SIGYLA 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREArrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLETSLTIWdEMLTVFTHLQQMEtklrrleqemgkeenfsneatyerlladydqlqlnykdqgGYQYEADIRSILSG 152
Cdd:COG4555 81 DERGLYDRLTVR-ENIRYFAELYGLF----------------------------------------DEELKKRIEELIEL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 153 LGFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRYFLDKL 229
Cdd:COG4555 120 LGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEAL 198
|
250
....*....|.
gi 446524801 230 VTQVYEISNKE 240
Cdd:COG4555 199 CDRVVILHKGK 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
331-517 |
7.52e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.92 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYYD 399
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLSampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QE--------QANLTSSKRVLNELWDEyplqpeKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:COG4619 81 QEpalwggtvRDNLPFPFQLRERKFDR------ERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 472 DEPTNHLDLNSKEILENALIDYP----GTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTL 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
330-517 |
1.73e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS-----VGYYDQeqa 403
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 NLTSSKR--------VLNELWDEYPL--QPEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARLALAKLMM 463
Cdd:COG1121 83 RAEVDWDfpitvrdvVLMGRYGRRGLfrRPSRADREAV-------DEALervgledladRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 464 QKSNLLILDEPTNHLDLNSKEILEN---ALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
332-510 |
5.73e-30 |
|
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: 117.63 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS-----VGYYDQ-EQAN 404
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFGKPLEkerkrIGYVPQrRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 405 LTSSKRVLnEL----------WDEYPLQPEKEI------RTILGNFLftgddvLKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:cd03235 81 RDFPISVR-DVvlmglyghkgLFRRLSKADKAKvdealeRVGLSELA------DRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 469 LILDEPTNHLDLNSKEI---LENALIDYPGTLLFVSHD----RYFINRV 510
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHDlglvLEYFDRV 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
5.94e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 118.24 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SIGYLAQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIWdEMLTVFTHLQQMETKLRRleqemgkeenfsneATYERLLadyDQLQLNYKdqggyqyeADIRsilsgl 153
Cdd:COG1131 81 EPALYPDLTVR-ENLRFFARLYGLPRKEAR--------------ERIDELL---ELFGLTDA--------ADRK------ 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 154 gfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSHD 222
Cdd:COG1131 129 ----------VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
234-318 |
3.08e-29 |
|
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: 110.74 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 234 YEISNKESRRFVGNYSKYLDLKSALYEQEMKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELLTRPLGDS 313
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 446524801 314 KSASF 318
Cdd:pfam12848 81 PKLRF 85
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
344-561 |
1.34e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 120.61 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 344 PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI--VNKLplLNGDVSFGSNVSVGYYDQEqANLTSSKRV---------- 411
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagVDKE--FEGEARPAPGIKVGYLPQE-PQLDPEKTVrenveegvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 -------LNELWDEYPLQPEK---------EIRTI--------LGNFLFTGDDVLK------PVSSLSGGQKARLALAKL 461
Cdd:PRK11819 98 vkaaldrFNEIYAAYAEPDADfdalaaeqgELQEIidaadawdLDSQLEIAMDALRcppwdaKVTKLSGGERRRVALCRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 462 MMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEKKNemiE 541
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKA---K 254
|
250 260
....*....|....*....|
gi 446524801 542 RAELEQQEsDVPVQKVVAQE 561
Cdd:PRK11819 255 RLAQEEKQ-EAARQKALKRE 273
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-238 |
1.41e-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: 112.11 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SIGYLAQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkEPEEVkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLetsltiwDEMLTVFTHLQqmetklrrleqemgkeenfsneatyerlladydqlqlnykdqggyqyeadirsilsgl 153
Cdd:cd03230 81 EPSL-------YENLTVRENLK---------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 154 gfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRYFLDKLV 230
Cdd:cd03230 96 -------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLC 162
|
....*...
gi 446524801 231 TQVYEISN 238
Cdd:cd03230 163 DRVAILNN 170
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
4.10e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQN 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETS--LTIWDemlTVFTHLQQMETKLRRLeqemGKEEnfsNEATYERLladyDQLQL-NYKDQggyqyeadirsils 151
Cdd:COG1121 84 AEVDWDfpITVRD---VVLMGRYGRRGLFRRP----SRAD---REAVDEAL----ERVGLeDLADR-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 glgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSHDRYFLDK 228
Cdd:COG1121 136 -----------PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVRE 204
|
....*
gi 446524801 229 LVTQV 233
Cdd:COG1121 205 YFDRV 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-230 |
4.66e-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: 113.21 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlasLSRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIWDemlTVfthlqqmetklrrleqEMGKeenfsneATYERLLAdydqlQLNYKDqggyqyEADIRSILS 151
Cdd:COG1120 81 PQEPPAPFGLTVRE---LV----------------ALGR-------YPHLGLFG-----RPSAED------REAVEEALE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 GLGFpveTH--QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD--- 222
Cdd:COG1120 124 RTGL---EHlaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDlnl 200
|
250
....*....|
gi 446524801 223 --RYFlDKLV 230
Cdd:COG1120 201 aaRYA-DRLV 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-251 |
2.61e-27 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 116.76 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 35 VGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQN-TGLETSLTIWdemltvfthlqqmetklrrleqemgkeEN 113
Cdd:PRK11819 356 IGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSrDALDPNKTVW---------------------------EE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 114 FSNEAtyerlladyDQLQLNykdqggyQYEADIRSILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEP 193
Cdd:PRK11819 409 ISGGL---------DIIKVG-------NREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 194 TNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQV--YEiSNKESRRFVGNYSKY 251
Cdd:PRK11819 473 TNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHIlaFE-GDSQVEWFEGNFQEY 531
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
330-529 |
2.73e-27 |
|
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: 109.49 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVsvgyydqeQANLTSS 408
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPI--------RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNELWDEYPLQPEkeiRTILGNFLF---------TGDDVL-------------KPVSSLSGGQKARLALAKLMMQKS 466
Cdd:COG4133 74 RRRLAYLGHADGLKPE---LTVRENLRFwaalyglraDREAIDealeavglagladLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 467 NLLILDEPTNHLDLNSKEILENALIDYP---GTLLFVSHDryfinrvtttvvELSTEGAQEY-LGDY 529
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQ------------PLELAAARVLdLGDF 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
330-503 |
2.99e-27 |
|
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: 110.90 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYY 398
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQEQA---NLTsskrVLnelwdE------YPLQP------EKEIRTIlgnflftgDDVL----------KPVSSLSGGQK 453
Cdd:COG1120 81 PQEPPapfGLT----VR-----ElvalgrYPHLGlfgrpsAEDREAV--------EEALertglehladRPVDELSGGER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524801 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSK-EILE--NALIDYPG-TLLFVSHD 503
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQlEVLEllRRLARERGrTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
332-503 |
1.56e-26 |
|
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: 106.75 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyydqeqanltssKRV 411
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD------------------GKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 LNELwdeyplqPEKEIRTILGnFLFTGDDVL-------KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSK 483
Cdd:cd03214 63 LASL-------SPKELARKIA-YVPQALELLglahladRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIaHQI 134
|
170 180
....*....|....*....|...
gi 446524801 484 EILE--NALIDYPG-TLLFVSHD 503
Cdd:cd03214 135 ELLEllRRLARERGkTVVMVLHD 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-195 |
4.21e-26 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 104.27 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYLAQNTGLETSLTIWDEM 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlLDGQDLTdderkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 ltvfthlqqmetKLRRLEQEMGKEEnfsneatyerlladydqlqlnykdqggyqYEADIRSILSGLGFPVETHQT---TI 164
Cdd:pfam00005 81 ------------RLGLLLKGLSKRE-----------------------------KDARAEEALEKLGLGDLADRPvgeRP 119
|
170 180 190
....*....|....*....|....*....|.
gi 446524801 165 STLSGGQKTRLALGKLLLTKPDLLILDEPTN 195
Cdd:pfam00005 120 GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
332-517 |
6.05e-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: 104.25 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVsfgsnvsvgyydqeqanltsskRV 411
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------------LI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 LNELWDEYPLqpeKEIRTILGnFLFtgddvlkpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI 491
Cdd:cd00267 59 DGKDIAKLPL---EELRRRIG-YVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180
....*....|....*....|....*....
gi 446524801 492 DYPG---TLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd00267 125 ELAEegrTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-233 |
1.26e-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: 104.99 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigylaqntgletslTI 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------------------TF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WD-EMLTVFTHLQQMETKLRR--LEQEMGKEENFSNEATYerlladydqLQLNYKdqggyqyeaDIRSILSGLGFPVETH 160
Cdd:cd03268 60 DGkSYQKNIEALRRIGALIEApgFYPNLTARENLRLLARL---------LGIRKK---------RIDEVLDVVGLKDSAK 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 161 QtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP---GAILIVSHDRYFLDKLVTQV 233
Cdd:cd03268 122 K-KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRI 196
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-239 |
1.48e-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: 104.92 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 5 QVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----IGYLAQNTGLE 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEkerkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 TS--LTIWDEMLTVFTHLQQMETKLRRleqemgkeenfsneATYERLLADYDQLQL-NYKDQggyqyeadirsilsglgf 155
Cdd:cd03235 81 RDfpISVRDVVLMGLYGHKGLFRRLSK--------------ADKAKVDEALERVGLsELADR------------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 156 pvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQyLQGYPGAILIVSHDRYFLDKLVT 231
Cdd:cd03235 129 -------QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHDLGLVLEYFD 200
|
....*...
gi 446524801 232 QVYEISNK 239
Cdd:cd03235 201 RVLLLNRT 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-238 |
2.51e-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: 104.09 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 5 QVNALSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYL 71
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlVDGKDLTklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTglETSL---TIWDEMLTVFTHLQ----QMETKLRRLEQEMGKEEnfsneatyerlLADYDqlqlnykdqggyqyea 144
Cdd:cd03225 81 FQNP--DDQFfgpTVEEEVAFGLENLGlpeeEIEERVEEALELVGLEG-----------LRDRS---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 145 dirsilsglgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSH 221
Cdd:cd03225 132 -------------------PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTH 192
|
250
....*....|....*..
gi 446524801 222 DRYFLDKLVTQVYEISN 238
Cdd:cd03225 193 DLDLLLELADRVIVLED 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-223 |
1.07e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.61 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII----------KPKDVSIGYLAQ 73
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLetsltiwdemltvFTHLQQME------TKLRRLEQEMgkeenfsnEATYERLLadyDQLQlnykdqggyqyeadir 147
Cdd:COG1118 83 HYAL-------------FPHMTVAEniafglRVRPPSKAEI--------RARVEELL---ELVQ---------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 148 siLSGLG--FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI---ETL-TWLEQYLQGYPGAILIVSH 221
Cdd:COG1118 123 --LEGLAdrYP---SQ-----LSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELrRWLRRLHDELGGTTVFVTH 192
|
..
gi 446524801 222 DR 223
Cdd:COG1118 193 DQ 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-260 |
9.19e-24 |
|
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: 105.62 E-value: 9.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGY 70
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLRrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTgletsltiwdemltvftHLqqMETKLR---RLeqemGKEEnfsneATYERLLADYDQLQLnykdqggyqyEADIR 147
Cdd:COG4987 414 VPQRP-----------------HL--FDTTLRenlRL----ARPD-----ATDEELWAALERVGL----------GDWLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 148 SILSGLGFPV-ETHqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGypGAILIVSHD 222
Cdd:COG4987 456 ALPDGLDTWLgEGG----RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeqalLADLLEALAG--RTVLLITHR 529
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446524801 223 RYFLDKlVTQVYEIsnkESRRFV--GNYSKYLDLKSALYE 260
Cdd:COG4987 530 LAGLER-MDRILVL---EDGRIVeqGTHEELLAQNGRYRQ 565
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
331-503 |
2.54e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 97.08 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVSvgyydqeqANLTSSK 409
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIK--------KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPLQPEkeirtilgnflFTGDDVLKpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENA 489
Cdd:cd03230 73 RRIGYLPEEPSLYEN-----------LTVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170
....*....|....*..
gi 446524801 490 LIDY---PGTLLFVSHD 503
Cdd:cd03230 138 LRELkkeGKTILLSSHI 154
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
332-518 |
6.50e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.15 E-value: 6.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYD--ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYY 398
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQEQANLTSSKRVLNELwdEYPL----QPEKEIRTILGNFL-FTGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03225 81 FQNPDDQFFGPTVEEEV--AFGLenlgLPEEEIEERVEEALeLVGLEGLrdRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 472 DEPTNHLDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
339-514 |
1.38e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 339 GYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQA-----NLTSSKRVLN 413
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpdslPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 414 ELWDEYPL--QPEKEIRTILGNFL--FTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILEN 488
Cdd:NF040873 81 GRWARRGLwrRLTRDDRAAVDDALerVGLADLAGrQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 446524801 489 ALIDYPG---TLLFVSHDRYFINRVTTTV 514
Cdd:NF040873 161 LLAEEHArgaTVVVVTHDLELVRRADPCV 189
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
331-502 |
1.57e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 94.76 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYD--ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLngdvsfgsnvsVGYYDQEQANLtss 408
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLK-------LL-----------LRLYDPTSGEI--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 krvlneLWDEYPLQ--PEKEIRTILG-----NFLFTGD--DVLkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03228 60 ------LIDGVDLRdlDLESLRKNIAyvpqdPFLFSGTirENI-----LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180
....*....|....*....|....*
gi 446524801 480 LNSKEILENALIDYPG--TLLFVSH 502
Cdd:cd03228 129 PETEALILEALRALAKgkTVIVIAH 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-251 |
1.73e-22 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 102.25 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQN--TGLETSLTIWDEMLTVF 91
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHhvDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 92 THLqqMETKLRRLEQEMGKEENFSNEATYerlladydqlqlnykdqggyqyeadirsilsglgfpvethqttisTLSGGQ 171
Cdd:PLN03073 600 PGV--PEQKLRAHLGSFGVTGNLALQPMY---------------------------------------------TLSGGQ 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 172 KTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGNYSKY 251
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
2.09e-22 |
|
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: 94.81 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 5 QVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYLAQ 73
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlasLSPKELArkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NtgletsltiwdemltvfthLQQMETklrrleqemgkeenfsneatyerlladydqlqLNYKDQGgyqyeadirsilsgl 153
Cdd:cd03214 81 A-------------------LELLGL--------------------------------AHLADRP--------------- 94
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 154 gfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:cd03214 95 ----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
331-515 |
4.27e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 100.61 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN--PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsNVSVGYYDQEQ-ANLTS 407
Cdd:COG4987 334 LELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDlRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 skrVLNE---LWDEyplqpekeirTILGNFLFTGDD--------VLKPV---------------------SSLSGGQKAR 455
Cdd:COG4987 413 ---VVPQrphLFDT----------TLRENLRLARPDatdeelwaALERVglgdwlaalpdgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLD-LNSKEILENALIDYPG-TLLFVSHDRYFINRVTTTVV 515
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGrTVLLITHRLAGLERMDRILV 541
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
346-476 |
4.94e-22 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 92.71 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFG-----------SNVSVGYYDQEqANLTSSKRVLNE 414
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 415 LWD----EYPLQPEKEIRTI-----LGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:pfam00005 80 LRLglllKGLSKREKDARAEealekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
330-515 |
6.98e-22 |
|
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: 94.92 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNGDVSFGSNV----SVGYYD 399
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPRearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QEQ---ANLTSSK--RVLNELWDEYPLQPEKEIRTILGNFLFtgDDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:COG4555 81 DERglyDRLTVREniRYFAELYGLFDEELKKRIEELIELLGL--EEFLdRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 474 PTNHLDLNSKEILEN---ALIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:COG4555 159 PTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-238 |
1.40e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 91.54 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 9 LSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSigylaqntgletsltiwdem 87
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlIDGKDIA-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 ltvfthlqqmETKLRRLEQEMGkeenfsneatyerlladydqlqlnykdqggyqyeadirsilsglgfpvethqtTISTL 167
Cdd:cd00267 65 ----------KLPLEELRRRIG-----------------------------------------------------YVPQL 81
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPgAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:cd00267 82 SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASrerlLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-223 |
1.82e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.97 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQN 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWDEMLTVFTHLQQMETKLRRLEQEMGKEENFSNEAtyerlladydqlqlnykdqggyqyeadirsilsglg 154
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL------------------------------------ 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 155 fpvethQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILI-VSHDR 223
Cdd:cd03259 125 ------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqreLGITTIyVTHDQ 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
300-515 |
3.13e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 98.37 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 300 LDRM-ELLTRPLgDSKSASFHFDIEKQSGNdvLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI 376
Cdd:COG2274 445 LERLdDILDLPP-EREEGRSKLSLPRLKGD--IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 377 VNKLPLLNGDVSF-GSNV----------SVGYYDQEQA--------NLTsskrvlneLWDEYPlqPEKEIRTILgnfLFT 437
Cdd:COG2274 522 LGLYEPTSGRILIdGIDLrqidpaslrrQIGVVLQDVFlfsgtireNIT--------LGDPDA--TDEEIIEAA---RLA 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 438 G--DDVLK-------PV----SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:COG2274 589 GlhDFIEAlpmgydtVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH 668
|
250
....*....|...
gi 446524801 503 DRYFINRVTTTVV 515
Cdd:COG2274 669 RLSTIRLADRIIV 681
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-233 |
3.55e-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: 91.93 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 11 KLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDV--SIGYLAQNTGLE-TSL 81
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpIKAKERrkSIGYVMQDVDYQlFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 TIWDEMLtvfthlqqmetklrrleqemgkeenFSNEATYErlladydqlqlnykdqggyqYEADIRSILSGLGF--PVET 159
Cdd:cd03226 88 SVREELL-------------------------LGLKELDA--------------------GNEQAETVLKDLDLyaLKER 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 160 HQTTistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD---IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQV 233
Cdd:cd03226 123 HPLS---LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-487 |
5.11e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQtKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDvsigy 70
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELR-PGEVhALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrSPRD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 lAQNTGL-----ETSLtiWDEmLTVfthlqqmetklrrleqemgkEEN--FSNEATyERLLADYDQLqlnykdqggyqyE 143
Cdd:COG1129 76 -AQAAGIaiihqELNL--VPN-LSV--------------------AENifLGREPR-RGGLIDWRAM------------R 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 144 ADIRSILSGLGFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----------IETLTwlEQylqgyp 213
Cdd:COG1129 119 RRARELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTereverlfriIRRLK--AQ------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 214 G-AILIVSHdryFLDklvtQVYEISnkesrrfvgnyskyldlksalyeqemkryekqqDEIAKLED--FVqkniarastt 290
Cdd:COG1129 190 GvAIIYISH---RLD----EVFEIA---------------------------------DRVTVLRDgrLV---------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 291 krAQSRRKQLDRMELLTRPLGDSKSASFHfDIEKQSGNDVLQVNDATIGydenPIIEHVTMRLTRGDSVALVGPNGIGKS 370
Cdd:COG1129 220 --GTGPVAELTEDELVRLMVGRELEDLFP-KRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRT 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 371 TLLKSIVNKLPLLNGDVSF-GSNVS-----------VGYY--D------------QEQANLTSSKRVLNELWdeypLQPE 424
Cdd:COG1129 293 ELARALFGADPADSGEIRLdGKPVRirsprdairagIAYVpeDrkgeglvldlsiRENITLASLDRLSRGGL----LDRR 368
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 425 KE------------IRTilgnflftgDDVLKPVSSLSGG--QKArlALAKLMMQKSNLLILDEPTNHLDLNSK-EILE 487
Cdd:COG1129 369 REralaeeyikrlrIKT---------PSPEQPVGNLSGGnqQKV--VLAKWLATDPKVLILDEPTRGIDVGAKaEIYR 435
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-240 |
6.82e-21 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 92.01 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS-----IGYL 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLRelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTglETSL---TIWDEMLTVFTHL----QQMETKLRRLEQEMGKEEnfsneatyerlLADydqlqlnykdqggyqyea 144
Cdd:COG1122 81 FQNP--DDQLfapTVEEDVAFGPENLglprEEIRERVEEALELVGLEH-----------LAD------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 145 diRSIlsglgfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSH 221
Cdd:COG1122 130 --RPP---------------HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTH 192
|
250
....*....|....*....
gi 446524801 222 DRYFLDKLVTQVYEISNKE 240
Cdd:COG1122 193 DLDLVAELADRVIVLDDGR 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-238 |
7.69e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 92.17 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGA----ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDV-----S 67
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpVTRRRRkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 IGYLAQNTglETSLtiwDEMLTVFTHLqqmetklrrleqemgkeenfsNEAtyerlladydqlqlnYKDQGGYQYEADIR 147
Cdd:COG1124 81 VQMVFQDP--YASL---HPRHTVDRIL---------------------AEP---------------LRIHGLPDREERIA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 148 SILSGLGFPVET-----HQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILI 218
Cdd:COG1124 120 ELLEQVGLPPSFldrypHQ-----LSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLF 194
|
250 260
....*....|....*....|
gi 446524801 219 VSHDRYFLDKLVTQVYEISN 238
Cdd:COG1124 195 VSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-222 |
1.16e-20 |
|
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: 91.03 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY----GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS---------- 67
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfDGKDLLklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 ---IGYLAQNTGleTSLtiwDEMLTVFTHLqqMETkLRRLEQEMGKEENfsneatYERLLADYDQLQLNykdqggyqyEA 144
Cdd:cd03257 81 rkeIQMVFQDPM--SSL---NPRMTIGEQI--AEP-LRIHGKLSKKEAR------KEAVLLLLVGVGLP---------EE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 145 DIRSilsglgFPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVS 220
Cdd:cd03257 138 VLNR------YP---HE-----LSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFIT 203
|
..
gi 446524801 221 HD 222
Cdd:cd03257 204 HD 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-222 |
1.16e-20 |
|
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: 96.44 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYLAQNTGL-ETS----L 81
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqIDPASLrrQIGVVLQDVFLfSGTirenI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 TIWDEMLTvfthLQQMETKLRRLEqemgkeenfsneatyerLLADYDQLQLnykdqgGYQyeadirSILSGLGfpvethq 161
Cdd:COG2274 570 TLGDPDAT----DEEIIEAARLAG-----------------LHDFIEALPM------GYD------TVVGEGG------- 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 162 ttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:COG2274 610 ---SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-222 |
2.36e-20 |
|
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: 90.05 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTK---DRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQNtglets 80
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 ltiwdemLTVFTHL---QQMETKLRRLEQemgKEENFSNEATYERLlaDYDQLQLNYKDQggyqyeadirsilsglgfpv 157
Cdd:cd03297 84 -------YALFPHLnvrENLAFGLKRKRN---REDRISVDELLDLL--GLDHLLNRYPAQ-------------------- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 158 ethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:cd03297 132 ---------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
297-503 |
2.43e-20 |
|
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: 94.73 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 297 RKQLDRMELLTRPLGDSKSASFHFDIEKQSGNDVLQVNDATIGYDENPII-EHVTMRLTRGDSVALVGPNGIGKSTLLKS 375
Cdd:TIGR02868 301 RAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 376 IVNKLPLLNGDVSFGSnVSVGYYDQ-----------EQANLTSSKrVLNELWDEYPLQPEKEIRTI-----LGNFLFTGD 439
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDG-VPVSSLDQdevrrrvsvcaQDAHLFDTT-VRENLRLARPDATDEELWAAlervgLADWLRALP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 440 DVLKPV-----SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILENALIDYPG-TLLFVSHD 503
Cdd:TIGR02868 459 DGLDTVlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
332-519 |
3.02e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 89.24 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENP-IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNV--------SVGYYDQE- 401
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKrVLNELW---DEYPLQPEKeIRTILGNF-LFTGDDVLkPVSsLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03226 81 DYQLFTDS-VREELLlglKELDAGNEQ-AETVLKDLdLYALKERH-PLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 478 LDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELST 519
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
345-586 |
3.46e-20 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 94.93 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI----VNKLP-----------LLNGDVS-----FGSNVSVGYYDQEQAN 404
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaIDGIPkncqilhveqeVVGDDTTalqcvLNTDIERTQLLEEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 405 LTSSKRVLN--------------------------------ELWDEYplQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQ 452
Cdd:PLN03073 272 LVAQQRELEfetetgkgkgankdgvdkdavsqrleeiykrlELIDAY--TAEARAASILAGLSFTPEMQVKATKTFSGGW 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 453 KARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYY 532
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTF 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 533 VEKKNEMI---ERAELEQQESDVPVQKVVaqEKLNYleEKERKQLERQRTRKIEELE 586
Cdd:PLN03073 430 ERTREEQLknqQKAFESNERSRSHMQAFI--DKFRY--NAKRASLVQSRIKALDRLG 482
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
328-502 |
5.70e-20 |
|
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: 89.76 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNGDV--SFGSNVSV---------- 395
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS-------LITGDLppTYGNDVRLfgerrggedv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 396 -------GYYDQE-QANLTSSKRVLN----------ELWDEYPLQPEKEIRTILGnfLFTGDDVL-KPVSSLSGGQKARL 456
Cdd:COG1119 74 welrkriGLVSPAlQLRFPRDETVLDvvlsgffdsiGLYREPTDEQRERARELLE--LLGLAHLAdRPFGTLSQGEQRRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLDLNSKE-ILE--NALIDYPG-TLLFVSH 502
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARElLLAllDKLAAEGApTLVLVTH 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
303-515 |
7.82e-20 |
|
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: 93.28 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 303 MELLTRPLGDSKSASfhfDIEKQSGNDVLQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP 381
Cdd:COG4988 312 FALLDAPEPAAPAGT---APLPAAGPPSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 382 LLNGDVSFGsNVSVGYYDQEQ--------------------ANLTSSK---------RVLNE--LWDEYPLQPEKeIRTI 430
Cdd:COG4988 389 PYSGSILIN-GVDLSDLDPASwrrqiawvpqnpylfagtirENLRLGRpdasdeeleAALEAagLDEFVAALPDG-LDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 431 LGNflfTGddvlkpvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFIN 508
Cdd:COG4988 467 LGE---GG-------RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLA 536
|
....*..
gi 446524801 509 RVTTTVV 515
Cdd:COG4988 537 QADRILV 543
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
8.40e-20 |
|
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: 93.28 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYL 71
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASWRrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLeTSLTIWDEMLtvfthlqqmetklrrleqeMGKEEnfsneATYERLLADYDQLQLnykdqggyqyEADIRSILS 151
Cdd:COG4988 417 PQNPYL-FAGTIRENLR-------------------LGRPD-----ASDEELEAALEAAGL----------DEFVAALPD 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 152 GLgfpvethQTTI----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYpgAILIVSHD 222
Cdd:COG4988 462 GL-------DTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGR--TVILITHR 531
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
331-518 |
1.44e-19 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 88.16 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyydqeqaNLTSSK 409
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-------------GKDITK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNEL--------------------WDE---YPLQ---PEKEIRTILgnflftgDDVL----------KPVSSLSGGQK 453
Cdd:COG1122 68 KNLRELrrkvglvfqnpddqlfaptvEEDvafGPENlglPREEIRERV-------EEALelvglehladRPPHELSGGQK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-194 |
1.76e-19 |
|
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: 87.49 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------IGYL 71
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIwdemltvfthlqqmetklrrleqemgkEENFsneatyerLLADYDQLQLNYKDQGGYQYEAdirsils 151
Cdd:cd03224 81 PEGRRIFPELTV---------------------------EENL--------LLGAYARRRAKRKARLERVYEL------- 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 152 glgFPV--ETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:cd03224 119 ---FPRlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-238 |
4.32e-19 |
|
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: 86.39 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------- 67
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDISklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 ---IGYLAQNTGLETSLTIwdemltvfthlqqmetklrrleqemgkEENFSneatyerlladydqLQLNYKDQGGYQYEA 144
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTA---------------------------LENVE--------------LPLLLAGVPKKERRE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 145 DIRSILSGLGFPvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVS 220
Cdd:cd03255 120 RAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVT 198
|
250
....*....|....*...
gi 446524801 221 HDRyFLDKLVTQVYEISN 238
Cdd:cd03255 199 HDP-ELAEYADRIIELRD 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-233 |
5.61e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.10 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYLAQNTGLeTSLTIWDEm 87
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqLDPADLRrnIGYVPQDVTL-FYGTLRDN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 LTVFTHLQQMETKLRRLEqemgkeenFSNEATYERLLADYDQLQLNykdQGGYQyeadirsilsglgfpvethqttistL 167
Cdd:cd03245 98 ITLGAPLADDERILRAAE--------LAGVTDFVNKHPNGLDLQIG---ERGRG-------------------------L 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHdRYFLDKLVTQV 233
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRI 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-222 |
6.65e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.50 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----IKPKDVS-------IGYL 71
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgVPVSSLDqdevrrrVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTgletsltiwdemltvftHLqqMETKLRrleqemgkeENF---SNEATYERLLADYDQLQLnykdqggyqyEADIRS 148
Cdd:TIGR02868 415 AQDA-----------------HL--FDTTVR---------ENLrlaRPDATDEELWAALERVGL----------ADWLRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 149 ILSGLGFPVETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET-LTWLEQYLQGYPG-AILIVSHD 222
Cdd:TIGR02868 457 LPDGLDTVLGEGG---ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAALSGrTVVLITHH 529
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
331-503 |
8.90e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 85.89 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS---------VGYYDQ 400
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVArdpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 401 EQA---NLTsSKRVLNELWDEYPLqPEKEIRTILGNFL-FTG-DDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:COG1131 81 EPAlypDLT-VRENLRFFARLYGL-PRKEARERIDELLeLFGlTDAAdRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 446524801 475 TNHLDLNSKEILENALIDYPG---TLLFVSHD 503
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-222 |
9.18e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSL--TIWDemlTV 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRD---LV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 91 FTHLQQMETKLRRLeqemGKEENFSNEATYERL-LADYDQLQLnykdqggyqyeadirsilsglgfpvethqttiSTLSG 169
Cdd:NF040873 79 AMGRWARRGLWRRL----TRDDRAAVDDALERVgLADLAGRQL--------------------------------GELSG 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 170 GQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSHD 222
Cdd:NF040873 123 GQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-230 |
1.19e-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: 83.78 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-------------IKPKDVSIGY 70
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLetsltiwdemltvFTHLqqmetklrrleqemgkeenfsneatyerlladydqlqlnykdqggyqyeadirSIL 150
Cdd:cd03229 81 VFQDFAL-------------FPHL-----------------------------------------------------TVL 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFPvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ------GYpgAILIVSHD-- 222
Cdd:cd03229 95 ENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaqlGI--TVVLVTHDld 162
|
250
....*....|
gi 446524801 223 --RYFLDKLV 230
Cdd:cd03229 163 eaARLADRVV 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-221 |
1.46e-18 |
|
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: 84.33 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------IGYLAQ 73
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAeqrdephenILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIWdEMLTVFTHLqqmetklrrleqeMGKEENFSNEATYERLLADYDQLQLNYkdqggyqyeadirsilsgl 153
Cdd:TIGR01189 81 LPGLKPELSAL-ENLHFWAAI-------------HGGAQRTIEDALAAVGLTGFEDLPAAQ------------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 154 gfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSH 221
Cdd:TIGR01189 128 -------------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-222 |
1.79e-18 |
|
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: 84.45 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQ 73
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIWDEMLTVFThLQQMETKLRRleqemgkeenfsneATYERLLADYDqlqlnykdqggyqyeadirsiLSGL 153
Cdd:cd03293 81 QDALLPWLTVLDNVALGLE-LQGVPKAEAR--------------ERAEELLELVG---------------------LSGF 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 154 G--FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:cd03293 125 EnaYP---HQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
2.13e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.14 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGY 70
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQntglETSLTIWdemLTVfthLQQMETKLRRleQEMGKEEnfsNEATYERLLAdydqlqlnykdqggyqyeadirsiL 150
Cdd:COG1116 85 VFQ----EPALLPW---LTV---LDNVALGLEL--RGVPKAE---RRERARELLE------------------------L 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLG-----FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET---L-TWLEQYLQGYPGAILIVSH 221
Cdd:COG1116 126 VGLAgfedaYP---HQ-----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerLqDELLRLWQETGKTVLFVTH 197
|
.
gi 446524801 222 D 222
Cdd:COG1116 198 D 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
331-515 |
2.17e-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: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVsvgyyDQEQANLTSSK 409
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDL-----TDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPLQPEKeirTILGNFLFtgddvlkpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILE-- 487
Cdd:cd03229 76 RRIGMVFQDFALFPHL---TVLENIAL----------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRal 142
|
170 180 190
....*....|....*....|....*....|
gi 446524801 488 -NALIDYPG-TLLFVSHDRYFINRVTTTVV 515
Cdd:cd03229 143 lKSLQAQLGiTVVLVTHDLDEAARLADRVV 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
331-503 |
2.59e-18 |
|
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: 84.48 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS-------------VG 396
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLiDGEDISglseaelyrlrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 397 YYDQeQANLTSSKRVLNELwdEYPLQ-----PEKEIRTI----LGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSN 467
Cdd:cd03261 81 MLFQ-SGALFDSLTVFENV--AFPLRehtrlSEEEIREIvlekLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 468 LLILDEPTNHLD-LNSKEILEnaLI-----DYPGTLLFVSHD 503
Cdd:cd03261 157 LLLYDEPTAGLDpIASGVIDD--LIrslkkELGLTSIMVTHD 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
3.28e-18 |
|
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: 83.71 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDV---------SIGYL 71
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSIrtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQntgletSLTIWDEmLTVFTHLQQMeTKLRRLEQEMGKEEnfsneatyerLLADYDQLQLN-YKDqggyqyeadirsil 150
Cdd:cd03263 81 PQ------FDALFDE-LTVREHLRFY-ARLKGLPKSEIKEE----------VELLLRVLGLTdKAN-------------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 151 sglgfpvethqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:cd03263 129 -----------KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
4.75e-18 |
|
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: 83.64 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------IGYL 71
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGEDITglppheiarlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIWDEMLTVfthlQQMETKLRRLEQEMGKEENFSNEATyERLLadyDQLQLnykdqggyqyeADIRSILS 151
Cdd:cd03219 81 FQIPRLFPELTVLENVMVA----AQARTGSGLLLARARREEREARERA-EELL---ERVGL-----------ADLADRPA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 152 GlgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT---NHLDIETLTWLEQYL--QGYpgAILIVSHD 222
Cdd:cd03219 142 G-------------ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELreRGI--TVLLVEHD 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-221 |
1.00e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 80.89 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYLAQNTGLeTSLT 82
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdLDLESLrkNIAYVPQDPFL-FSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWdemltvfthlqqmetklrrleqemgkeENFsneatyerlladydqlqlnykdqggyqyeadirsilsglgfpvethqt 162
Cdd:cd03228 92 IR---------------------------ENI------------------------------------------------ 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 163 tistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSH 221
Cdd:cd03228 97 ----LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-502 |
1.10e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 341 DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDV--------SFGSN---VSVGYYDQEqanltssk 409
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNelgDHVGYLPQD-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 rvlNELWDEyplqpekeirTILGNFLftgddvlkpvsslSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENA 489
Cdd:cd03246 85 ---DELFSG----------SIAENIL-------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170
....*....|....*.
gi 446524801 490 LIDYP---GTLLFVSH 502
Cdd:cd03246 139 IAALKaagATRIVIAH 154
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
331-490 |
1.56e-17 |
|
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: 81.25 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGS---NVSVGYYDQEQANLTS 407
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 SKRVLNELWDEYPLQpekEIRTILGNFLFTGDDVLK----------PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:TIGR01189 81 LPGLKPELSALENLH---FWAAIHGGAQRTIEDALAavgltgfedlPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|...
gi 446524801 478 LDLNSKEILENAL 490
Cdd:TIGR01189 158 LDKAGVALLAGLL 170
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
2.24e-17 |
|
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: 82.39 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS---------IGy 70
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfDGRDITglpphriarLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LA---QNTGLETSLTIWDEMLtVFTHLQQ---METKLRRLEQEMGKEENFSNEAtyERLLadyDQLQLnykdqggyqyeA 144
Cdd:COG0411 81 IArtfQNPRLFPELTVLENVL-VAAHARLgrgLLAALLRLPRARREEREARERA--EELL---ERVGL-----------A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 145 DIRSILSGlgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT---NHLDIETLTWLEQYLQGYPG-AILIVS 220
Cdd:COG0411 144 DRADEPAG-------------NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIE 210
|
..
gi 446524801 221 HD 222
Cdd:COG0411 211 HD 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-510 |
2.31e-17 |
|
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: 85.62 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG--ELSHDGGEIIKpkDVSI----GYLAQNTGL 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIY--HVALcekcGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 78 ETSLTIWDEMLTVFthlqqmETKLRRLEQEMGKEENFSNEATYERLLADYDQLQ-----LNYKDQGGYQYEADIRSILSG 152
Cdd:TIGR03269 79 GEPCPVCGGTLEPE------EVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 153 LGFPVETHQTT--ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETL----TWLEQYLQGYPGAILIVSHDRYFL 226
Cdd:TIGR03269 153 IEMVQLSHRIThiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 227 DKLVTQVYEISNKESRRfVGN----YSKYLDLKSALyeqEMKRYEKQQDEIAKLEDFvqkniarastTKRAQSrrkqLDR 302
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKE-EGTpdevVAVFMEGVSEV---EKECEVEVGEPIIKVRNV----------SKRYIS----VDR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 303 melltrplGDSKSasfhfdiekqsgndvlqvndatigydenpiIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPL 382
Cdd:TIGR03269 295 --------GVVKA------------------------------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 383 LNGDVsfgsNVSVGyydQEQANLTS--------SKRVLNELWDEYPLQPEkeiRTILGNF-----LFTGDD--------V 441
Cdd:TIGR03269 337 TSGEV----NVRVG---DEWVDMTKpgpdgrgrAKRYIGILHQEYDLYPH---RTVLDNLteaigLELPDElarmkaviT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 442 LKPV---------------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR03269 407 LKMVgfdeekaeeildkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSH 486
|
....*...
gi 446524801 503 DRYFINRV 510
Cdd:TIGR03269 487 DMDFVLDV 494
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
331-481 |
2.32e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQE--------- 401
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTS---SKRVL--------NELWDEYPLQPEKEIRTILGNflfTGDDVL--KPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK11231 83 QHHLTPegiTVRELvaygrspwLSLWGRLSAEDNARVNQAMEQ---TRINHLadRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170
....*....|...
gi 446524801 469 LILDEPTNHLDLN 481
Cdd:PRK11231 160 VLLDEPTTYLDIN 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
328-503 |
2.61e-17 |
|
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: 85.34 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP---LLNGDVSF-GSNV-------- 393
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLdGRDLlelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 394 --SVGYYDQEQANLTSSKRVLNELWD--EYPLQPEKEIRT-ILGNFLFTGDDVL--KPVSSLSGGQKARLALAKLMMQKS 466
Cdd:COG1123 82 grRIGMVFQDPMTQLNPVTVGDQIAEalENLGLSRAEARArVLELLEAVGLERRldRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 467 NLLILDEPTNHLD-LNSKEILE--NALIDYPG-TLLFVSHD 503
Cdd:COG1123 162 DLLIADEPTTALDvTTQAEILDllRELQRERGtTVLLITHD 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-222 |
2.74e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGY 70
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLAdwspaelarrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLETSLTIwdemltvfthlqqmetklrrlEQ--EMGKEENFSNEATYERLLADYdqLQlnykdqggyqyEADIrS 148
Cdd:PRK13548 81 LPQHSSLSFPFTV---------------------EEvvAMGRAPHGLSRAEDDALVAAA--LA-----------QVDL-A 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 149 ILSGLGFPvethqttisTLSGGQKTRLALGKLL--LTKPD----LLILDEPTNHLDI----ETLTWLEQYLQGYPGAILI 218
Cdd:PRK13548 126 HLAGRDYP---------QLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIV 196
|
....
gi 446524801 219 VSHD 222
Cdd:PRK13548 197 VLHD 200
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-514 |
2.85e-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: 81.00 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 339 GYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSvGYYDQEQA-------------- 403
Cdd:cd03255 13 GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIS-KLSEKELAafrrrhigfvfqsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 NLTSSKRVLNELwdEYPLQ----PEKEIRTILGNFLFT---GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:cd03255 92 NLLPDLTALENV--ELPLLlagvPKKERRERAEELLERvglGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 477 HLDL-NSKEILE--NALIDYPG-TLLFVSHDRYFINRVTTTV 514
Cdd:cd03255 170 NLDSeTGKEVMEllRELNKEAGtTIVVVTHDPELAEYADRII 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-231 |
2.90e-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: 85.42 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYL 71
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladADADSWrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLeTSLTIWDEMLtvfthlqqmetkLRRLEqemgkeenfsneatyerllADYDQLQLNYKDQGGYQYEADIRSils 151
Cdd:TIGR02857 402 PQHPFL-FAGTIAENIR------------LARPD-------------------ASDAEIREALERAGLDEFVAALPQ--- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 GLGFPVETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYpgAILIVSHDR---Y 224
Cdd:TIGR02857 447 GLDTPIGEGG---AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeaevLEALRALAQGR--TVLLVTHRLalaA 521
|
....*..
gi 446524801 225 FLDKLVT 231
Cdd:TIGR02857 522 LADRIVV 528
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
330-510 |
3.10e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 81.01 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDE----NPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS---------- 394
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLLklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 ---VGYYDQE-QANLTSSKRV---LNE-LWDEYPLQPEKEIRTILGNFLF---TGDDVLK--PvSSLSGGQKARLALAKL 461
Cdd:cd03257 81 rkeIQMVFQDpMSSLNPRMTIgeqIAEpLRIHGKLSKKEARKEAVLLLLVgvgLPEEVLNryP-HELSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 462 MMQKSNLLILDEPTNHLD-LNSKEILEnaLID-----YPGTLLFVSHD----RYFINRV 510
Cdd:cd03257 160 LALNPKLLIADEPTSALDvSVQAQILD--LLKklqeeLGLTLLFITHDlgvvAKIADRV 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-502 |
3.32e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 84.68 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQV-NALSKLYGAETILANiKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkdvsigylaqntgLET 79
Cdd:PRK10938 1 MSSLQIsQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-----------------RQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 80 SLT-IWdemLTVFTHLQQM-ETKLRRLEQEM--GKEENFSNEATyerlladyDQLQLNYKDQGGYQYEADIRSILSGLGF 155
Cdd:PRK10938 63 QFShIT---RLSFEQLQKLvSDEWQRNNTDMlsPGEDDTGRTTA--------EIIQDEVKDPARCEQLAQQFGITALLDR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 156 PvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGypgailiVSHDRYFLDKLVTQVYE 235
Cdd:PRK10938 132 R-------FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS-------LHQSGITLVLVLNRFDE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 236 ISNkesrrFVGNYSKYLDLksALYEQEMKRYEKQQDEIAKLedfvqkniarasttkrAQSrrKQLDRMELltrPLGDSKS 315
Cdd:PRK10938 198 IPD-----FVQFAGVLADC--TLAETGEREEILQQALVAQL----------------AHS--EQLEGVQL---PEPDEPS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 316 ASFHFDiekqSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIV--------NKLPLLN--- 384
Cdd:PRK10938 250 ARHALP----ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysNDLTLFGrrr 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 385 -------------GDVS------FGSNVSV------GYYDQ---EQAnLTSSKRVLNELWdeyplqpekeiRTILGNFLF 436
Cdd:PRK10938 326 gsgetiwdikkhiGYVSsslhldYRVSTSVrnvilsGFFDSigiYQA-VSDRQQKLAQQW-----------LDILGIDKR 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 437 TGDdvlKPVSSLSGGQKaRLAL-AKLMMQKSNLLILDEPTNHLD-LNSKEILE--NALIDYPGT-LLFVSH 502
Cdd:PRK10938 394 TAD---APFHSLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLDpLNRQLVRRfvDVLISEGETqLLFVSH 460
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
3.42e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigyLAQNTGLETSlti 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------LAGTAPLAEA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 wdemltvfthlqQMETKLrrleqeMGKEenfsneatyERLL---ADYDQLQLNYKdqGGYQYEAdiRSILSGLGFpVETH 160
Cdd:PRK11247 80 ------------REDTRL------MFQD---------ARLLpwkKVIDNVGLGLK--GQWRDAA--LQALAAVGL-ADRA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----------IETLtWLEqylQGYpgAILIVSHD 222
Cdd:PRK11247 128 NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdlIESL-WQQ---HGF--TVLLVTHD 193
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-233 |
3.52e-17 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 85.30 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDVS--IGYLAQNTGLetsltiwdem 87
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLlglyqptEGSVLLDGVDIrqIDPADLRrnIGYVPQDPRL---------- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 ltvFThlqqmeTKLRrleqemgkeENFsneaTYERLLADyDQLQLNYKDQGGYqyEADIRSILSGLGFPV-ETHQTtist 166
Cdd:TIGR03375 551 ---FY------GTLR---------DNI----ALGAPYAD-DEEILRAAELAGV--TEFVRRHPDGLDMQIgERGRS---- 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHDRYFLDkLVTQV 233
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSLLD-LVDRI 669
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
3.88e-17 |
|
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: 81.01 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-------------IG 69
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDISglseaelyrlrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 70 YLAQNTGLETSLTIWDE-MLTVFTHLQQMETKLRRLeqemgkeenfsneatyerlladydqlqlnykdqggyqyeadIRS 148
Cdd:cd03261 81 MLFQSGALFDSLTVFENvAFPLREHTRLSEEEIREI-----------------------------------------VLE 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 149 ILSGLGFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQY---LQGYPGA-ILIVSHD 222
Cdd:cd03261 120 KLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLtSIMVTHD 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-223 |
3.97e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.21 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQN 74
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrFHGTDVSrlhardrkVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWDEM---LTVFThlqqmetklRRleqemgkeENFSNEATYERLLADYDQLQLNYKdqggyqyeADirsils 151
Cdd:PRK10851 83 YALFRHMTVFDNIafgLTVLP---------RR--------ERPNAAAIKAKVTQLLEMVQLAHL--------AD------ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 152 glGFPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHDR 223
Cdd:PRK10851 132 --RYP--------AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
331-502 |
4.73e-17 |
|
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: 79.95 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSVGYYDQEQA------ 403
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIgaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 -----NLTSSKRVlnELWDEYPLQPEKEIRTILGNFLFTGDDVlKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:cd03268 81 pgfypNLTARENL--RLLARLLGIRKKRIDEVLDVVGLKDSAK-KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180
....*....|....*....|....*..
gi 446524801 479 D-LNSKEILE--NALIDYPGTLLFVSH 502
Cdd:cd03268 158 DpDGIKELREliLSLRDQGITVLISSH 184
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
5.77e-17 |
|
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: 78.62 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigylaqntgletsltI 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI----------------------L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDemltvfthlqqmetklrrleqemGKEENFSN--EAtyerlladydqlqlnyKDQGgyqyeadIRSIlsglgfpvetHQ 161
Cdd:cd03216 59 VD-----------------------GKEVSFASprDA----------------RRAG-------IAMV----------YQ 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 162 ttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-----QGypGAILIVSH 221
Cdd:cd03216 83 -----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrlraQG--VAVIFISH 140
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
342-488 |
6.31e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-----------GSNVSVGYYDQEQANLTSSKR 410
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdiddpdvaEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VlnELWdeyplqpekeiRTILGNFLFTGDDVLK----------PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK13539 94 L--EFW-----------AAFLGGEELDIAAALEavglaplahlPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
....*...
gi 446524801 481 NSKEILEN 488
Cdd:PRK13539 161 AAVALFAE 168
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
331-504 |
6.59e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 79.87 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS--------VGYYDQE 401
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QAN---LTSSKRVLnelwdeYPLQ----PEKEIRTILGNFLF-TGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03259 81 YALfphLTVAENIA------FGLKlrgvPKAEIRARVRELLElVGLEGLlnRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524801 472 DEPTNHLDLNSKEILENALIDYPG----TLLFVSHDR 504
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-200 |
6.81e-17 |
|
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: 79.93 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTkDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------IGYLAQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIWdEMLTVFTHLQQMETKLRRleqemgkeenfsneATYERLLadyDQLQLN-YKDQggyqyeadirsilsg 152
Cdd:cd03264 80 EFGVYPNFTVR-EFLDYIAWLKGIPSKEVK--------------ARVDEVL---ELVNLGdRAKK--------------- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 153 lgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:cd03264 127 ----------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-194 |
7.64e-17 |
|
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: 80.03 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------I 68
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITglpphriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 69 GYLAQNTGLETSLTIWDemltvftHLqQMETKLRRLEQEMgkeenfsnEATYERLLADYDQLqlnykdqggyqyeADIRS 148
Cdd:COG0410 81 GYVPEGRRIFPSLTVEE-------NL-LLGAYARRDRAEV--------RADLERVYELFPRL-------------KERRR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524801 149 ILSGlgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:COG0410 132 QRAG-------------TLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
574-639 |
1.34e-16 |
|
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: 74.42 E-value: 1.34e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 574 LERQRTRKIEELEQSIVELEEEIATLEDQLCLPEIYADYEKASEITTKKQTLQEQLETCMAEWEEL 639
Cdd:pfam16326 2 LSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDYEKLQELSAELEELEAELEELYERWEEL 67
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-508 |
1.42e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.32 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 32 IALVGRNGAGKSTLLKIIAGELshdggeiiKPkdvsigylaqNTGLETSLTIWDEMLTVF--THLQQMETKLRrleqemG 109
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGEL--------IP----------NLGDYEEEPSWDEVLKRFrgTELQNYFKKLY------N 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 110 KEENFSNEATYERLLADY-----DQLQLNYKDQGGYQY---EADIRSILSglgfpvethqTTISTLSGGQKTRLALGKLL 181
Cdd:PRK13409 158 GEIKVVHKPQYVDLIPKVfkgkvRELLKKVDERGKLDEvveRLGLENILD----------RDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 182 LTKPDLLILDEPTNHLDI-ETLT---WLEQYLQGYPgaILIVSHDRYFLDKLVTQV---------YEI--SNKESRRFVG 246
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIrQRLNvarLIRELAEGKY--VLVVEHDLAVLDYLADNVhiaygepgaYGVvsKPKGVRVGIN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 247 NYskyldLKSALYEQEMK-RyekqQDEIakledfvqkniaraSTTKRAQSRRKQLDRmeLLTRPlgdsksasfhfDIEKQ 325
Cdd:PRK13409 306 EY-----LKGYLPEENMRiR----PEPI--------------EFEERPPRDESERET--LVEYP-----------DLTKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 326 SGNDVLQVNDATIgydenpiiehvtmrlTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSfgSNVSVGY---Y---D 399
Cdd:PRK13409 350 LGDFSLEVEGGEI---------------YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYkpqYikpD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QE---QANLTSSKRVLNE--LWDEY--PLQPEKeirtilgnfLFTgddvlKPVSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:PRK13409 413 YDgtvEDLLRSITDDLGSsyYKSEIikPLQLER---------LLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446524801 473 EPTNHLDLNS--------KEILENAlidyPGTLLFVSHDRYFIN 508
Cdd:PRK13409 479 EPSAHLDVEQrlavakaiRRIAEER----EATALVVDHDIYMID 518
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-517 |
1.51e-16 |
|
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: 79.46 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGY----DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSVGYYDQEQANL 405
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 -------TSS-------KRVLNE-LWDEYPLQPEKEIRTILgnflftgDDV-LKP------VSSLSGGQKARLALAKLMM 463
Cdd:COG1124 82 qmvfqdpYASlhprhtvDRILAEpLRIHGLPDREERIAELL-------EQVgLPPsfldryPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 464 QKSNLLILDEPTNHLDL-NSKEILeNALIDYPG----TLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG1124 155 LEPELLLLDEPTSALDVsVQAEIL-NLLKDLREerglTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
330-534 |
1.54e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.02 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQANLtSSK 409
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAF-EEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLN-------ELWdeyplQPEKEIRTILGNFLFTGDDVLK------------------------------------PVS 446
Cdd:PRK15064 80 TVLDtvimghtELW-----EVKQERDRIYALPEMSEEDGMKvadlevkfaemdgytaearagelllgvgipeeqhygLMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYL 526
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYP 234
|
....*...
gi 446524801 527 GDYDYYVE 534
Cdd:PRK15064 235 GNYDEYMT 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-244 |
1.58e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 16 ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTgletsltiwdemltvftHLQ 95
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRP-----------------YLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 96 QmeTKLRRLeqemgkeenfsneATYERLLADYDqlqlnykdqggyqyEADIRSILS--GLGFPVE---THQTTISTLSGG 170
Cdd:COG4178 439 L--GTLREA-------------LLYPATAEAFS--------------DAELREALEavGLGHLAErldEEADWDQVLSLG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 171 QKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQG-YPGAILI-VSHdRYFLDKLVTQVYEISNKESRRF 244
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTTVIsVGH-RSTLAAFHDRVLELTGDGSWQL 564
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.75e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.30 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYL 71
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlLDGRDVTglppekrnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLetsltiwdemltvFTHLqqmeT---------KLRRleqeMGKEEnfsNEATYERLLadyDQLQLnykdqGGYqy 142
Cdd:COG3842 83 FQDYAL-------------FPHL----TvaenvafglRMRG----VPKAE---IRARVAELL---ELVGL-----EGL-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 143 eADIRsilsglgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILI 218
Cdd:COG3842 129 -ADRY----------------PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIY 191
|
....*
gi 446524801 219 VSHDR 223
Cdd:COG3842 192 VTHDQ 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
331-502 |
2.07e-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: 77.35 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN--PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSvgyydQEQANLTS 407
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdGVPVS-----DLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 SKRVLNElwdeyplQPEKEIRTILGNFlftGddvlkpvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEIL 486
Cdd:cd03247 76 LISVLNQ-------RPYLFDTTLRNNL---G-------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLL 138
|
170
....*....|....*..
gi 446524801 487 ENALIDYPG-TLLFVSH 502
Cdd:cd03247 139 SLIFEVLKDkTLIWITH 155
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
331-475 |
2.21e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 78.63 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS-----------VGYY 398
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQEQ---ANLTsskrVL-NELWDEYPLQPEKEIRTI---LGNFlftgdDVLK-----PVSSLSGGQKARLALAKLMMQKS 466
Cdd:cd03224 81 PEGRrifPELT----VEeNLLLGAYARRRAKRKARLervYELF-----PRLKerrkqLAGTLSGGEQQMLAIARALMSRP 151
|
....*....
gi 446524801 467 NLLILDEPT 475
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
326-503 |
2.36e-16 |
|
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: 78.87 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 326 SGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVSvgyydqeqan 404
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 405 lTSSKRVLNE-------------LWD--------EYPLQ-----PEKEIRTI---------LGNFLFtgddvLKPvSSLS 449
Cdd:COG1127 71 -GLSEKELYElrrrigmlfqggaLFDsltvfenvAFPLRehtdlSEAEIRELvleklelvgLPGAAD-----KMP-SELS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 450 GGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEIleNALI-----DYPGTLLFVSHD 503
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITSAVI--DELIrelrdELGLTSVVVTHD 201
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-194 |
3.26e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 78.34 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----------IGYL 71
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrLDGEDITklppheraragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIWDEMLTVFTHLQQMETKLRrleqemgkeenfsneatyERLLADYDQLQLNYKDQGGyqyeadirsils 151
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIP------------------DEIYELFPVLKEMLGRRGG------------ 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 152 glgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:TIGR03410 131 --------------DLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
3.37e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.16 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------- 67
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlIDGQDISslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 ----IGYLAQNTGLETSLTIWdemltvfthlqqmetklrrleqemgkeENFsneatyerlladydQLQLNYKDQGGYQYE 143
Cdd:COG1136 84 rrrhIGFVFQFFNLLPELTAL---------------------------ENV--------------ALPLLLAGVSRKERR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 144 ADIRSILSGLG-------FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGY 212
Cdd:COG1136 123 ERARELLERVGlgdrldhRP--------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNREL 194
|
250 260
....*....|....*....|....*.
gi 446524801 213 PGAILIVSHDRyFLDKLVTQVYEISN 238
Cdd:COG1136 195 GTTIVMVTHDP-ELAARADRVIRLRD 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
331-490 |
3.43e-16 |
|
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: 77.53 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF---------GSNVSVGYYDQE 401
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfqrDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKRVLNELWDEYPLQPEKEIRTILGNFLFTG-DDVlkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGfEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 446524801 481 NSKEILENAL 490
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
331-503 |
3.60e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 77.90 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN----PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF------GSNVSVGYYDQ 400
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 401 eQANLTSSKRVLNELwdEYPLQ----PEKEIRTIlgnflftGDDVLKPV----------SSLSGGQKARLALAKLMMQKS 466
Cdd:cd03293 81 -QDALLPWLTVLDNV--ALGLElqgvPKAEARER-------AEELLELVglsgfenaypHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 467 NLLILDEPTNHLDLNSKEILENALID----YPGTLLFVSHD 503
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-238 |
6.09e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.40 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQvnALSKLYGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV---- 66
Cdd:COG2884 1 MIRFE--NVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrLKRREIpylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 67 -SIGYLAQNTGLETSLTIWDemltvfthlqqmetklrrleqemgkeenfsNEAtyerlLAdydqLQLNYKDQGgyQYEAD 145
Cdd:COG2884 79 rRIGVVFQDFRLLPDRTVYE------------------------------NVA-----LP----LRVTGKSRK--EIRRR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 146 IRSILS--GLG-----FPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ-----Gyp 213
Cdd:COG2884 118 VREVLDlvGLSdkakaLPHE--------LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEeinrrG-- 187
|
250 260
....*....|....*....|....*
gi 446524801 214 GAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:COG2884 188 TTVLIATHDLELVDRMPKRVLELED 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-222 |
6.23e-16 |
|
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: 79.77 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 22 IKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQntglETSLtiwde 86
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQ----EARL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 87 mltvFTHLQQMETKLRRLEQEMGKEENFSNEATYERLladydqlqlnykdqggyqyeadirsilsGLGFPVethQTTIST 166
Cdd:TIGR02142 87 ----FPHLSVRGNLRYGMKRARPSERRISFERVIELL----------------------------GIGHLL---GRLPGR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHS 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
331-503 |
6.51e-16 |
|
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: 77.22 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLLN------GDVSF-GSNVSVGYYD---- 399
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIpgapdeGEVLLdGKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 --------QE--------QANLTSSKRVLNELWDEyplQPEKEIRTILGNFLFTG--DDVLKPvSSLSGGQKARLALAKL 461
Cdd:cd03260 80 rrrvgmvfQKpnpfpgsiYDNVAYGLRLHGIKLKE---ELDERVEEALRKAALWDevKDRLHA-LGLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524801 462 MMQKSNLLILDEPTNHLDLNSKEILENALI----DYpgTLLFVSHD 503
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAelkkEY--TIVIVTHN 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-198 |
7.93e-16 |
|
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: 76.55 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KPKDVS----IGYLAQNTG 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgKPLDIAarnrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 LETSLTIWDeMLTVFTHLQQMetklrrleqemgKEENFSNEATY--ERL-LADYdqlqlnykdqggyqyeADIRsilsgl 153
Cdd:cd03269 81 LYPKMKVID-QLVYLAQLKGL------------KKEEARRRIDEwlERLeLSEY----------------ANKR------ 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 154 gfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03269 126 ----------VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
331-490 |
9.10e-16 |
|
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: 76.35 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDE-----NPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSnvSVGYYDQEQanl 405
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 tsskrvlnelWdeypLQPEkeirTILGNFLFtG--------DDVLKPVS---------------------SLSGGQKARL 456
Cdd:cd03250 76 ----------W----IQNG----TIRENILF-GkpfdeeryEKVIKACAlepdleilpdgdlteigekgiNLSGGQKQRI 136
|
170 180 190
....*....|....*....|....*....|....*
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLDLN-SKEILENAL 490
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCI 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-508 |
9.19e-16 |
|
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: 80.60 E-value: 9.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 32 IALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvsigylaqntgletsltiWDEMLTVF--THLQQMETKLRrlEQEM- 108
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPS------------------WDEVLKRFrgTELQDYFKKLA--NGEIk 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 109 ----------------GkeenfsneaTYERLLADYDQLqlnyKDQGGYQYEADIRSILSglgfpvethqTTISTLSGGQK 172
Cdd:COG1245 162 vahkpqyvdlipkvfkG---------TVRELLEKVDER----GKLDELAEKLGLENILD----------RDISELSGGEL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 173 TRLALGKLLLTKPDLLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVY----------EISNK 239
Cdd:COG1245 219 QRVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHilygepgvygVVSKP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 240 ESRRfVG--NYskyldLKSALYEQEMK-RyekqQDEIakleDFvqkniarasttkRAQSRRKQLDRMELLTRPlgdsksa 316
Cdd:COG1245 299 KSVR-VGinQY-----LDGYLPEENVRiR----DEPI----EF------------EVHAPRREKEEETLVEYP------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 317 sfhfDIEKQSGNDVLQVNDATIgydenpiiehvtmrlTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSvg 396
Cdd:COG1245 346 ----DLTKSYGGFSLEVEGGEI---------------REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIS-- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 397 YYDQeqanltsskrvlnELWDEYPLQPEKEIRTILGNFLFTG---DDVLKP----------VSSLSGGQKARLALAKLMM 463
Cdd:COG1245 405 YKPQ-------------YISPDYDGTVEEFLRSANTDDFGSSyykTEIIKPlgleklldknVKDLSGGELQRVAIAACLS 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 464 QKSNLLILDEPTNHLDLNS--------KEILENalidYPGTLLFVSHDRYFIN 508
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQrlavakaiRRFAEN----RGKTAMVVDHDIYLID 520
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-222 |
1.11e-15 |
|
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: 76.94 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-------------I 68
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlVDGQDITglsekelyelrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 69 GYLAQNTGLETSLTIWDEM---LTVFTHL------QQMETKLRRLEqemgkeenfsneatyerlLADYDQLqlnykdqgg 139
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVafpLREHTDLseaeirELVLEKLELVG------------------LPGAADK--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 140 yqyeadirsilsglgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----------IETLTwleqyl 209
Cdd:COG1127 138 ---------------MPSE--------LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavidelIRELR------ 188
|
250
....*....|...
gi 446524801 210 QGYPGAILIVSHD 222
Cdd:COG1127 189 DELGLTSVVVTHD 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
331-518 |
1.29e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvnklpllNGDVSFGS-NVSVGYYDQEQANLTSSK 409
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI-------NGTLTPTAgTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPLQPEKEIRTI--------LGNFLFTGDD-----------------VLKPVSSLSGGQKARLALAKLMMQ 464
Cdd:PRK09536 77 RRVASVPQDTSLSFEFDVRQVvemgrtphRSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 465 KSNLLILDEPTNHLDLNSK-EILENA--LIDYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQvRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-221 |
1.33e-15 |
|
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: 77.05 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELsH--DGGEI--------------IKPKdvsIGY----LA 72
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL-PptYGNDVrlfgerrggedvweLRKR---IGLvspaLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNtgLETSLTIWDEMLT-------VFTHL-QQMETKLRRLEQEMGKEEnfsneatyerlLADydqlqlnykdqggyqyea 144
Cdd:COG1119 89 LR--FPRDETVLDVVLSgffdsigLYREPtDEQRERARELLELLGLAH-----------LAD------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 145 dirsilsglgfpvethqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVS 220
Cdd:COG1119 138 -----------------RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVT 200
|
.
gi 446524801 221 H 221
Cdd:COG1119 201 H 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-511 |
1.50e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLLNGDVS-------FGSNVSvgyydQEQA 403
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRvegrvefFNQNIY-----ERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 NLTSSKRVLNELWDE---YPL---------------QPEKEIRTILGNFLFTGD-------DVLKPVSSLSGGQKARLAL 458
Cdd:PRK14258 82 NLNRLRRQVSMVHPKpnlFPMsvydnvaygvkivgwRPKLEIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 459 AKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPGTLLFVSHDRYFINRVT 511
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-222 |
1.56e-15 |
|
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: 75.75 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQN 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWDEMltvfthlqQMETKLRRleqemgkeenFSNEATYERLLADYDQLQlnykdqggyqyeadIRSILSGLg 154
Cdd:cd03301 81 YALYPHMTVYDNI--------AFGLKLRK----------VPKDEIDERVREVAELLQ--------------IEHLLDRK- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 155 fpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:cd03301 128 ---------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-221 |
2.67e-15 |
|
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: 74.84 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigyLAQNTGLETSLTI 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----------LLNGGPLDFQRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMLTVFTHLQQMETKLRRLEQEMGKEENFSNEATYERLladyDQLQLNykdqgGYQYEAdirsilsglgfpvethqtt 163
Cdd:cd03231 71 IARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEAL----ARVGLN-----GFEDRP------------------- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP---GAILIVSH 221
Cdd:cd03231 123 VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-210 |
2.77e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.05 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYLAQNTGLeTSLT 82
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTLESLrrQIGVVPQDTFL-FSGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWDEMLtvfthlqqmetklrrleqeMGKEEnfsneATYERLLADYDQLQLnykdqggyqyEADIRSILSGLgfpvethQT 162
Cdd:COG1132 430 IRENIR-------------------YGRPD-----ATDEEVEEAAKAAQA----------HEFIEALPDGY-------DT 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524801 163 TI----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQ 210
Cdd:COG1132 469 VVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET----EALIQ 516
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
330-487 |
3.13e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.86 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS------------- 394
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdGQDVTalrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQeQANLTSSKRVL-NEL---------WdeyplqpekeiRTILGnfLFTGDDV----------------LKPVSSL 448
Cdd:COG3638 82 IGMIFQ-QFNLVPRLSVLtNVLagrlgrtstW-----------RSLLG--LFPPEDReralealervgladkaYQRADQL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 449 SGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE 487
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDpKTARQVMD 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-198 |
3.18e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------- 67
Cdd:COG1101 2 LELKNLSKTFNPGTvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKDVTklpeykraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 IGYLAQNTGLET--SLTIwdemltvfthlqqmetklrrleqemgkEENFSneatyerlLADYDQLQLNYKDQGGYQYEAD 145
Cdd:COG1101 82 IGRVFQDPMMGTapSMTI---------------------------EENLA--------LAYRRGKRRGLRRGLTKKRREL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524801 146 IRSILSGLGFPVETHQTT-ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG1101 127 FRELLATLGLGLENRLDTkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-201 |
3.35e-15 |
|
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: 75.45 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGaETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQN 74
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWDEMLTVFTHLQQMETKLRRLEQEMGKEENFSNeatyerlladydqlQLNYKDQggyqyeadirsilsglg 154
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDH--------------LLNRKPE----------------- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 155 fpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03299 129 -----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-222 |
3.87e-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: 75.45 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQN 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWDemlTVFTHLQQMETKLRRLEQEMgkeenfsnEATYERLLadyDQLQlnykdqggyqyeadirsiLSGLG 154
Cdd:cd03296 83 YALFRHMTVFD---NVAFGLRVKPRSERPPEAEI--------RAKVHELL---KLVQ------------------LDWLA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 155 --FPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:cd03296 131 drYPAQ--------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-198 |
5.36e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQtKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS-IGYLAQNT 75
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVP-KGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgepLDPEDRRrIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 76 GLETSLTIWDEmLTVFTHLQQMETK--LRRLEQEMgkeenfsneatyERL-LADYdqlqlnYKDQggyqyeadirsilsg 152
Cdd:COG4152 81 GLYPKMKVGEQ-LVYLARLKGLSKAeaKRRADEWL------------ERLgLGDR------ANKK--------------- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524801 153 lgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG4152 127 -----------VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
310-502 |
6.14e-15 |
|
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: 78.24 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 310 LGDSKSASFHFDIEKQSGNDVLQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS 388
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 389 fgsnvsVGYYDQEQANLTSSKRVLNELwdeyPLQPEKEIRTILGNFLF------TGDDVLKPV----------------- 445
Cdd:TIGR01193 533 ------LNGFSLKDIDRHTLRQFINYL----PQEPYIFSGSILENLLLgakenvSQDEIWAACeiaeikddienmplgyq 602
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 446 -------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR01193 603 telseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-192 |
7.28e-15 |
|
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: 74.11 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSiGYLAQNTGLetsltiwDEMLTVfthlqq 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-SLLGLGGGF-------NPELTG------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 97 metklrrleqemgkEENFsneatyeRLLAdydqLQLNYKDQGGYQYEADIRSiLSGLGFPVETHqttISTLSGGQKTRLA 176
Cdd:cd03220 102 --------------RENI-------YLNG----RLLGLSRKEIDEKIDEIIE-FSELGDFIDLP---VKTYSSGMKARLA 152
|
170
....*....|....*.
gi 446524801 177 LGKLLLTKPDLLILDE 192
Cdd:cd03220 153 FAIATALEPDILLIDE 168
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
331-475 |
8.55e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 74.10 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS-----------VGYY 398
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLdGEDITklppheraragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQEQ---ANLT--------------SSKRVLNELWDEYPLQpeKEIRTILGnflftGDdvlkpvssLSGGQKARLALAKL 461
Cdd:TIGR03410 81 PQGReifPRLTveenlltglaalprRSRKIPDEIYELFPVL--KEMLGRRG-----GD--------LSGGQQQQLAIARA 145
|
170
....*....|....
gi 446524801 462 MMQKSNLLILDEPT 475
Cdd:TIGR03410 146 LVTRPKLLLLDEPT 159
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-239 |
1.05e-14 |
|
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: 72.19 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLeTSLTiwdemltvfthlqq 96
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGT-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 97 metkLRRleqemgkeenfsneatyerlladydqlQLNYkdqggyqyeadirsilsglgfPVEthqttiSTLSGGQKTRLA 176
Cdd:cd03223 80 ----LRE---------------------------QLIY---------------------PWD------DVLSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 177 LGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYpGAILI-VSHdRYFLDKLVTQVYEISNK 239
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL-GITVIsVGH-RPSLWKFHDRVLDLDGE 163
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-198 |
1.10e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.88 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSIGYL 71
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtdLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLetsltiWDEMlTVFthlQQMET--KLRRL-EQEMGKEenfSNEATyERL-LADYdqlqLNYKdqggyqyeadir 147
Cdd:COG3839 81 FQSYAL------YPHM-TVY---ENIAFplKLRKVpKAEIDRR---VREAA-ELLgLEDL----LDRK------------ 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 148 silsglgfPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG3839 131 --------P--------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-222 |
1.84e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 73.49 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 9 LSKLYGA-ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDV----------SIGYLAQNTG 76
Cdd:cd03295 6 VTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfIDGEDIreqdpvelrrKIGYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 LETSLTIWDEMLTVFTHLQQMETKLRRLEQEmgkeenfsneatyerLLADYDQLQLNYKDQggYQYEadirsilsglgfp 156
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWPKEKIRERADE---------------LLALVGLDPAEFADR--YPHE------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 157 vethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ---YLQGYPG-AILIVSHD 222
Cdd:cd03295 136 ----------LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGkTIVFVTHD 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-503 |
1.89e-14 |
|
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: 72.71 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 354 TRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVsvgYYDQEQA-NLTSSKRVLNELWDEYPLQP--------- 423
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKiNLPPQQRKIGLVFQQYALFPhlnvrenla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 424 ---------EKEIRT--ILGnfLFTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL- 490
Cdd:cd03297 98 fglkrkrnrEDRISVdeLLD--LLGLDHLLNrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELk 175
|
170
....*....|....*.
gi 446524801 491 ---IDYPGTLLFVSHD 503
Cdd:cd03297 176 qikKNLNIPVIFVTHD 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
330-475 |
2.01e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.09 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS-----------VGY 397
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 398 YDQEQ---ANLT----------------SSKRVLNELWDEYP-LqpeKEIRTILGNflftgddvlkpvsSLSGGQKARLA 457
Cdd:COG0410 83 VPEGRrifPSLTveenlllgayarrdraEVRADLERVYELFPrL---KERRRQRAG-------------TLSGGEQQMLA 146
|
170
....*....|....*...
gi 446524801 458 LAKLMMQKSNLLILDEPT 475
Cdd:COG0410 147 IGRALMSRPKLLLLDEPS 164
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-201 |
2.53e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 72.18 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGYLAQNTGLETSLTI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII------IDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMLTVFTH---------LQQMETKLRRLeQEMGKEEnfsNEATYERLLadydqlqlnykDQGGYQYEADirsilsglG 154
Cdd:cd03262 75 RQKVGMVFQQfnlfphltvLENITLAPIKV-KGMSKAE---AEERALELL-----------EKVGLADKAD--------A 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 155 FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03262 132 YP--------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-200 |
3.22e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI---IKPKDVSIGYLAQ 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLE-TSLTIWDEMlTVFTHLQQMETKLRRLEQEMGKEENfsneatyERLLAdydQLQLNYKdqggyqyeADirsilsg 152
Cdd:PRK11124 83 NVGMVfQQYNLWPHL-TVQQNLIEAPCRVLGLSKDQALARA-------EKLLE---RLRLKPY--------AD------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 153 lGFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK11124 137 -RFPLH--------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-201 |
4.21e-14 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 72.22 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIKPKDVS-------I 68
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLnglveptSGSVLIDGTDINKLKGKAlrqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 69 GYLAQNTGLETSLTIWDEMLTVFthLQQMETkLRRLEQEMGKEEnfsneatYERLLADYDQLQLnykdqggyqyeadirs 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGR--LGRRST-WRSLFGLFPKEE-------KQRALAALERVGL---------------- 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 149 ilsglgfpVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03256 135 --------LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPAS 179
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
330-517 |
4.60e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 71.62 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS------------- 394
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvNGQDLSrlkrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQEQanltsskRVLNEL--WD--EYPLQ----PEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARL 456
Cdd:COG2884 81 IGVVFQDF-------RLLPDRtvYEnvALPLRvtgkSRKEIRRRV-------REVLdlvglsdkakALPHELSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLD-LNSKEILE-----NALidypG-TLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDpETSWEIMElleeiNRR----GtTVLIATHDLELVDRMPKRVLEL 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-222 |
4.66e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.09 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANikLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-------------KPkdVSIgy 70
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltalppaeRP--VSM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLetsltiwdemltvFTHLqqmetklrRLEQEMGkeenfsneatyerlLADYDQLQLNYKDQggyqyeADIRSIL 150
Cdd:COG3840 76 LFQENNL-------------FPHL--------TVAQNIG--------------LGLRPGLKLTAEQR------AQVEQAL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 S--GLG-----FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIV 219
Cdd:COG3840 115 ErvGLAglldrLP--------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMV 186
|
...
gi 446524801 220 SHD 222
Cdd:COG3840 187 THD 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
331-515 |
5.11e-14 |
|
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: 71.02 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLPLLNGDVSFGsnvsvgyyDQEQANLTSS 408
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK--------GEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNEL---WdEYPLqpekEIRTIlgnflfTGDDVLKPVS-SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKE 484
Cdd:cd03217 73 ERARLGIflaF-QYPP----EIPGV------KNADFLRYVNeGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190
....*....|....*....|....*....|....
gi 446524801 485 ILENA---LIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:cd03217 142 LVAEVinkLREEGKSVLIITHYQRLLDYIKPDRV 175
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
5.29e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.46 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSI--GYL 71
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplaaWSPWELARrrAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIWDemlTVfthlqqmetklrrleqEMGKEENFSNEATYERLLADYdqLQLnykdqggyqyeADirsiLS 151
Cdd:COG4559 81 PQHSSLAFPFTVEE---VV----------------ALGRAPHGSSAAQDRQIVREA--LAL-----------VG----LA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 GLGfpvethQTTISTLSGGQKTRLALGKLLL-------TKPDLLILDEPTNHLDI----ETLTWLEQYLQGyPGAILIVS 220
Cdd:COG4559 125 HLA------GRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQLARR-GGGVVAVL 197
|
..
gi 446524801 221 HD 222
Cdd:COG4559 198 HD 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-222 |
5.35e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTiwdemLTVfthlqqmetklrrleqemgkeenfsneatyERLLadydQLQLNYKDqggyqyeADIRSILSGLGfPVETH 160
Cdd:PRK09544 82 LP-----LTV------------------------------NRFL----RLRPGTKK-------EDILPALKRVQ-AGHLI 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWL----EQYLQGYPGAILIVSHD 222
Cdd:PRK09544 115 DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
340-503 |
6.75e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.59 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSvgyYDQEQANLTSSKRVL---NELW 416
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVP---WKRRKKFLRRIGVVFgqkTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 417 -------------DEYPLQPEKEIRTI--LGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:cd03267 108 wdlpvidsfyllaAIYDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180
....*....|....*....|....*.
gi 446524801 482 SKEILENALIDY----PGTLLFVSHD 503
Cdd:cd03267 188 AQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
331-518 |
7.20e-14 |
|
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: 71.77 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYYD 399
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLaGVDLHglsrrararrVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QE---QANLTSSKRVL------NELWDEYPLQPEKEIRTILGNflfTGDDVL--KPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:TIGR03873 82 QDsdtAVPLTVRDVVAlgriphRSLWAGDSPHDAAVVDRALAR---TELSHLadRDMSTLSGGERQRVHVARALAQEPKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 469 LILDEPTNHLDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:TIGR03873 159 LLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLD 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-201 |
7.52e-14 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 71.63 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDV-----S 67
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtalRGRALrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 IGYLAQNTGLetsltIwdEMLTVFT-----HLQQMETkLRRLEQEMGKEEnfsneatYERLLADYDQLQLnyKDQggyqy 142
Cdd:COG3638 82 IGMIFQQFNL-----V--PRLSVLTnvlagRLGRTST-WRSLLGLFPPED-------RERALEALERVGL--ADK----- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 143 eADIRSilsglgfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG3638 140 -AYQRA----------------DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKT 181
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
330-503 |
8.28e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.73 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVSvGYYDQEQA----- 403
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlNGRPLA-DWSPAELArrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 -----NLTSSKRVlnelwDE------YPL-QPEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARLALAKL 461
Cdd:PRK13548 81 lpqhsSLSFPFTV-----EEvvamgrAPHgLSRAEDDALV-------AAALaqvdlahlagRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524801 462 MMQKSN------LLILDEPTNHLDL----NSKEILENALIDYPGTLLFVSHD 503
Cdd:PRK13548 149 LAQLWEpdgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-221 |
9.89e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIA-------GELSHDGGEIIKPKDV-SIGYLAQNT 75
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAgllppaaGTIKLDGGDIDDPDVAeACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 76 GLETSLTIwdemltvfthlqqmetklrrleqemgkEENfsneatyerlladydqLQL--NYKDQGgyqyEADIRSILSGL 153
Cdd:PRK13539 83 AMKPALTV---------------------------AEN----------------LEFwaAFLGGE----ELDIAAALEAV 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 154 GFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSH 221
Cdd:PRK13539 116 GLAPLAH-LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-222 |
1.05e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHdGGEII---KP-KDVSI-------GYLAQNTgleTSLTiwdeM 87
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILlngRPlSDWSAaelarhrAYLSQQQ---SPPF----A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 LTVFTHLQqmetklrrLEQEMGkeenfSNEATYERLLADY-DQLQLNYKdqggyqyeadirsilsgLGFPVethqttiST 166
Cdd:COG4138 84 MPVFQYLA--------LHQPAG-----ASSEAVEQLLAQLaEALGLEDK-----------------LSRPL-------TQ 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 167 LSGG--QKTRLAlGKLLLTKPD------LLILDEPTNHLDIE----TLTWLEQY-LQGypGAILIVSHD 222
Cdd:COG4138 127 LSGGewQRVRLA-AVLLQVWPTinpegqLLLLDEPMNSLDVAqqaaLDRLLRELcQQG--ITVVMSSHD 192
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
342-502 |
1.09e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 73.92 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDV-------------SFGSnvSVGYYDQeQANLTSS 408
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkqwdreTFGK--HIGYLPQ-DVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNELWDEYPLQPEKEIRT---------ILGnfLFTG-DDVLKPV-SSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:TIGR01842 407 TVAENIARFGENADPEKIIEAaklagvhelILR--LPDGyDTVIGPGgATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180
....*....|....*....|....*...
gi 446524801 478 LDLNSKEILENALIDYP---GTLLFVSH 502
Cdd:TIGR01842 485 LDEEGEQALANAIKALKargITVVVITH 512
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-198 |
1.36e-13 |
|
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: 69.89 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELS--HDGGEI------IKPKDV--SIGYLAQNTGLETSLTI 83
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVlingrpLDKRSFrkIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WdEMLtvfthlqqmetklrrleqemgkeenfsneatyerlladydqlqlnykdqggyQYEADIRSIlsglgfpvethqtt 163
Cdd:cd03213 100 R-ETL----------------------------------------------------MFAAKLRGL-------------- 112
|
170 180 190
....*....|....*....|....*....|....*
gi 446524801 164 istlSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03213 113 ----SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-210 |
1.39e-13 |
|
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: 70.48 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SIGYLAQ 73
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrEPREVrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIWDEMLTvfthlqqmetklrrleqeMGKEENFSNEATYERlladydqlqlnykdqggyqyeadIRSILSGL 153
Cdd:cd03265 81 DLSVDDELTGWENLYI------------------HARLYGVPGAERRER-----------------------IDELLDFV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 154 GFpVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ 210
Cdd:cd03265 120 GL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
329-479 |
1.42e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 329 DVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPllNGDVSFGSNVSVGYYDQEQAnltss 408
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--GTPVAGCVDVPDNQFGREAS----- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 409 krVLNELWDEYPLQPEKEIRTILG---NFLFtgddvLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:COG2401 102 --LIDAIGRKGDFKDAVELLNAVGlsdAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
339-517 |
1.49e-13 |
|
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: 70.25 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 339 GYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVS------VGYydqeQANLTSSKRV- 411
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllglgGGF----NPELTGRENIy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 LNELWdeYPLQPeKEIRTILGNFL-FT--GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN----SKE 484
Cdd:cd03220 107 LNGRL--LGLSR-KEIDEKIDEIIeFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQR 183
|
170 180 190
....*....|....*....|....*....|...
gi 446524801 485 ILENaLIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03220 184 RLRE-LLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
331-515 |
1.56e-13 |
|
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: 73.47 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI------------VNKLPLLNGDVSF-------- 389
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlgfvdptegsiaVNGVPLADADADSwrdqiawv 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 390 --------GS---NVSVGYYDQEQANLT-SSKRV-LNELWDEYPLQPEKEIrtilgnflftGDDVlkpvSSLSGGQKARL 456
Cdd:TIGR02857 402 pqhpflfaGTiaeNIRLARPDASDAEIReALERAgLDEFVAALPQGLDTPI----------GEGG----AGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVV 515
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAALADRIVV 528
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
1.82e-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: 68.78 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYG--AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGY 70
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrLDGADISqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNtgletsltiwdemltvfthlqqmetklrrleqemgkeenfsneatyerlladyDQLqlnykdqggyqyeadirsiL 150
Cdd:cd03246 81 LPQD-----------------------------------------------------DEL-------------------F 88
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 151 SGlgfpvethqtTIS--TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSH 221
Cdd:cd03246 89 SG----------SIAenILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAH 154
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
331-487 |
1.97e-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: 70.29 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgsnvsvgyYDQEQANLtsSK 409
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI--------DGTDINKL--KG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNEL-------WDEYPLQPEKE---------------IRTILGnfLFTG----------------DDVLKPVSSLSGG 451
Cdd:cd03256 71 KALRQLrrqigmiFQQFNLIERLSvlenvlsgrlgrrstWRSLFG--LFPKeekqralaalervgllDKAYQRADQLSGG 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524801 452 QKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE 487
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDpASSRQVMD 185
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-200 |
2.80e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 69.64 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQNTG 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 letsltiwdeMltVFthlQQ-------------ME--TKLRRleqeMGKEENfsnEATYERLLadyDQLQL-NYKDQggy 140
Cdd:COG1126 81 ----------M--VF---QQfnlfphltvlenvTLapIKVKK----MSKAEA---EERAMELL---ERVGLaDKADA--- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 141 qyeadirsilsglgFPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:COG1126 133 --------------YP--------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
331-490 |
3.05e-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: 69.57 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTL--------------------------LKSIVNKLPL 382
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnliprfydvdsgrilidghdvrdytLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 383 LNGDV-----SFGSNVSVGYYDQEQANLTSSKRVLN--ELWDEYPLQPEKEIrtilgnflftGDDVLKpvssLSGGQKAR 455
Cdd:cd03251 81 VSQDVflfndTVAENIAYGRPGATREEVEEAARAANahEFIMELPEGYDTVI----------GERGVK----LSGGQRQR 146
|
170 180 190
....*....|....*....|....*....|....*
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
3.30e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAetILAN--IKLEVQtKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------- 67
Cdd:COG3845 5 ALELRGITKRFGG--VVANddVSLTVR-PGEIhALLGENGAGKSTLMKILYGLYQPDSGEIlIDGKPVRirsprdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 IGYLAQNTGLETSLTIWdemltvfthlqqmetklrrleqemgkeENF--SNEATyERLLADYDQLqlnykdqggyqyEAD 145
Cdd:COG3845 82 IGMVHQHFMLVPNLTVA---------------------------ENIvlGLEPT-KGGRLDRKAA------------RAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 146 IRSILSGLGFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD-------IETLTWLEQylQGYpgAILI 218
Cdd:COG3845 122 IRELSERYGLDVDPD-AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRLAA--EGK--SIIF 196
|
...
gi 446524801 219 VSH 221
Cdd:COG3845 197 ITH 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-193 |
3.41e-13 |
|
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: 69.49 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----------IGYL 71
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlLDGQDITklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIWDEMLTVF-THLQQMETKLRRLEQemgkeenfsneatyerLLADYdqlqlnykdqggyqyeaDIRSIL 150
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLeIRGLSKKEREEKLEE----------------LLEEF-----------------HITHLR 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 151 SGLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEP 193
Cdd:cd03218 128 KSKA----------SSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
331-504 |
3.60e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.28 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLTSSKR 410
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD--------GRDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLN------ELWD--------EYPLQ----PEKEIRTI---------LGNFlftGDdvlKPVSSLSGGQKARLALAKLMM 463
Cdd:COG3842 78 NVGmvfqdyALFPhltvaenvAFGLRmrgvPKAEIRARvaellelvgLEGL---AD---RYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 464 QKSNLLILDEPTNHLDLNSKEILENALIDY----PGTLLFVSHDR 504
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQ 196
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-200 |
4.79e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI---IKPKDVSIGYLAQ 73
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLE-TSLTIWDEmLTVFTHLQQMETKLRRLEQEMGKEENfsneatyERLLAdydQLQL-NYKDQggyqyeadirsils 151
Cdd:COG4161 83 KVGMVfQQYNLWPH-LTVMENLIEAPCKVLGLSKEQAREKA-------MKLLA---RLRLtDKADR-------------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 152 glgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:COG4161 138 ---FPLH--------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-222 |
4.92e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNTGLetslt 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRDGQL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 iwdemltvfTHLQQM-ETKLRRL--------EQ--EMGKEENFSNEATY-ERLLAdydqlqlnykdQGGYQYeADIRSIL 150
Cdd:PRK11701 73 ---------RDLYALsEAERRRLlrtewgfvHQhpRDGLRMQVSAGGNIgERLMA-----------VGARHY-GDIRATA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFPVETHQTTI----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG----AILIVSHD 222
Cdd:PRK11701 132 GDWLERVEIDAARIddlpTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelglAVVIVTHD 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-221 |
4.94e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 68.55 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAE--TILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SI 68
Cdd:cd03266 1 MITADALTKRFRDVkkTVQAvdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAEArrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 69 GYLAQNTGLETSLTIWdEMLTVFTHLQQMEtklrrleqemgkeenfsneatyerlladydqlqlnykdqgGYQYEADIRS 148
Cdd:cd03266 81 GFVSDSTGLYDRLTAR-ENLEYFAGLYGLK----------------------------------------GDELTARLEE 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 149 ILSGLGFPvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSH 221
Cdd:cd03266 120 LADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
5.87e-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: 67.34 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYG--AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigYLaqntgletsl 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TL---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 tiwdemltvfthlqqmetklrrleqemgkeeNFSNEATYERLLADYdqlqLNYKDQGGYQYEAdirSILSGLGFPvethq 161
Cdd:cd03247 62 -------------------------------DGVPVSDLEKALSSL----ISVLNQRPYLFDT---TLRNNLGRR----- 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 162 ttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET-LTWLEQYLQGYPG-AILIVSH 221
Cdd:cd03247 99 -----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITH 155
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-238 |
6.60e-13 |
|
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: 68.20 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 11 KLYGAETI-LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS------IGYLAQNTGL--ETS 80
Cdd:cd03292 8 KTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSdlrgraIPYLRRKIGVvfQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDemLTVFTHLQ-QMEtklrrLEQEMGKEENfsneatyERLLADYDQLQLNYKdqggyqyeadirsilsglgfpvet 159
Cdd:cd03292 88 RLLPD--RNVYENVAfALE-----VTGVPPREIR-------KRVPAALELVGLSHK------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 160 HQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHDRYFLDKLVTQVYEI 236
Cdd:cd03292 130 HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIAL 209
|
..
gi 446524801 237 SN 238
Cdd:cd03292 210 ER 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-503 |
6.87e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 68.30 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 339 GYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvGYYDQEQANltSSKRVL------ 412
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-----GYSIRTDRK--AARQSLgycpqf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 413 NELWDEY-PLQ-----------PEKEIRTILGNFLFT---GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03263 84 DALFDELtVREhlrfyarlkglPKSEIKEEVELLLRVlglTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180
....*....|....*....|....*...
gi 446524801 478 LDLNSKEILENALIDYPG--TLLFVSHD 503
Cdd:cd03263 164 LDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
337-522 |
6.90e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 337 TIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVsfgsnvsvgYYDQEQANLTSSKRV----- 411
Cdd:PRK10253 14 TLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDGEHIQHYASKEVarrig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 -------------LNEL--WDEYPLQP------EKEIRTILGNFLFTG--DDVLKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK10253 85 llaqnattpgditVQELvaRGRYPHQPlftrwrKEDEEAVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 469 LILDEPTNHLDLNSK----EILENALIDYPGTLLFVSHD-----RYFINRVTTTVVELSTEGA 522
Cdd:PRK10253 165 MLLDEPTTWLDISHQidllELLSELNREKGYTLAAVLHDlnqacRYASHLIALREGKIVAQGA 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
330-492 |
7.07e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNklpLLNGDVSFGSNVSV-------------- 395
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAGSHIELlgrtvqregrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 396 --------GYYDQeQANLTSSKRVLNE----------LWDE-----YPLQPEKEIR--TILGNFLFTGddvlKPVSSLSG 450
Cdd:PRK09984 81 irksrantGYIFQ-QFNLVNRLSVLENvligalgstpFWRTcfswfTREQKQRALQalTRVGMVHFAH----QRVSTLSG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 451 GQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALID 492
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRD 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-542 |
7.14e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 325 QSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQAN 404
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 405 LTSSKRVLNELWDE--------------YPLQP-----EKEIRTIL-------GNFLFTGDDVLKPVSSLSGGQKARLAL 458
Cdd:PRK14246 85 AIKLRKEVGMVFQQpnpfphlsiydniaYPLKShgikeKREIKKIVeeclrkvGLWKEVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 459 AKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEKK 536
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
....*.
gi 446524801 537 NEMIER 542
Cdd:PRK14246 245 NELTEK 250
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
331-523 |
7.22e-13 |
|
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: 66.79 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLksivnklpllngdvsfgsnvsvgyydqeqanltssk 409
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLF------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWdeyPLQPEKEIRTILGNFLF--------TG---DDVLKPVSS-LSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03223 45 RALAGLW---PWGSGRIGMPEGEDLLFlpqrpylpLGtlrEQLIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 478 LDLNSK----EILENALIdypgTLLFVSHdRYFINRVTTTVVELSTEGAQ 523
Cdd:cd03223 122 LDEESEdrlyQLLKELGI----TVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4-222 |
7.55e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSklygAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSI----------GYLAQ 73
Cdd:PRK03695 1 MQLNDVA----VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAwsaaelarhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIWdEMLTVF----THLQQMETKLRRLEQemgkeenfsneatyerlladydQLQLNYKdqggyqyeadirsi 149
Cdd:PRK03695 77 QQTPPFAMPVF-QYLTLHqpdkTRTEAVASALNEVAE----------------------ALGLDDK-------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 150 lsgLGFPvethqttISTLSGG--QKTRLAlGKLLLTKPD------LLILDEPTNHLDIETLTWLEQYL-----QGypGAI 216
Cdd:PRK03695 120 ---LGRS-------VNQLSGGewQRVRLA-AVVLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLselcqQG--IAV 186
|
....*.
gi 446524801 217 LIVSHD 222
Cdd:PRK03695 187 VMSSHD 192
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
293-515 |
8.32e-13 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 71.44 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 293 AQSRRKQLDrmELLTRPLGDSKSASFhFDIEKQSGNdvLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKS 370
Cdd:TIGR03375 431 AKTALQSLD--ELMQLPVERPEGTRF-LHRPRLQGE--IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKS 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 371 TLLKSIVNKLPLLNGDVSF-GSNVS----------VGYYDQEQA--------NLTSSKRVLNelwDEYPLQPEKeiRTIL 431
Cdd:TIGR03375 506 TLLKLLLGLYQPTEGSVLLdGVDIRqidpadlrrnIGYVPQDPRlfygtlrdNIALGAPYAD---DEEILRAAE--LAGV 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 432 GNFLFT---GDDvlKPVS----SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:TIGR03375 581 TEFVRRhpdGLD--MQIGergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTH 658
|
250
....*....|...
gi 446524801 503 DRYFINRVTTTVV 515
Cdd:TIGR03375 659 RTSLLDLVDRIIV 671
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
9.48e-13 |
|
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: 67.98 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikPKDVSIGYLAQNtgletsltI 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLDGKD--------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMLTVfthlqqmeTKLRRleqEMG----KEENFSneatyerlLADYDQLQLNYKDQG---GYQYEADIRSILSGLGFP 156
Cdd:cd03260 70 YDLDVDV--------LELRR---RVGmvfqKPNPFP--------GSIYDNVAYGLRLHGiklKEELDERVEEALRKAALW 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 157 VETH-QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD------IETLtwLEQYLQGYpgAILIVSHD 222
Cdd:cd03260 131 DEVKdRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpistakIEEL--IAELKKEY--TIVIVTHN 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
341-515 |
1.12e-12 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 67.61 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 341 DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYYDQE-------- 401
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGYVPQDvtlfygtl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKRVLNelwDEYPLqpekEIRTILGNFLFTGDD-------VLKPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:cd03245 95 RDNITLGAPLAD---DERIL----RAAELAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 475 TNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVV 515
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVDRIIV 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
331-517 |
1.24e-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: 67.52 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIieHVTMRLTRGDSVALVGPNGIGKSTLLKSIVN-KLP-----LLNG-DVSFG--SNVSVGYYDQE 401
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPqsgrvLINGvDVTAAppADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 Q---ANLTSSKRVLNELWDEYPLQPE--KEIRTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:cd03298 79 NnlfAHLTVEQNVGLGLSPGLKLTAEdrQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 477 HLDlnskEILENALIDY--------PGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03298 158 ALD----PALRAEMLDLvldlhaetKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-201 |
1.41e-12 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 67.71 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYG-AETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDV-----S 67
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCInrlvepsSGSILLEGTDItkLRGKKLrklrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 IGYLAQNTGLETSLTIWDEMLTVFthLQQMETkLRRLEQEMGKEEnfsneatYERLLADYDQLQLNYKdqggyqyeADIR 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGR--LGYKPT-WRSLLGRFSEED-------KERALSALERVGLADK--------AYQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524801 148 SilsglgfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:TIGR02315 143 A----------------DQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-233 |
1.71e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKD--VSIGYLA 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTInlVRDKDgqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLETSLTIWDEMLTVFTHLQQMETKLRRLEQEMGkeenFSNEATYERLLADYDQLQLNYKDQGGYqyeadirsilsg 152
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLG----LSKQEARERAVKYLAKVGIDERAQGKY------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 153 lgfPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHDRYFLDKL 229
Cdd:PRK10619 150 ---PVH--------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHV 218
|
....
gi 446524801 230 VTQV 233
Cdd:PRK10619 219 SSHV 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-198 |
2.39e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----------IKPKDVSIGY 70
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLETSLTIwDEMLTVFTHLQQMETklRRLEQEMGKEENFSneatyeRLladydqlqlnykdqggyQYEADIRsil 150
Cdd:PRK13536 119 VPQFDNLDLEFTV-RENLLVFGRYFGMST--REIEAVIPSLLEFA------RL-----------------ESKADAR--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 151 sglgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13536 170 -------------VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-522 |
2.48e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 324 KQSGNDVLQVNDATIG-YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQE- 401
Cdd:COG4178 356 ETSEDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 ---QANLtssKRVLNelwdeYPLQPEK----EIRTI-----LGNF---LFTGDD---VLkpvsslSGGQKARLALAKLMM 463
Cdd:COG4178 436 ylpLGTL---REALL-----YPATAEAfsdaELREAleavgLGHLaerLDEEADwdqVL------SLGEQQRLAFARLLL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 464 QKSNLLILDEPTNHLDLNSKEILENALID-YPG-TLLFVSHdRYFINRVTTTVVELSTEGA 522
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-502 |
2.57e-12 |
|
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: 66.73 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENP---IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGY---YDQEQA 403
Cdd:cd03248 11 IVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 NLTSSKRVL--NELWDE--YPLQ--PEKEIRT----------ILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:cd03248 91 SLVGQEPVLfaRSLQDNiaYGLQscSFECVKEaaqkahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524801 468 LLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-501 |
2.77e-12 |
|
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: 69.47 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG--GEIikpkdvsigylaqntglets 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEI-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 ltIWDEMLTVFTHLQQMETK-LRRLEQEMGKEENFS--------NEATYERLLADYDQLQLNYKdqggyqyeadirSILS 151
Cdd:TIGR02633 61 --YWSGSPLKASNIRDTERAgIVIIHQELTLVPELSvaeniflgNEITLPGGRMAYNAMYLRAK------------NLLR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 GLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSHdryfldK 228
Cdd:TIGR02633 127 ELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISH------K 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 229 LvTQVYEISnkesrrfvgnyskyldlksalyeqemkryekqqDEIAKLEDfvqkniARASTTKRAQSrrkqLDRMELLTR 308
Cdd:TIGR02633 201 L-NEVKAVC---------------------------------DTICVIRD------GQHVATKDMST----MSEDDIITM 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 309 PLGDSKSASFHFDiEKQSGNDVLQVNDATIGYDENPII---EHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP---- 381
Cdd:TIGR02633 237 MVGREITSLYPHE-PHEIGDVILEARNLTCWDVINPHRkrvDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkfe 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 382 ---LLNG---DV-----SFGSNVSVGYYDQEQ----------ANLTSSkrVLNELWDEYPLQPEKEIRTILGNF----LF 436
Cdd:TIGR02633 316 gnvFINGkpvDIrnpaqAIRAGIAMVPEDRKRhgivpilgvgKNITLS--VLKSFCFKMRIDAAAELQIIGSAIqrlkVK 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 437 TGDDVLkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI--LENALIDYPGTLLFVS 501
Cdd:TIGR02633 394 TASPFL-PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyEIykLINQLAQEGVAIIVVS 460
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-198 |
2.77e-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: 66.53 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG---GEI------IKPKDV--SIGYLAQNTGLETSLTIwDE 86
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqpRKPDQFqkCVAYVRQDDILLPGLTV-RE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 87 MLTVFTHLqqmetKLRRLeqemgkeenfSNEATYERLLADYDQLQLNYKDQGGYQYEAdirsilsglgfpvethqttist 166
Cdd:cd03234 101 TLTYTAIL-----RLPRK----------SSDAIRKKRVEDVLLRDLALTRIGGNLVKG---------------------- 143
|
170 180 190
....*....|....*....|....*....|..
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03234 144 ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
328-514 |
3.16e-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: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDAT----IGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLksivNKLPLL----NGDVSF-GSNVS---- 394
Cdd:COG1136 2 SPLLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL----NILGGLdrptSGEVLIdGQDISslse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 ----------VGYYDQeQANLtsskrvLNEL--WD--EYPL--------QPEKEIRTILGNF-LftGDDVLKPVSSLSGG 451
Cdd:COG1136 78 relarlrrrhIGFVFQ-FFNL------LPELtaLEnvALPLllagvsrkERRERARELLERVgL--GDRLDHRPSQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 452 QKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILE--NALIDYPG-TLLFVSHDRYFINRVTTTV 514
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSkTGEEVLEllRELNRELGtTIVMVTHDPELAARADRVI 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-237 |
4.45e-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: 65.92 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSK-----LYGAETI--LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQN 74
Cdd:COG4778 3 TLLEVENLSKtftlhLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLE-TSLTIWdEMLtvfthlqqmetKLRRleQEMGKEENFSN--------EATYERLLAdydqlqlnykdQGGYQYEAD 145
Cdd:COG4778 75 GWVDlAQASPR-EIL-----------ALRR--RTIGYVSQFLRviprvsalDVVAEPLLE-----------RGVDREEAR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 146 IR--SILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGypG-AILI 218
Cdd:COG4778 130 ARarELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GtAIIG 207
|
250
....*....|....*....
gi 446524801 219 VSHDRYFLDKLVTQVYEIS 237
Cdd:COG4778 208 IFHDEEVREAVADRVVDVT 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-221 |
5.60e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 24 LEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKD----------VSIgyLAQNTGLETSLTIWDEM----- 87
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDhtttppsrrpVSM--LFQENNLFSHLTVAQNIglgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 --LTVfTHLQQMetKLRRLEQEMGKEENFsneatyERLladydqlqlnykdqggyqyeadirsilsglgfPvethqttiS 165
Cdd:PRK10771 98 pgLKL-NAAQRE--KLHAIARQMGIEDLL------ARL--------------------------------P--------G 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSH 221
Cdd:PRK10771 129 QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-201 |
6.47e-12 |
|
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: 65.68 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQvnALSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDV- 66
Cdd:cd03258 1 MIELK--NVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLtlLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 67 ----SIGYLAQNTGLETSLTIWDEMltvfthlqqmetklrRLEQEMGKEENFSNEATYERLLAdydqlqlnykdqggyqy 142
Cdd:cd03258 79 karrRIGMIFQHFNLLSSRTVFENV---------------ALPLEIAGVPKAEIEERVLELLE----------------- 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 143 eadirsiLSGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03258 127 -------LVGLE---DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-221 |
6.47e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIG----YLA 72
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepIRRQRDEYHqdllYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLETSLTIWdemltvfthlqqmetklrrleqemgkeENfsneatyerlladydqLQLNYKDQGGYQyEADIRSILS- 151
Cdd:PRK13538 81 HQPGIKTELTAL---------------------------EN----------------LRFYQRLHGPGD-DEALWEALAq 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 -GL-GF---PVethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-----QGypGAILIVSH 221
Cdd:PRK13538 117 vGLaGFedvPV-------RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhaeQG--GMVILTTH 187
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-194 |
6.96e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVsigylaqnTGLET 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfDGKDI--------TDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 80 SLTIWDEMLTVfthlqqmeTKLRRLEQEMGKEENFSneatyerlladydqlqlnykdQGGY-----QYEADIRSILSGLG 154
Cdd:PRK11614 75 AKIMREAVAIV--------PEGRRVFSRMTVEENLA---------------------MGGFfaerdQFQERIKWVYELFP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 155 FPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:PRK11614 126 RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
331-502 |
1.15e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.50 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNG--DVSFGSnVSVGYYDQEQANLTS 407
Cdd:COG1132 340 IEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVN-------LLLRfyDPTSGR-ILIDGVDIRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 skrvlnelwdeyplqpekeIRTILG-----NFLFTG----------------------------DDVLK-------PV-- 445
Cdd:COG1132 412 -------------------LRRQIGvvpqdTFLFSGtirenirygrpdatdeeveeaakaaqahEFIEAlpdgydtVVge 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 446 --SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:COG1132 473 rgVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-229 |
1.21e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVS--IGYlaqNTGLETSLTiwdemltvfthl 94
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalLEL---GAGFHPELT------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 95 qqmetklrrleqemGkEEN-FSNEATYERLLADYDQLqlnykdqggyqyEADIRSiLSGLG-F---PVethqttiSTLSG 169
Cdd:COG1134 105 --------------G-RENiYLNGRLLGLSRKEIDEK------------FDEIVE-FAELGdFidqPV-------KTYSS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 170 GQKTRLALGKLLLTKPDLLILDEPTNHLDIE----TLTWLEQYLQGyPGAILIVSHDRYFLDKL 229
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRL 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-222 |
1.24e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLY---------GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigyL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV----------S 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETsltiwdemltvfthLQQMETKLRRLEQEMGKEENFSN---EATYERLLAD--YDQLQLNYKDQggyqyEADI 146
Cdd:PRK10419 71 WRGEPLAK--------------LNRAQRKAFRRDIQMVFQDSISAvnpRKTVREIIREplRHLLSLDKAER-----LARA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 147 RSILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK10419 132 SEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-233 |
1.41e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 9 LSKLYGAETILANIKLEVQTKDRIALVGRNGAGKST----LLKIIA--GELSHDGGEIikpkdvsigylaQNTGLETSLT 82
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPL------------HNLNRRQLLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWDEMLTVFthlQQMETKLR-RLEQEMGKEENfsneatyerlladydqLQLNYKDQGGYQYEADIRSILSGLGFPVETHQ 161
Cdd:PRK15134 360 VRHRIQVVF---QDPNSSLNpRLNVLQIIEEG----------------LRVHQPTLSAAQREQQVIAVMEEVGLDPETRH 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 162 TTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQV 233
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
330-503 |
1.64e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 65.11 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGY----DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS-----VGYYD 399
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPVTgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QE---------QANLtsskrvlnelwdEYPLQ----PEKEIRTILGNFLftgDDV-LKPV-----SSLSGGQKARLALAK 460
Cdd:COG1116 87 QEpallpwltvLDNV------------ALGLElrgvPKAERRERARELL---ELVgLAGFedaypHQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 461 LMMQKSNLLILDEPTNHLDLNSKEILENALID----YPGTLLFVSHD 503
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwqeTGKTVLFVTHD 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
331-504 |
1.65e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI----------VnklpLLNGDVSFgSNVS-----V 395
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdsgrI----VLNGRDLF-TNLPprerrV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 396 GYYDQEQA---NLTSSK------RVLNelwdeyplQPEKEIRTILgnflftgDDVLKPV----------SSLSGGQKARL 456
Cdd:COG1118 78 GFVFQHYAlfpHMTVAEniafglRVRP--------PSKAEIRARV-------EELLELVqlegladrypSQLSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHDR 504
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQ 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-222 |
2.27e-11 |
|
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: 65.89 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 21 NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQntglETSLtiwd 85
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqdsargifLPPHRRRIGYVFQ----EARL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 86 emltvFTHLqqmetklrrleqemGKEENfsneatyerlladydqLQLNYKDQGGYQYEADIRSILSGLGFpveTH--QTT 163
Cdd:COG4148 89 -----FPHL--------------SVRGN----------------LLYGRKRAPRAERRISFDEVVELLGI---GHllDRR 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQyLQ---GYPgaILIVSHD 222
Cdd:COG4148 131 PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLER-LRdelDIP--ILYVSHS 193
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
330-515 |
2.41e-11 |
|
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: 64.29 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNG-DVS-------------- 388
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGrDITglpphriarlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 389 -------FGS-----NVSVGYYDQEQANLTSSKRVLNELWDEYPlQPEKEIRTILGnflFTG-DDVL-KPVSSLSGGQKA 454
Cdd:COG0411 84 tfqnprlFPEltvleNVLVAAHARLGRGLLAALLRLPRARREER-EARERAEELLE---RVGlADRAdEPAGNLSYGQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 455 RLALAKLMMQKSNLLILDEPTNhlDLNSKEILE-NALI----DYPG-TLLFVSHDRYFINRVTTTVV 515
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAA--GLNPEETEElAELIrrlrDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
331-502 |
2.48e-11 |
|
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: 62.45 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgsnvsvgyyDQEQANLTSSKR 410
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV---------DGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNelwdeyplqpeKEIRTilgnflftgddvlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILEN-- 488
Cdd:cd03216 72 ARR-----------AGIAM---------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKvi 125
|
170
....*....|....*
gi 446524801 489 -ALIDYPGTLLFVSH 502
Cdd:cd03216 126 rRLRAQGVAVIFISH 140
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-479 |
2.53e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIGYLAQNTGLETSL 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 TIWDEMLtvFTHLQQMETKLRRLEQemgkeenfsNEATYERLLADYDQL--QLNYKDQGGYQYEAD--IRSILSGlgfpv 157
Cdd:PRK15439 91 VPQEPLL--FPNLSVKENILFGLPK---------RQASMQKMKQLLAALgcQLDLDSSAGSLEVADrqIVEILRG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 158 ethqttistlsggqktrlalgklLLTKPDLLILDEPTNHLD-IETLTwleqylqgypgailIVSHDRYFLDKLVTQVYeI 236
Cdd:PRK15439 155 -----------------------LMRDSRILILDEPTASLTpAETER--------------LFSRIRELLAQGVGIVF-I 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 237 SNK--ESRRFVGNYSKYLDLKSALYEqemkryekqqdeiaKLEDFVQKNIARASTTKraqSRRKQLDRMELLTRPLGDSK 314
Cdd:PRK15439 197 SHKlpEIRQLADRISVMRDGTIALSG--------------KTADLSTDDIIQAITPA---AREKSLSASQKLWLELPGNR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 315 SAsfhfdieKQSGNDVLQVNDAT-IGYdenpiiEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFG--- 390
Cdd:PRK15439 260 RQ-------QAAGAPVLTVEDLTgEGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgke 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 391 -SNVSVG--------YY--DQEQA----------NLTSSKRVLNELWdeypLQPEKEIRTILG-----NFLFTGDDvlKP 444
Cdd:PRK15439 327 iNALSTAqrlarglvYLpeDRQSSglyldaplawNVCALTHNRRGFW----IKPARENAVLERyrralNIKFNHAE--QA 400
|
490 500 510
....*....|....*....|....*....|....*
gi 446524801 445 VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-224 |
2.54e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-------IGYLAQN 74
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTATrgdrsrfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWdEMLTVFTHLQQmetklRRLEQEMGKEENFSNEATYErlladydqlqlnykdqggyqyeadirsilsglg 154
Cdd:PRK13543 91 PGLKADLSTL-ENLHFLCGLHG-----RRAKQMPGSALAIVGLAGYE--------------------------------- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 155 fpvethQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRY 224
Cdd:PRK13543 132 ------DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-223 |
2.58e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVSigylaqntglets 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDIS------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 lTIWDEmltvfTHLQQMetklrrleqemgkeenfSNEATYERLLAD--YDQLQLNYKDQGGYQYEADIRSILSGLGFPVE 158
Cdd:PRK10247 73 -TLKPE-----IYRQQV-----------------SYCAQTPTLFGDtvYDNLIFPWQIRNQQPDPAIFLDDLERFALPDT 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 159 THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLT----WLEQYLQGYPGAILIVSHDR 223
Cdd:PRK10247 130 ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDK 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-238 |
2.87e-11 |
|
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: 63.26 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 10 SKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKdvSIGYLAQNTGLEtSLTIWDEMLt 89
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQ-NGTIRENIL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 90 vfthlqqmetklrrleqeMGKEEnfsNEATYER------LLADYDQLqlnykdQGGYQYEADIRSIlsglgfpvethqtt 163
Cdd:cd03250 88 ------------------FGKPF---DEERYEKvikacaLEPDLEIL------PDGDLTEIGEKGI-------------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 164 isTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWL-EQYLQGY---PGAILIVSHDRYFLDKlVTQVYEISN 238
Cdd:cd03250 127 --NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
331-517 |
2.93e-11 |
|
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: 63.45 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS------VGYYDQEQA 403
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDiaarnrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 nLTSSKRV------LNELWDEYPLQPEKEIRTILGNFLFtGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03269 81 -LYPKMKVidqlvyLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 478 LDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-492 |
3.37e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSVG---YYDQ----- 400
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRQrdeYHQDllylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 401 EQA----------NLTSSKRVLNELWDEyplqpekEIRTILGNFLFTG-DDVlkPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK13538 81 HQPgikteltaleNLRFYQRLHGPGDDE-------ALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|...
gi 446524801 470 ILDEPTNHLDLNSKEILEnALID 492
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLE-ALLA 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-200 |
3.65e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 65.83 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIK--PKDV--SIGYLAQNTGLETSlt 82
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIvgiwpptSGSVRLDGADLKQwdRETFgkHIGYLPQDVELFPG-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 iwdemlTVFTHLQQMEtklrrleqemgkeENFSNEATYERL-LADYDQLQLNYKDQggyqYEADIrsilsGLGFpvethq 161
Cdd:TIGR01842 407 ------TVAENIARFG-------------ENADPEKIIEAAkLAGVHELILRLPDG----YDTVI-----GPGG------ 452
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524801 162 ttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:TIGR01842 453 ---ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-490 |
4.52e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD--GGEIikpkdvsigylaqntglets 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEI-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 ltIWDEMLTVFTHLQQMETK--------LrRLEQEMGKEEN--FSNEATYERLLaDYDQLQLNYKdqggyqyeadirSIL 150
Cdd:PRK13549 65 --IFEGEELQASNIRDTERAgiaiihqeL-ALVKELSVLENifLGNEITPGGIM-DYDAMYLRAQ------------KLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSHdryfld 227
Cdd:PRK13549 129 AQLKLDINPA-TPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 228 KLvTQVYEISnkesrrfvgnyskyldlksalyeqemkryekqqDEIAKLEDfvQKNIArastTKRAQsrrkQLDRMELLT 307
Cdd:PRK13549 202 KL-NEVKAIS---------------------------------DTICVIRD--GRHIG----TRPAA----GMTEDDIIT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 308 RPLGDSKSASFHfDIEKQSGNDVLQVNDATIGYDENP---IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP--- 381
Cdd:PRK13549 238 MMVGRELTALYP-REPHTIGEVILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrw 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 382 ----LLNG------------------------------DVSFGSNVSVGYYDQeqanlTSSKRVLNElwdeyplqpEKEI 427
Cdd:PRK13549 317 egeiFIDGkpvkirnpqqaiaqgiamvpedrkrdgivpVMGVGKNITLAALDR-----FTGGSRIDD---------AAEL 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 428 RTILgnflfTGDDVLK--------PVSSLSGG--QKArlALAKLMMQKSNLLILDEPTNHLDLNSK-EI--LENAL 490
Cdd:PRK13549 383 KTIL-----ESIQRLKvktaspelAIARLSGGnqQKA--VLAKCLLLNPKILILDEPTRGIDVGAKyEIykLINQL 451
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
331-516 |
4.67e-11 |
|
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: 62.60 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSvALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS---------VGYYDQ 400
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 401 E---QANLTSSKRV-----LNELWDEyplQPEKEIRTILGNfLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:cd03264 80 EfgvYPNFTVREFLdyiawLKGIPSK---EVKARVDEVLEL-VNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524801 473 EPTNHLDLNSKEILENALIDypgtllfVSHDRYFInrVTTTVVE 516
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSE-------LGEDRIVI--LSTHIVE 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
331-503 |
4.83e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.24 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIieHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLTSSKR 410
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN--------GQDLTALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNELWDEYPLQP----------------------EKEIRTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNL 468
Cdd:COG3840 72 PVSMLFQENNLFPhltvaqniglglrpglkltaeqRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 469 LILDEPTNHLDLNSK-EILenALID-----YPGTLLFVSHD 503
Cdd:COG3840 151 LLLDEPFSALDPALRqEML--DLVDelcreRGLTVLMVTHD 189
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-200 |
5.17e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.19 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 10 SKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIKPKdVSIGYLAQNTGLETslt 82
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVNDPK-VDERLIRQEAGMVF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 iwdEMLTVFTHLQQME------TKLRRleqeMGKEENfsneatyerlladydqlqlnykdqggyqyEADIRSILSGLGFP 156
Cdd:PRK09493 84 ---QQFYLFPHLTALEnvmfgpLRVRG----ASKEEA-----------------------------EKQARELLAKVGLA 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524801 157 VETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK09493 128 ERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
331-503 |
5.38e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNG-DVSFGSNVSVGyydqeQANLTSSK 409
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-------LLAGlETPSAGELLAG-----TAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPLQPEKEIRTILGNFLfTGD------DVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNVGLGL-KGQwrdaalQALAAVgladranewpAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 446524801 474 PTNHLD----LNSKEILENALIDYPGTLLFVSHD 503
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-201 |
5.57e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.53 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYG-AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYL 71
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIlLNGFSLKdidrhtlrqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSlTIWDEMLtvfthlqqmetklrrleqeMGKEENFSNEATYERL-LADYDqlqlnykdqggyqyeADIRSIL 150
Cdd:TIGR01193 554 PQEPYIFSG-SILENLL-------------------LGAKENVSQDEIWAACeIAEIK---------------DDIENMP 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 151 SGLGFPVETHQTTIStlsGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:TIGR01193 599 LGYQTELSEEGSSIS---GGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-222 |
5.72e-11 |
|
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: 63.02 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQN 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlLDGKDITnlpphkrpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 75 TGLETSLTIWDEMltvfthlqQMETKLRRLEQEMGKEEnfsneatYERLLadyDQLQLnykdqGGYQYEadirsilsglg 154
Cdd:cd03300 81 YALFPHLTVFENI--------AFGLRLKKLPKAEIKER-------VAEAL---DLVQL-----EGYANR----------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 155 fpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLE---QYLQGYPG-AILIVSHD 222
Cdd:cd03300 127 --------KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
360-509 |
5.83e-11 |
|
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: 62.24 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 360 ALVGPNGIGKSTLLKSIvnkLPLLNGDVSFGSNVSVGYYD--QEQANLTSSKRVLNELWDEyPLQPEKEIRtILGNFLFT 437
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL---KYALTGELPPNSKGGAHDPKliREGEVRAQVKLAFENANGK-KYTITRSLA-ILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 438 -GDDVLKP----VSSLSGGQKA------RLALAKLMMQKSNLLILDEPTNHLDLNSK-----EILENALIDYPGTLLFVS 501
Cdd:cd03240 101 hQGESNWPlldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeeslaEIIEERKSQKNFQLIVIT 180
|
....*...
gi 446524801 502 HDRYFINR 509
Cdd:cd03240 181 HDEELVDA 188
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
353-515 |
6.18e-11 |
|
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: 63.20 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 353 LTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgSNVSVGYYDQE-QANLTSSKRVLnelwdeyplqpEKEIRTIL 431
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYiKADYEGTVRDL-----------LSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 432 GNFLFTGDDVLKP----------VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS--------KEILENAlidy 493
Cdd:cd03237 90 YTHPYFKTEIAKPlqieqildreVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmaskviRRFAENN---- 165
|
170 180
....*....|....*....|..
gi 446524801 494 PGTLLFVSHDRYFINRVTTTVV 515
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLI 187
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-83 |
7.34e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.79 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MIllQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKD----VS 67
Cdd:COG4604 1 MI--EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvatTPSRElakrLA 78
|
90
....*....|....*.
gi 446524801 68 IgyLAQNTGLETSLTI 83
Cdd:COG4604 79 I--LRQENHINSRLTV 92
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-233 |
7.40e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNtgl 77
Cdd:PRK11629 4 ILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI--------FNGQP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 78 etsltiwdemltvfthLQQMET----KLRrlEQEMGKEENFSNeatyerLLADYDQLQ-------LNYKDQGGYQYEAdi 146
Cdd:PRK11629 73 ----------------MSKLSSaakaELR--NQKLGFIYQFHH------LLPDFTALEnvampllIGKKKPAEINSRA-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 147 RSILSGLGFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL------QGypGAILIVS 220
Cdd:PRK11629 127 LEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgelnrlQG--TAFLVVT 203
|
250
....*....|...
gi 446524801 221 HDRYFLDKLVTQV 233
Cdd:PRK11629 204 HDLQLAKRMSRQL 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
330-509 |
8.66e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS------------VG 396
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlctyqkqlcfVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 397 YYDQEQANLTSSKrvlNELWDEYPLQPEKEIRTILGnfLFTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PRK13540 81 HRSGINPYLTLRE---NCLYDIHFSPGAVGITELCR--LFSLEHLIDyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524801 476 NHLDLNSKEILENALIDYP---GTLLFVSHDRYFINR 509
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
9.99e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----------I 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiIDDEDISllplhararrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 69 GYLAQNTGLETSLTIWDEMLTVFthlqQMETKLRRLEQEMGKEEnfsneatyerLLADYdqlqlnykdqggyqyeaDIRS 148
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVL----QIRDDLSAEQREDRANE----------LMEEF-----------------HIEH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 149 ILSGLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDE------PTNHLDIETLTwleQYLQGYPGAILIVSHD 222
Cdd:PRK10895 130 LRDSMG----------QSLSGGERRRVEIARALAANPKFILLDEpfagvdPISVIDIKRII---EHLRDSGLGVLITDHN 196
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-200 |
1.05e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIaGELSHDGGEIIKPKDVSIgylaqNTGlets 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAGTIRVGDITI-----DTA---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 ltiwdemltvfTHLQQMETKLRRLEQEMG-KEENFsNEATYERLLADYDQLQLNYKDQGGYQYEADIRSILSGLGFPVEt 159
Cdd:PRK11264 71 -----------RSLSQQKGLIRQLRQHVGfVFQNF-NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 160 HQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK11264 138 ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
155-503 |
1.28e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 155 FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHDRYFLDKLV 230
Cdd:PRK15134 153 YP---HQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 231 TQVYEISNKESrrfvgnyskyldlksalyeqemkryekqqdeiakledfVQKNIARASTTKRAQSRRKQLdrmeLLTRPL 310
Cdd:PRK15134 225 DRVAVMQNGRC--------------------------------------VEQNRAATLFSAPTHPYTQKL----LNSEPS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 311 GDSKSASfhfdiekQSGNDVLQVNDATIGY-----------DENPIIEHVTMRLTRGDSVALVGPNGIGKST----LLKS 375
Cdd:PRK15134 263 GDPVPLP-------EPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 376 I-------VNKLPLLNGD----VSFGSNVSVGYYDQEQA---NLTSSKRVLNELWDEYPL----QPEKEIRTILGNFLFT 437
Cdd:PRK15134 336 InsqgeiwFDGQPLHNLNrrqlLPVRHRIQVVFQDPNSSlnpRLNVLQIIEEGLRVHQPTlsaaQREQQVIAVMEEVGLD 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 438 GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN-SKEILenALI-----DYPGTLLFVSHD 503
Cdd:PRK15134 416 PETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTvQAQIL--ALLkslqqKHQLAYLFISHD 485
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-237 |
1.34e-10 |
|
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: 61.96 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----IKPKDVSIGYLAQNT---GLETSLtIWDemltvf 91
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRRIGvvfGQKTQL-WWD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 92 thLQQMETklRRLEQEMGKEENFSNEATYERLLadyDQLqlnykdqggyqyeaDIRSILsglgfpvethQTTISTLSGGQ 171
Cdd:cd03267 110 --LPVIDS--FYLLAAIYDLPPARFKKRLDELS---ELL--------------DLEELL----------DTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 172 KTRLALGKLLLTKPDLLILDEPTNHLDI---ETL-TWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEIS 237
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIrNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-199 |
1.38e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.71 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS------IGYLAQ 73
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlVAGDDVEalsaraASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTiwdemltvfthlqqMETKLRRLeQEMGKEENFSNEATYErlladydqlqlnykdqggyqyEADIRSILSGL 153
Cdd:PRK09536 81 SVPQDTSLS--------------FEFDVRQV-VEMGRTPHRSRFDTWT---------------------ETDRAAVERAM 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 154 GfPVETHQ---TTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK09536 125 E-RTGVAQfadRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
355-487 |
1.41e-10 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 61.93 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 355 RGDSVALVGPNGIGKSTLLKSIvNKLPLLN-GDVSF-GSNV-------------SVGYYDQeQANLTSSKRVL-NELWDE 418
Cdd:TIGR02315 27 PGEFVAIIGPSGAGKSTLLRCI-NRLVEPSsGSILLeGTDItklrgkklrklrrRIGMIFQ-HYNLIERLTVLeNVLHGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 419 ypLQPEKEIRTILGnfLFTGDD----------------VLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LN 481
Cdd:TIGR02315 105 --LGYKPTWRSLLG--RFSEEDkeralsalervgladkAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDpKT 180
|
....*.
gi 446524801 482 SKEILE 487
Cdd:TIGR02315 181 SKQVMD 186
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
331-503 |
1.47e-10 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 61.68 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNG-DVS--------------- 388
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGeDITglppheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 389 ------FGS-----NVSVGYYDQEQANLTSSKRVlnelwdeyplQPEKEIRTILGNFL-FTG-DDVL-KPVSSLSGGQKA 454
Cdd:cd03219 81 fqiprlFPEltvleNVMVAAQARTGSGLLLARAR----------REEREARERAEELLeRVGlADLAdRPAGELSYGQQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 455 RLALAKLMMQKSNLLILDEPTNhlDLNSKEIleNALIDY------PG-TLLFVSHD 503
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAA--GLNPEET--EELAELirelreRGiTVLLVEHD 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-233 |
1.59e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.37 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQNTGLetsltiwdemltVFt 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvdITDKKVKLSDIRKKVGL------------VF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 93 hlQQMETKLrrLEQEMGKEENF-------SNEATYERLLADYDQLQLNY---KDQGgyqyeadirsilsglgfPVEthqt 162
Cdd:PRK13637 90 --QYPEYQL--FEETIEKDIAFgpinlglSEEEIENRVKRAMNIVGLDYedyKDKS-----------------PFE---- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 163 tistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQV 233
Cdd:PRK13637 145 ----LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRI 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-222 |
1.59e-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: 61.71 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG-ELSHDGGEIIKPKDVSIG-----YLAQNTGLETSLTIWDEM-LTVF 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQITEPgpdrmVVFQNYSLLPWLTVRENIaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 92 THLQQMetklRRLEQEMGKEENFsneatyerlladydqlqlnykDQGGYQYEADIRsilsglgfpvethqttISTLSGGQ 171
Cdd:TIGR01184 81 RVLPDL----SKSERRAIVEEHI---------------------ALVGLTEAADKR----------------PGQLSGGM 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 172 KTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:TIGR01184 120 KQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-230 |
1.68e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAgelshdggEIIKPKDvsigylaqntgleTSLTI 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--------RLLTPQS-------------GTVFL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMLTVFTHlQQMETKLRRLEQEMGKEENFSneatyERLLADYDQL-------QLNYKDQGGYQYEADIRSIlsglgfp 156
Cdd:PRK11231 62 GDKPISMLSS-RQLARRLALLPQHHLTPEGIT-----VRELVAYGRSpwlslwgRLSAEDNARVNQAMEQTRI------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 157 VETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHD-----RYfLDK 228
Cdd:PRK11231 129 NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDlnqasRY-CDH 207
|
..
gi 446524801 229 LV 230
Cdd:PRK11231 208 LV 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-502 |
1.79e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS------------VGY 397
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPararlararigvVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 398 YDQEQANLTSSKRVLneLWDEYPLQPEKEIRTILGNFL-FT--GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:PRK13536 122 FDNLDLEFTVRENLL--VFGRYFGMSTREIEAVIPSLLeFArlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190
....*....|....*....|....*....|.
gi 446524801 475 TNHLDLNSKE-ILE--NALIDYPGTLLFVSH 502
Cdd:PRK13536 200 TTGLDPHARHlIWErlRSLLARGKTILLTTH 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-503 |
1.83e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.17 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSN-------------VSV 395
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 396 GYYDQEQANLTSSKRVLNEL-WDEYPLQ-PEKEIRTILGNFLF-TGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVsFGAVNLKlPEDEVRKRVDNALKrTGIEHLkdKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524801 471 LDEPTNHLD-LNSKEILENALIDYPG---TLLFVSHD 503
Cdd:PRK13636 165 LDEPTAGLDpMGVSEIMKLLVEMQKElglTIIIATHD 201
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-222 |
1.98e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.96 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD---GGEI---------IKPKDVSIGYL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVllngrrltaLPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLTIWDEMLtvfthlqqmetklrrleqeMGKEENFSNEATYERLLADYDQLQLnykdqgGYQYEADIrsils 151
Cdd:COG4136 82 FQDDLLFPHLSVGENLA-------------------FALPPTIGRAQRRARVEQALEEAGL------AGFADRDP----- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 152 glgfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:COG4136 132 -------------ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
330-502 |
1.99e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLLNGDVSFgsnvsVGYYDQEQANLTSSK 409
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTI-----TGSIVYNGHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPL---QPEKEIRTILGNFLF-----------TGDDV----LKPVS--------------SLSGGQKARLA 457
Cdd:PRK14239 79 TDTVDLRKEIGMvfqQPNPFPMSIYENVVYglrlkgikdkqVLDEAveksLKGASiwdevkdrlhdsalGLSGGQQQRVC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 458 LAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYpgTLLFVSH 502
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLglkdDY--TMLLVTR 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
331-514 |
2.00e-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: 61.48 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYD-ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnkLPLLNGDVSFGSnVSVGYYDQEQANLTSSK 409
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-----LLFRFYDVSSGS-ILIDGQDIREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVL------NELWDEyplqpekeirTILGNFLF-----TGDDVLKPVSS------------------------LSGGQKA 454
Cdd:cd03253 75 RAIgvvpqdTVLFND----------TIGYNIRYgrpdaTDEEVIEAAKAaqihdkimrfpdgydtivgerglkLSGGEKQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHdryfinRVTTTV 514
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH------RLSTIV 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
342-502 |
2.03e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.97 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKST---LLK-----------------------------SIVNKLPLLNGDvSF 389
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQnlyqptggqvlldgvplvqydhhylhrqvALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 390 GSNVSVGYYDQEQANLTSSKRVLNElwDEYPLQPEKEIRTILGNflfTGddvlkpvSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAKAANA--HDFIMEFPNGYDTEVGE---KG-------SQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190
....*....|....*....|....*....|...
gi 446524801 470 ILDEPTNHLDLNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR00958 640 ILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-210 |
2.07e-10 |
|
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: 61.09 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVS-------IGYLAQNTGLETSlti 83
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGHDV---RDYTlaslrrqIGLVSQDVFLFND--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 wdemlTVFthlqqmetklrrleqemgkeENFsneaTYERLLADYDQLQLNYKDQGGYQYeadIRSILSGLgfpvethQTT 163
Cdd:cd03251 91 -----TVA--------------------ENI----AYGRPGATREEVEEAARAANAHEF---IMELPEGY-------DTV 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 164 I----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQ 210
Cdd:cd03251 132 IgergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES----ERLVQ 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-211 |
2.19e-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: 61.09 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDV-------SIGYLAQNTGLETSlTI 83
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDGQDI---REVtldslrrAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMltvfthlqqmetklrrleqEMGKEeNFSNEATYE-RLLADYDQLQLNYKDqgGYQYEADIRsilsGLgfpvethqt 162
Cdd:cd03253 92 GYNI-------------------RYGRP-DATDEEVIEaAKAAQIHDKIMRFPD--GYDTIVGER----GL--------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 163 tisTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQG 211
Cdd:cd03253 137 ---KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT----EREIQA 178
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-222 |
2.25e-10 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 61.37 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 33 ALVGRNGAGKSTLLKIIAGELSHDGGEII-----------KPKDVSIGYLAQNTGLETSLTIWDEMLTvfthlqqMETKL 101
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVEQDSDTAVPLTVRDVVAL-------GRIPH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 102 RRLeqeMGKEENFSNEATyERLLADYDQLQLnykdqggyqyeADirsilsglgfpvethqTTISTLSGGQKTRLALGKLL 181
Cdd:TIGR03873 104 RSL---WAGDSPHDAAVV-DRALARTELSHL-----------AD----------------RDMSTLSGGERQRVHVARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 182 LTKPDLLILDEPTNHLDI----ETLTWLEQyLQGYPGAILIVSHD 222
Cdd:TIGR03873 153 AQEPKLLLLDEPTNHLDVraqlETLALVRE-LAATGVTVVAALHD 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
324-577 |
2.27e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 324 KQSGNDVLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSvgyYDQE 401
Cdd:TIGR00957 630 KPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA---YVPQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKRVLNELWDeYPLQPEKEIRTILG-------NFLFTGD--DVLKPVSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:TIGR00957 707 QAWIQNDSLRENILFG-KALNEKYYQQVLEAcallpdlEILPSGDrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 473 EPTNHLDLN-SKEILENaLIDYPGTL-----LFVSHDRYFINRVTTTVVelSTEGAQEYLGDYDYYVEKKNEMIE----- 541
Cdd:TIGR00957 786 DPLSAVDAHvGKHIFEH-VIGPEGVLknktrILVTHGISYLPQVDVIIV--MSGGKISEMGSYQELLQRDGAFAEflrty 862
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446524801 542 -RAELEQQESDVPVQKVVAQEKLNYLEEKE-------RKQLERQ 577
Cdd:TIGR00957 863 aPDEQQGHLEDSWTALVSGEGKEAKLIENGmlvtdvvGKQLQRQ 906
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-229 |
2.63e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigyLAQntgleTS 80
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL---------LNG-----QP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDE-----MLTVFT---HLqqMETKLRrleqemgkeENF---SNEATYERLLADYDQLQLNYKDQGgyqyEADIRSI 149
Cdd:PRK11160 404 IADYSEaalrqAISVVSqrvHL--FSATLR---------DNLllaAPNASDEALIEVLQQVGLEKLLED----DKGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 150 LSGLGFPvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGypGAILIVSHDRYF 225
Cdd:PRK11160 469 LGEGGRQ----------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITHRLTG 536
|
....
gi 446524801 226 LDKL 229
Cdd:PRK11160 537 LEQF 540
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-221 |
2.64e-10 |
|
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: 63.20 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETI--LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDEML---TVFTHLqqmetKLRRLEQemgkeenfSNEATYERLLADYDQLQLnykdqggyqyeadIRSILSGLGFPV 157
Cdd:TIGR02203 410 LVSQDVVLfndTIANNI-----AYGRTEQ--------ADRAEIERALAAAYAQDF-------------VDKLPLGLDTPI 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 158 ETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGaiLIVSH 221
Cdd:TIGR02203 464 GENG---VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTT--LVIAH 526
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
342-490 |
3.23e-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: 60.63 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYYDQEQANLTSSKR 410
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VlNELWDEYPLQPEKEIRTI----LGNFLFT----GDDVLKPV-SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:cd03249 95 E-NIRYGKPDATDEEVEEAAkkanIHDFIMSlpdgYDTLVGERgSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
....*....
gi 446524801 482 SKEILENAL 490
Cdd:cd03249 174 SEKLVQEAL 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
3.32e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.03 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGY 70
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLETsltiWdemLTVfthLQQMETKLRRleQEMGKEENfsnEATYERLLAdydqlqlnykdqggyqyeadirsiL 150
Cdd:COG4525 81 VFQKDALLP----W---LNV---LDNVAFGLRL--RGVPKAER---RARAEELLA------------------------L 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 151 SGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG4525 122 VGLA---DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
331-503 |
3.34e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 60.46 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGD-VSFGSNV---------SVGYYDQ 400
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 401 EQA---------NLTSSKRVLNELWDEYplqpEKEIRTILgNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03265 81 DLSvddeltgweNLYIHARLYGVPGAER----RERIDELL-DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 446524801 472 DEPTNHLDLNSK----EILENALIDYPGTLLFVSHD 503
Cdd:cd03265 156 DEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHY 191
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
331-518 |
3.41e-10 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 60.26 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIieHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLTSSKR 410
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVN--------DQSHTGLAPYQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNELWDEYPLQPEKEIRTILGNFLFTG--------------------DDVLKPV-SSLSGGQKARLALAKLMMQKSNLL 469
Cdd:TIGR01277 71 PVSMLFQENNLFAHLTVRQNIGLGLHPGlklnaeqqekvvdaaqqvgiADYLDRLpEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 470 ILDEPTNHLD-LNSKEILenALI-----DYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:TIGR01277 151 LLDEPFSALDpLLREEML--ALVkqlcsERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-221 |
3.42e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 21 NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQNTGLetsltiwd 85
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvlfdaekgicLPPEKRRIGYVFQDARL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 86 emltvFTHlqqmetklrrleqemgkeenfsneatyerlladydqlqlnYKDQGGYQY------EADIRSILSGLG----- 154
Cdd:PRK11144 88 -----FPH----------------------------------------YKVRGNLRYgmaksmVAQFDKIVALLGiepll 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 155 --FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSH 221
Cdd:PRK11144 123 drYP--------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-229 |
3.46e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 32 IALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvSIGYLAQNTGLETSLTIwDEMLtvfthlqqmetklrrleqeMGKE 111
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTV-RDLL-------------------SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 112 ENFSNEATYERLLADYDQLQLNYKDQggyqyeadirsilsglgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILD 191
Cdd:cd03237 87 KDFYTHPYFKTEIAKPLQIEQILDRE--------------------------VPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 192 EPTNHLDIE----TLTWLEQYLQGYPGAILIVSHDRYFLDKL 229
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYL 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
339-517 |
3.51e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.87 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 339 GYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNGDVSFGSNVSVGYydqeQANLT------ 406
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsgrvEVNGRVSALLELGAGF----HPELTgreniy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 407 SSKRVLNelwdeyplQPEKEIRTI---------LGNFLFTgddvlkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:COG1134 111 LNGRLLG--------LSRKEIDEKfdeivefaeLGDFIDQ------PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524801 478 LDLN----SKEILENaLIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG1134 177 GDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
335-526 |
4.11e-10 |
|
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: 62.81 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 335 DATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLlksiVNKLP----------LLNGD-------------VSF-G 390
Cdd:TIGR02203 337 TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL----VNLIPrfyepdsgqiLLDGHdladytlaslrrqVALvS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 391 SNV---------SVGYYDQEQANLTSSKRVL-----NELWDEYPLQPEKEIrtilgnflftGDDVlkpvSSLSGGQKARL 456
Cdd:TIGR02203 413 QDVvlfndtianNIAYGRTEQADRAEIERALaaayaQDFVDKLPLGLDTPI----------GENG----VLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLDLNSKEILENALidypgtllfvshDRYFINRvTTTVV--ELST-EGAQEYL 526
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAAL------------ERLMQGR-TTLVIahRLSTiEKADRIV 538
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-198 |
4.44e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----------IKPKDVSIGYLAQ 73
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpsrARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLETSLTIwDEMLTVFthlqqmetklrrleqemGKEENFSNEATYERL--LADYDQLQlnykdqggyqYEADIRsils 151
Cdd:PRK13537 88 FDNLDPDFTV-RENLLVF-----------------GRYFGLSAAAARALVppLLEFAKLE----------NKADAK---- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 152 glgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13537 136 ------------VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
321-517 |
4.54e-10 |
|
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: 59.73 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 321 DIEKQSGNDVLQVNDatigydenpiiehVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSvGYYD 399
Cdd:cd03292 5 NVTKTYPNGTAALDG-------------INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVS-DLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QEQANLtssKRVLNELWDEYPLQPEkeiRTILGNFLFT-------GDDVLKPVSS-----------------LSGGQKAR 455
Cdd:cd03292 71 RAIPYL---RRKIGVVFQDFRLLPD---RNVYENVAFAlevtgvpPREIRKRVPAalelvglshkhralpaeLSGGEQQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLDL-NSKEILE--NALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPdTTWEIMNllKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
328-508 |
4.56e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDatIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS---------- 394
Cdd:PRK10247 5 SPLLQLQN--VGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIStlkpeiyrqq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQEQANLTSSkrVLNEL---WDEYPLQPE-KEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:PRK10247 83 VSYCAQTPTLFGDT--VYDNLifpWQIRNQQPDpAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 471 LDEPTNHLDLNSK----EILENALIDYPGTLLFVSHDRYFIN 508
Cdd:PRK10247 161 LDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEIN 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-502 |
4.60e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 349 VTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP-----LLNG----DVSFGS---------------------NVSVGYY 398
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGielrELDPESwrkhlswvgqnpqlphgtlrdNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 D--QEQANLTSSKRVLNELWDEYPLQPEKEIrtilgnflftGDDVlkpvSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:PRK11174 449 DasDEQLQQALENAWVSEFLPLLPQGLDTPI----------GDQA----AGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180
....*....|....*....|....*...
gi 446524801 477 HLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRrqTTLMVTH 542
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
331-479 |
4.62e-10 |
|
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: 59.85 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKL-PLLNGDVSFgsnvsvgyydqEQANLTSSK 409
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTIII-----------DGLKLTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDE-------YPLQPEKeirTILGNFLF---------------TGDDVLKPV----------SSLSGGQKARLA 457
Cdd:cd03262 69 KNINELRQKvgmvfqqFNLFPHL---TVLENITLapikvkgmskaeaeeRALELLEKVgladkadaypAQLSGGQQQRVA 145
|
170 180
....*....|....*....|..
gi 446524801 458 LAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALD 167
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
330-504 |
4.74e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSnvsvgyydQEQANLTSSK 409
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--------VDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDEYPLQP----EKEIRTILGNFLFTGDDVLKPVS-----------------SLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK11607 91 RPINMMFQSYALFPhmtvEQNIAFGLKQDKLPKAEIASRVNemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 469 LILDEPTNHLDLNSKEILENALID----YPGTLLFVSHDR 504
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDilerVGVTCVMVTHDQ 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-230 |
4.84e-10 |
|
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: 60.59 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY---------GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGelshdggeIIKPKDVSIGYLAQ 73
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG--------LEKPAQGTVSFRGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NtgletsltiwdemltvFTHLQQMETKLRRLEQEMGKEENFSN---EATYERLLADYDQlqlNYKDQGGYQYEADIRSIL 150
Cdd:TIGR02769 74 D----------------LYQLDRKQRRAFRRDVQLVFQDSPSAvnpRMTVRQIIGEPLR---HLTSLDESEQKARIAELL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD---- 222
Cdd:TIGR02769 135 DMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDlrlv 214
|
....*...
gi 446524801 223 RYFLDKLV 230
Cdd:TIGR02769 215 QSFCQRVA 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-233 |
5.37e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.46 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGelsHDGGEIIKPKdvsIGYlaqntgletslti 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKYEVTEGE---ILF------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 wdemltvfthlqqmetklrrleqemgKEENFSNEATYERLLAdydqlqlnykdqG---GYQYEADI---------RSIls 151
Cdd:cd03217 62 --------------------------KGEDITDLPPEERARL------------GiflAFQYPPEIpgvknadflRYV-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 152 GLGFpvethqttistlSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ---YLQGYPGAILIVSHDRYFLDK 228
Cdd:cd03217 102 NEGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDY 169
|
....*
gi 446524801 229 LVTQV 233
Cdd:cd03217 170 IKPDR 174
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-518 |
6.03e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS----------VGYY 398
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATrgdrsrfmayLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQEQANLTSSKRV--LNELWDEYPLQPEKEIRTILGnfLFTGDDVLkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:PRK13543 91 PGLKADLSTLENLhfLCGLHGRRAKQMPGSALAIVG--LAGYEDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 477 HLDLNSKEILENAL---IDYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK13543 167 NLDLEGITLVNRMIsahLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-503 |
6.45e-10 |
|
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: 60.54 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNGDV--SFGSnVSVGYYDQEqanlTSSKRVLNELWDEY 419
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQ-------HLNGLLkpTSGT-VTIDGRDIT----AKKKKKLKDLRKKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 420 PL---QPEKEI--RTIL-------GNFLFTGDDVLKPVS------------------SLSGGQKARLALAKLMMQKSNLL 469
Cdd:TIGR04521 85 GLvfqFPEHQLfeETVYkdiafgpKNLGLSEEEAEERVKealelvgldeeylerspfELSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 470 ILDEPTNHLDLNS-KEILEnaLID-----YPGTLLFVSHD 503
Cdd:TIGR04521 165 ILDEPTAGLDPKGrKEILD--LFKrlhkeKGLTVILVTHS 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
347-502 |
6.58e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.60 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 347 EHVTMRLT----RGDSVALVGPNGIGKSTLLKSIVNKLP------LLNGdvsfgsnvsvgyydQEQANLTSSKRVLNELW 416
Cdd:PRK10771 12 HHLPMRFDltveRGERVAILGPSGAGKSTLLNLIAGFLTpasgslTLNG--------------QDHTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 417 DEYPLQPEKEIRTILGNFLFTG-----------DDVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PRK10771 78 QENNLFSHLTVAQNIGLGLNPGlklnaaqreklHAIARQMgiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 446524801 476 NHLD--LNSK--EILENALIDYPGTLLFVSH 502
Cdd:PRK10771 158 SALDpaLRQEmlTLVSQVCQERQLTLLMVSH 188
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
331-479 |
6.74e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.42 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPllnGDVSFGSNVSVGyyDQEQANLTSSKR 410
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS---PAFSASGEVLLN--GRRLTALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNELWDEYPLQPEkeiRTILGNFLF-------------TGDDVL----------KPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:COG4136 77 RIGILFQDDLLFPH---LSVGENLAFalpptigraqrraRVEQALeeaglagfadRDPATLSGGQRARVALLRALLAEPR 153
|
170
....*....|..
gi 446524801 468 LLILDEPTNHLD 479
Cdd:COG4136 154 ALLLDEPFSKLD 165
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-479 |
6.84e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 339 GYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPL---LNGDVSFGsnvsvGYYDQEQANLTSSKRVLNEL 415
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYN-----GIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 416 WDEYPlqPEKEIR-TILGNFLFTGDDVlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03233 91 EDVHF--PTLTVReTLDFALRCKGNEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
359-517 |
7.64e-10 |
|
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: 60.90 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 359 VALVGPNGIGKSTLLKSIVNKLPL------LNGDVSFGSNV---------SVGYYDQEqANL---TSSKRVLNE-LWD-- 417
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPdegeivLNGRTLFDSRKgiflppekrRIGYVFQE-ARLfphLSVRGNLRYgMKRar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 418 -EYPLQPEKEIRTILGnflfTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI---LEN--AL 490
Cdd:TIGR02142 105 pSERRISFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKyEIlpyLERlhAE 180
|
170 180
....*....|....*....|....*..
gi 446524801 491 IDYPgtLLFVSHDRYFINRVTTTVVEL 517
Cdd:TIGR02142 181 FGIP--ILYVSHSLQEVLRLADRVVVL 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-201 |
8.57e-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: 59.16 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----IKPKDVS-------IGYLAQNTGLeTSLTIWDE 86
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgIDIRDISrkslrsmIGVVLQDTFL-FSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 87 MLtvfthlqqmetklrrleqeMGKeenfsNEATYERLLADYDQLQLNY---KDQGGYQYEADIRSilsglgfpvethqtt 163
Cdd:cd03254 97 IR-------------------LGR-----PNATDEEVIEAAKEAGAHDfimKLPNGYDTVLGENG--------------- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524801 164 iSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03254 138 -GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-227 |
8.75e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGaetilaNIKLEVQ-----TKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpkDVSIGYLAQNTg 76
Cdd:PRK13409 339 TLVEYPDLTKKLG------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYI- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 letsltiwdemltvfthlqqmetklrRLEQEMGKEENFSNEAtyerlladyDQLQLNYkdqggYQYEadirsILSGLGFP 156
Cdd:PRK13409 410 --------------------------KPDYDGTVEDLLRSIT---------DDLGSSY-----YKSE-----IIKPLQLE 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 157 vETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE----TLTWLEQYLQGYPGAILIVSHDRYFLD 227
Cdd:PRK13409 445 -RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMID 518
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
340-503 |
1.12e-09 |
|
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: 59.17 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLTSSKRVLNELWDEY 419
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------GKDITNLPPHKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 420 PLQP------------------EKEIR---------TILGNFLFtgddvlKPVSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:cd03300 82 ALFPhltvfeniafglrlkklpKAEIKervaealdlVQLEGYAN------RKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 446524801 473 EPTNHLDLNSKEILE---NALIDYPG-TLLFVSHD 503
Cdd:cd03300 156 EPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
340-474 |
1.56e-09 |
|
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: 58.71 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSN------------VSVGYYDQEQA---N 404
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLPQEASifrK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 405 LTSSKRVLNELwdEYPLQPEKEIRTILGNFL--FTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:cd03218 90 LTVEENILAVL--EIRGLSKKEREEKLEELLeeFHITHLRKsKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-201 |
1.72e-09 |
|
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: 58.60 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigYLAQntgle 78
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV---------RLAG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 TSLTIWDE----------MLTVFTHLQQMETkLRRLEQEM------GKEENFsneATYERLLADYdqlqlnykdqggyqy 142
Cdd:COG4181 74 QDLFALDEdararlrarhVGFVFQSFQLLPT-LTALENVMlplelaGRRDAR---ARARALLERV--------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 143 eadirsilsGLG-----FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG4181 135 ---------GLGhrldhYP--------AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
331-503 |
1.81e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGydenPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLlNGDVSF-GSNVSV----------GYYD 399
Cdd:PRK03695 1 MQLNDVAVS----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEAwsaaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QEQ-------------------ANLTSSKRVLNELwdeyplqpekeirtilGNFLFTGDDVLKPVSSLSGGQKARLALAK 460
Cdd:PRK03695 76 QQQtppfampvfqyltlhqpdkTRTEAVASALNEV----------------AEALGLDDKLGRSVNQLSGGEWQRVRLAA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 461 LMMQ-------KSNLLILDEPTNHLDLNSKEILE---NALIDYPGTLLFVSHD 503
Cdd:PRK03695 140 VVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-479 |
1.81e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDEN--PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSnvsvgyydqeqanl 405
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 tsskRVLNE--LWDeyplqpekeIRTILGNFL------FTG----DDV---------------------LKPV------- 445
Cdd:PRK13635 69 ----MVLSEetVWD---------VRRQVGMVFqnpdnqFVGatvqDDVafglenigvpreemvervdqaLRQVgmedfln 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524801 446 ---SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13635 136 repHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
344-518 |
1.97e-09 |
|
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: 58.21 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 344 PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIV-NKLPLlNGDVSFGSNVSV-------------------GY------ 397
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYgNYLPD-SGSILVRHDGGWvdlaqaspreilalrrrtiGYvsqflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 398 -------------------YDQEQAnLTSSKRVLN------ELWDEYPlqpekeirtilGNFlftgddvlkpvsslSGGQ 452
Cdd:COG4778 104 viprvsaldvvaepllergVDREEA-RARARELLArlnlpeRLWDLPP-----------ATF--------------SGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 453 KARLALAKLMMQKSNLLILDEPTNHLDLNSK----EILENALIDypGT-LLFVSHDRYFINRVTTTVVELS 518
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR--GTaIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-221 |
1.98e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 57.89 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 24 LEVQTKDRIALVGRNGAGKSTLLKIIAG-ELSHDGGEIIKPKDVSIGYLAQNTgleTSLTIWDEmlTVFTHLQqmetklr 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPPADRP---VSMLFQEN--NLFAHLT------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 103 rLEQEMGkeenfsneatyerlLADYDQLQLNYKDQGGyqyeadIRSILSGLGFPvETHQTTISTLSGGQKTRLALGKLLL 182
Cdd:cd03298 87 -VEQNVG--------------LGLSPGLKLTAEDRQA------IEVALARVGLA-GLEKRLPGELSGGERQRVALARVLV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 183 TKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSH 221
Cdd:cd03298 145 RDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-201 |
2.00e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 5 QVNALSKLYGAE------TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELShdggeiiKPKDVSIGYLAQNTgle 78
Cdd:COG2401 26 RVAIVLEAFGVElrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------GTPVAGCVDVPDNQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 tsltiWDEMLTVFTHLqqmetklrrleqemGKEENFsNEATYerLLADydqlqlnykdqggyqyeadirsilSGLGFPVe 158
Cdd:COG2401 96 -----FGREASLIDAI--------------GRKGDF-KDAVE--LLNA------------------------VGLSDAV- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 159 THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG2401 129 LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
340-512 |
2.03e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLP------LLNGDVSF-GSNVSVGYYDQEqANLtsskrvl 412
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEeitsgdLIVDGLKVnDPKVDERLIRQE-AGM------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 413 neLWDEYPLQPEkeiRTILGNFLF---------------TGDDVLKPV----------SSLSGGQKARLALAKLMMQKSN 467
Cdd:PRK09493 82 --VFQQFYLFPH---LTALENVMFgplrvrgaskeeaekQARELLAKVglaerahhypSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 468 LLILDEPTNHLDLNSK-EILE--NALIDYPGTLLFVSHDRYFINRVTT 512
Cdd:PRK09493 157 LMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEKVAS 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-485 |
2.24e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKD---VSIGY 70
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevtfnGPKSsqeAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLETSLTIWDEMLtvfthlqqmetklrrleqeMGKEenFSNeaTYERLlaDYDQLqlnykdqggYQyEADirSIL 150
Cdd:PRK10762 84 IHQELNLIPQLTIAENIF-------------------LGRE--FVN--RFGRI--DWKKM---------YA-EAD--KLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFPVETHQtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL-DIETLTWL----EQYLQGYpgAILIVSHDryf 225
Cdd:PRK10762 127 ARLNLRFSSDK-LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFrvirELKSQGR--GIVYISHR--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 226 ldklVTQVYEISnkesrrfvgnyskyldlksalyeqemkryekqqDEIAKLED--FVqkniarasttkrAQSRRKQLDRM 303
Cdd:PRK10762 201 ----LKEIFEIC---------------------------------DDVTVFRDgqFI------------AEREVADLTED 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 304 ELLTRPLGdSKSASFHFDIEKQSGNDVLQVNDATigydeNPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLL 383
Cdd:PRK10762 232 SLIEMMVG-RKLEDQYPRLDKAPGEVRLKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 384 NGDVS-FGSNVS-------------------------VGYYDQEQANLTSskrvLNELWDEYPLQPEKEIRTILGNF--L 435
Cdd:PRK10762 306 SGYVTlDGHEVVtrspqdglangivyisedrkrdglvLGMSVKENMSLTA----LRYFSRAGGSLKHADEQQAVSDFirL 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 436 F-----TGDdvlKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS-KEI 485
Cdd:PRK10762 382 FniktpSME---QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkKEI 434
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-229 |
2.57e-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: 58.53 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 34 LVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvsigylaqntgletsltiWDEMLTVF--THLQQMETKLRrleqemGKE 111
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPD------------------WDEILDEFrgSELQNYFTKLL------EGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 112 ENFSNEATYERLL-----ADYDQLqLNYKDQGGYQYEADIRSILSGLgfpVETHqttISTLSGGQKTRLALGKLLLTKPD 186
Cdd:cd03236 87 VKVIVKPQYVDLIpkavkGKVGEL-LKKKDERGKLDELVDQLELRHV---LDRN---IDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524801 187 LLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHDRYFLDKL 229
Cdd:cd03236 160 FYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYL 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
344-490 |
2.59e-09 |
|
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: 60.69 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 344 PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDV------SFGSNVS--------------VGYydqEQA 403
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgriSFSPQTSwimpgtikdniifgLSY---DEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 NLTSskrVLN--ELWDEYPLQPEKEiRTILGNFLFTgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-L 480
Cdd:TIGR01271 517 RYTS---VIKacQLEEDIALFPEKD-KTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTHLDvV 582
|
170
....*....|
gi 446524801 481 NSKEILENAL 490
Cdd:TIGR01271 583 TEKEIFESCL 592
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-198 |
2.84e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 10 SKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSIGYLAQNTGLETS 80
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndVPPAERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDEMltvfthlqQMETKLRRleqeMGKEEnfsneaTYERLLADYDQLQLNY------KDqggyqyeadirsilsglg 154
Cdd:PRK11000 90 LSVAENM--------SFGLKLAG----AKKEE------INQRVNQVAEVLQLAHlldrkpKA------------------ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524801 155 fpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11000 134 ------------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
331-503 |
2.87e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 58.12 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLTSSKR 410
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG--------GEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNELWDEYPL----------------------QPEKEIRTILGNFL-FTGDDVLK---PvSSLSGGQKARLALAKLMMQ 464
Cdd:cd03296 75 NVGFVFQHYALfrhmtvfdnvafglrvkprserPPEAEIRAKVHELLkLVQLDWLAdryP-AQLSGGQRQRVALARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 465 KSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHD 503
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRrlhdELHVTTVFVTHD 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
329-517 |
3.15e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 329 DVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQE---QANL 405
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 T-SSKRVLNelwdeypLQPEKEIRTILGNF--LFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS 482
Cdd:PRK09544 83 PlTVNRFLR-------LRPGTKKEDILPALkrVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 483 KEILENaLIDYPGT-----LLFVSHDRYFINRVTTTVVEL 517
Cdd:PRK09544 156 QVALYD-LIDQLRReldcaVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
325-474 |
3.27e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.24 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 325 QSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSV----GYYD 399
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAmsrsRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 --QEQANLTSSKRVLNEL--WDE--YPLQ-----PEKEIRTILGNFL----FTGDDVLKPvSSLSGGQKARLALAKLMMQ 464
Cdd:PRK11831 82 vrKRMSMLFQSGALFTDMnvFDNvaYPLRehtqlPAPLLHSTVMMKLeavgLRGAAKLMP-SELSGGMARRAALARAIAL 160
|
170
....*....|
gi 446524801 465 KSNLLILDEP 474
Cdd:PRK11831 161 EPDLIMFDEP 170
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-480 |
3.40e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 57.82 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNGDVSfGSNVSVGYYDQEQANLT---- 406
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLK-------LLTGELT-PSSGEVRLNGRPLAAWSpwel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 407 SSKR-VL---NEL----------------WDEYPLQPEKEIRTILGNflfTGDDVL--KPVSSLSGGQKARLALAKLMMQ 464
Cdd:COG4559 74 ARRRaVLpqhSSLafpftveevvalgrapHGSSAAQDRQIVREALAL---VGLAHLagRSYQTLSGGEQQRVQLARVLAQ 150
|
170 180
....*....|....*....|...
gi 446524801 465 -------KSNLLILDEPTNHLDL 480
Cdd:COG4559 151 lwepvdgGPRWLFLDEPTSALDL 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-503 |
3.58e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 57.73 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 349 VTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS--------VGYYDQEQA---NLTSSKRVlnelw 416
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITnlppekrdISYVPQNYAlfpHMTVYKNI----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 417 dEYPL--------QPEKEIRTILGnflFTGDDVL---KPvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEI 485
Cdd:cd03299 93 -AYGLkkrkvdkkEIERKVLEIAE---MLGIDHLlnrKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|..
gi 446524801 486 LENALID----YPGTLLFVSHD 503
Cdd:cd03299 168 LREELKKirkeFGVTVLHVTHD 189
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
320-542 |
3.62e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 320 FDIEKQSGNdvLQVNDATIGYD--ENPIIEHVTMRLTRGDSVALVGPNGIGKSTllksIVNklpLLNG--DVSFGS---- 391
Cdd:PRK11176 333 RVIERAKGD--IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKST----IAN---LLTRfyDIDEGEilld 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 392 NVSVGYYD----QEQANLTSSK------RVLNELW----DEYPL-QPEKEIRTILG-NFLFTGDDVLKPV-----SSLSG 450
Cdd:PRK11176 404 GHDLRDYTlaslRNQVALVSQNvhlfndTIANNIAyartEQYSReQIEEAARMAYAmDFINKMDNGLDTVigengVLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 451 GQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL--IDYPGTLLFVSHdryfinrvtttvvELST-EGAQEYLg 527
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH-------------RLSTiEKADEIL- 549
|
250
....*....|....*
gi 446524801 528 dydyyVEKKNEMIER 542
Cdd:PRK11176 550 -----VVEDGEIVER 559
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-479 |
4.36e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.79 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 341 DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNG-DVSF-------------------GS--- 391
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPpdsgsiLIDGkDVTKlpeykrakyigrvfqdpmmGTaps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 392 -----NVSVGYYDQEQANLtsSKRVLNELWDEYplqpeKEIRTILGNFLftgDDVLK-PVSSLSGGQkaRLALAKLM--M 463
Cdd:COG1101 97 mtieeNLALAYRRGKRRGL--RRGLTKKRRELF-----RELLATLGLGL---ENRLDtKVGLLSGGQ--RQALSLLMatL 164
|
170
....*....|....*.
gi 446524801 464 QKSNLLILDEPTNHLD 479
Cdd:COG1101 165 TKPKLLLLDEHTAALD 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-222 |
4.60e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.79 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQNTG 76
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkpVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 LETSLTIWDemlTVFTHLQQmetklrrleQEMGKEEnfsNEATYERLLADYDqlqlnykdqggyqyeadirsiLSGLGfp 156
Cdd:PRK11248 81 LLPWRNVQD---NVAFGLQL---------AGVEKMQ---RLEIAHQMLKKVG---------------------LEGAE-- 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 157 vethQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK11248 123 ----KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTreqmQTLLLKLWQETGKQVLLITHD 188
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
4.93e-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 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: 57.85 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGYLAQNTGLE 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVT------IDGRDITAKKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 TSLT-IWDEMLTVFthlQQMETKLrrleqemgkeenFsnEATYERLLAdYDQLQLNYKDQggyqyEAD--IRSILSGLGF 155
Cdd:TIGR04521 75 KKLKdLRKKVGLVF---QFPEHQL------------F--EETVYKDIA-FGPKNLGLSEE-----EAEerVKEALELVGL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 156 PVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:TIGR04521 132 DEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgrKEILDLFKRLHKEKGLTVILVTHS 202
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
331-502 |
5.33e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.96 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN-PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNV---------------S 394
Cdd:cd03290 1 VQVTNGYFSWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnryS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQE--------QANLTS----SKRVLNELWDEYPLQPEKEIrtilgnfLFTGD--DVLKPVSSLSGGQKARLALAK 460
Cdd:cd03290 81 VAYAAQKpwllnatvEENITFgspfNKQRYKAVTDACSLQPDIDL-------LPFGDqtEIGERGINLSGGQRQRICVAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 461 LMMQKSNLLILDEPTNHLDLN-SKEILENALI----DYPGTLLFVSH 502
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHlSDHLMQEGILkflqDDKRTLVLVTH 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-222 |
5.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTL-------LKIIAGELSHDGGEII-KPKDVSIGYLAQNTGletsltiwdeMLTV 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLiqninalLKPTTGTVTVDDITIThKTKDKYIRPVRKRIG----------MVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 91 FTHLQQMETKLRRlEQEMGKEeNFsneatyerlladydqlQLNYKDQGGYQYEadirsILSGLGFPVETHQTTISTLSGG 170
Cdd:PRK13646 93 FPESQLFEDTVER-EIIFGPK-NF----------------KMNLDEVKNYAHR-----LLMDLGFSRDVMSQSPFQMSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 171 QKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-238 |
6.04e-09 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 56.41 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 24 LEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIiKPKDVSIGYLAQNtglETSLTIWDEMLTVFTHLQqmetklrr 103
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-KVNDQSHTGLAPY---QRPVSMLFQENNLFAHLT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 104 LEQEMGkeenfsneatyerlLADYDQLQLNYKDQggYQYEADIRSIlsGLGFPVEThqtTISTLSGGQKTRLALGKLLLT 183
Cdd:TIGR01277 87 VRQNIG--------------LGLHPGLKLNAEQQ--EKVVDAAQQV--GIADYLDR---LPEQLSGGQRQRVALARCLVR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 184 KPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:TIGR01277 146 PNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQ 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-222 |
7.50e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.92 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiIKPKDVSIgylaqnTGLETSLT 82
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQHI------EGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWDEMLTVFTHLqqmetklrRLEQEMGKEENFsneatyerLLADYDQLQLNY-----KDQGGYQYEADI--RSI--LSGL 153
Cdd:PRK11300 78 ARMGVVRTFQHV--------RLFREMTVIENL--------LVAQHQQLKTGLfsgllKTPAFRRAESEAldRAAtwLERV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 154 GFpVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPT---NHLDIETLTWLEQYLQGYPG-AILIVSHD 222
Cdd:PRK11300 142 GL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvTVLLIEHD 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
344-510 |
7.78e-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: 57.12 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 344 PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgSNVSVGYYDQEQANltSSKRVLNELWDEYP--L 421
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-RGQDLYQLDRKQRR--AFRRDVQLVFQDSPsaV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 422 QPEKEIRTILGNFL-----------------------FTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:TIGR02769 102 NPRMTVRQIIGEPLrhltsldeseqkariaelldmvgLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 479 DL-NSKEILE--NALIDYPGT-LLFVSHD----RYFINRV 510
Cdd:TIGR02769 182 DMvLQAVILEllRKLQQAFGTaYLFITHDlrlvQSFCQRV 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-222 |
7.99e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.33 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkdVSIgylaqntgLE 78
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGE------VSL--------VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 TSLTIWDEmltvfthlqQMETKLRrlEQEMG-KEENFSNEATYERLlaDYDQLQLNYKDQGGYQYEADIRSILSGLGFPV 157
Cdd:PRK10584 72 QPLHQMDE---------EARAKLR--AKHVGfVFQSFMLIPTLNAL--ENVELPALLRGESSRQSRNGAKALLEQLGLGK 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 158 ETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:PRK10584 139 RLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
355-509 |
8.01e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 355 RGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgsnvsvgyydqeqANLTSSKRVLNELWDEYPLQPEKEirtilgnf 434
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------------IDGEDILEEVLDQLLLIIVGGKKA-------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 435 lftgddvlkpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD---------LNSKEILENALIDYPGTLLFVSHDRY 505
Cdd:smart00382 60 ------------SGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEK 127
|
....
gi 446524801 506 FINR 509
Cdd:smart00382 128 DLGP 131
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
8.39e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.28 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY-----GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-----------IKPKDV 66
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 67 S-------IGYLAQNTGLETSLTIWDEmLTVFTHLQqmetklrrLEQEMGKEEnfsneATYERLLADYDqlqlnykdqgg 139
Cdd:TIGR03269 359 GrgrakryIGILHQEYDLYPHRTVLDN-LTEAIGLE--------LPDELARMK-----AVITLKMVGFD----------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 140 yqyEADIRSILSGLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET--------LTWLEQYLQG 211
Cdd:TIGR03269 414 ---EEKAEEILDKYP----------DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITkvdvthsiLKAREEMEQT 480
|
250
....*....|....*
gi 446524801 212 YpgaiLIVSHDRYFL 226
Cdd:TIGR03269 481 F----IIVSHDMDFV 491
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-475 |
9.32e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 56.66 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQANL-- 405
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLgi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 -----TSSkrVLNEL--WD--EYPLQPEKEIRTILGNFLfTG------DDVL----------KPVSSLSGGQKARLALAK 460
Cdd:COG4674 88 grkfqKPT--VFEELtvFEnlELALKGDRGVFASLFARL-TAeerdriEEVLetigltdkadRLAGLLSHGQKQWLEIGM 164
|
170
....*....|....*
gi 446524801 461 LMMQKSNLLILDEPT 475
Cdd:COG4674 165 LLAQDPKLLLLDEPV 179
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
345-510 |
1.08e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgSNVSVGYYDQEQANltSSKRVLNELWDEYP--LQ 422
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRAQRK--AFRRDIQMVFQDSIsaVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 423 PEKEIRTILGNFL--FTG----------DDVLKPV-----------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK10419 104 PRKTVREIIREPLrhLLSldkaerlaraSEMLRAVdlddsvldkrpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524801 480 LnskeILENALIDYPGTL--------LFVSHD----RYFINRV 510
Cdd:PRK10419 184 L----VLQAGVIRLLKKLqqqfgtacLFITHDlrlvERFCQRV 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-502 |
1.19e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 325 QSGNDVLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgSNVSVGYYDQEQ 402
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 403 -------------------------ANLTSS----KRVLNELWDEYPLQPEKEIRTILGnflftgdDVLKPvssLSGGQK 453
Cdd:PRK11160 412 lrqaisvvsqrvhlfsatlrdnlllAAPNASdealIEVLQQVGLEKLLEDDKGLNAWLG-------EGGRQ---LSGGEQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 454 ARLALAKLMMQKSNLLILDEPTNHLDLNS-KEILENALIDYPG-TLLFVSH 502
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITH 532
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
359-479 |
1.26e-08 |
|
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: 55.25 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 359 VALVGPNGIGKSTLLKSIVNKL--PLLNGDVSF-GSNVS-------VGYYDQEQAnltsskrVLNELwdeyplqpekeir 428
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLInGRPLDkrsfrkiIGYVPQDDI-------LHPTL------------- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 429 TILGNFLFTGddVLKpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03213 98 TVRETLMFAA--KLR---GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
325-514 |
1.33e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 325 QSGNdvLQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDV---------------- 387
Cdd:PRK10790 337 QSGR--IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsvlr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 388 ---------------SFGSNVSVGYYDQEQANLTSSKRV-LNELWDEYPlqpeKEIRTILGnflftgddvlKPVSSLSGG 451
Cdd:PRK10790 415 qgvamvqqdpvvladTFLANVTLGRDISEEQVWQALETVqLAELARSLP----DGLYTPLG----------EQGNNLSVG 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 452 QKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL--IDYPGTLLFVSHdryfinRVTTTV 514
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALaaVREHTTLVVIAH------RLSTIV 539
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-222 |
1.36e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.76 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigylaqntgletslTIWDEMLTvfthLQQME 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---------------------TIAGYHIT----PETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 99 TKLRRLEQEMGKEENFSNEATYER-LLADYDQLQLNYkdqGGYQYEADIRSI--LSGLGFPVETHQTTISTLSGGQKTRL 175
Cdd:PRK13641 78 KNLKKLRKKVSLVFQFPEAQLFENtVLKDVEFGPKNF---GFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 176 ALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHD 222
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
164-238 |
1.37e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.31 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 164 ISTLSGGQKT------RLALGKLLLTKPDLLILDEPTNHLDIETLTW-----LEQYLQGYPGAILIVSHDRYFLDKLvTQ 232
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA-DH 191
|
....*.
gi 446524801 233 VYEISN 238
Cdd:cd03240 192 IYRVEK 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-223 |
1.53e-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: 58.00 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGgeiikpkDVSIGYLAQNTgleTSL 81
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-------EIQIDGVSWNS---VTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 TIWDEMLTVFthlqqmetklrrleqemgKEENFSNEATYERLLADYDQlqlnYKDQGGYQY--EADIRSILSglGFPVET 159
Cdd:TIGR01271 1288 QTWRKAFGVI------------------PQKVFIFSGTFRKNLDPYEQ----WSDEEIWKVaeEVGLKSVIE--QFPDKL 1343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 160 HQTTIS---TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-QGYPGAILIVSHDR 223
Cdd:TIGR01271 1344 DFVLVDggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-501 |
1.72e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpKDVSIGYLAQNTGLETSLT 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWDEMLTVFthlqqmetklrrleQEMGKEENFsneatYERLLADYDQLQLNYKDQGGYQYEADIrsILSGLGFPVEThQT 162
Cdd:PRK09700 84 IIYQELSVI--------------DELTVLENL-----YIGRHLTKKVCGVNIIDWREMRVRAAM--MLLRVGLKVDL-DE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSHdryfldKLvtqvyeisnK 239
Cdd:PRK09700 142 KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH------KL---------A 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 240 ESRRFVGNYSKYLDlKSALYEQEMKryEKQQDEIAKLedFVQKNIarastTKRAQSRRKQLDRMELLTRplgdsksasfh 319
Cdd:PRK09700 207 EIRRICDRYTVMKD-GSSVCSGMVS--DVSNDDIVRL--MVGREL-----QNRFNAMKENVSNLAHETV----------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 320 FDIEKQSGNDVLQVNDatigydenpiiehVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVSV-GY 397
Cdd:PRK09700 266 FEVRNVTSRDRKKVRD-------------ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlNGKDISPrSP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 398 YDQEQ---ANLTSSKRVlNELWDEYPLQPEKEIRTILGNFLFTG-------------------------DDVLKPVSSLS 449
Cdd:PRK09700 333 LDAVKkgmAYITESRRD-NGFFPNFSIAQNMAISRSLKDGGYKGamglfhevdeqrtaenqrellalkcHSVNQNITELS 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 450 GGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI--LENALIDYPGTLLFVS 501
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKaEIykVMRQLADDGKVILMVS 466
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
345-479 |
1.89e-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: 55.35 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP---LLNGDVSF-GSNVS-------VGYYDQEQANL-------- 405
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFnGQPRKpdqfqkcVAYVRQDDILLpgltvret 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 -----------TSSKRVLNELWDEYPLqpeKEIR-TILGNFLFTGddvlkpvssLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:cd03234 102 ltytailrlprKSSDAIRKKRVEDVLL---RDLAlTRIGGNLVKG---------ISGGERRRVSIAVQLLWDPKVLILDE 169
|
....*.
gi 446524801 474 PTNHLD 479
Cdd:cd03234 170 PTSGLD 175
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
327-502 |
1.90e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 327 GNDVLQVNDATIGYDENPI--------IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYY 398
Cdd:TIGR00954 441 GRGIVEYQDNGIKFENIPLvtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 399 DQE--QANLTSSKRVLnelwdeYPLQPE---------KEIRTILGNFLFtgDDVLKPVSS----------LSGGQKARLA 457
Cdd:TIGR00954 521 PQRpyMTLGTLRDQII------YPDSSEdmkrrglsdKDLEQILDNVQL--THILEREGGwsavqdwmdvLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 458 LAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
331-479 |
2.08e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 56.62 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI-----------------VNKLPLLNGDVS--FGS 391
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagledptsgeiliggrdVTDLPPKDRNIAmvFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 392 -----NVSVgyYDqeqaNLtsskrvlnelwdEYPLQ----PEKEIR-------TILGnfLftgDDVL--KPvSSLSGGQK 453
Cdd:COG3839 84 yalypHMTV--YE----NI------------AFPLKlrkvPKAEIDrrvreaaELLG--L---EDLLdrKP-KQLSGGQR 139
|
170 180
....*....|....*....|....*.
gi 446524801 454 ARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-201 |
2.47e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD----------------GGEI---IKP 63
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqrEGRLardIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 64 KDVSIGYLAQNTGLETSLTIWDEMLtvfthlqqmetklrrleqeMGKeenFSNEATYERLLADYDQLQlnykDQGGYQye 143
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVL-------------------IGA---LGSTPFWRTCFSWFTREQ----KQRALQ-- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 144 adirsILSGLGFPVETHQTtISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:PRK09984 136 -----ALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-223 |
2.58e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVSIGYLAQNTGletsltiwdemlTVF 91
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDI---RTVTRASLRRNIA------------VVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 92 thlqqmetklrrleQEMGK-----EENFS---NEATYERLLADYDQLQLN---YKDQGGYQYEADIRSilsglgfpveth 160
Cdd:PRK13657 416 --------------QDAGLfnrsiEDNIRvgrPDATDEEMRAAAERAQAHdfiERKPDGYDTVVGERG------------ 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 161 qttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQgypGAILIVSHDR 223
Cdd:PRK13657 470 ----RQLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVK---AALDELMKGR 521
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
331-503 |
2.66e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 54.57 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSvgyydqeqANLTSSKR 410
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--------TDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNELWDEYPLQPEKeirTILGNFLF-------TGDDVLKPVSS-----------------LSGGQKARLALAKLMMQKS 466
Cdd:cd03301 73 DIAMVFQNYALYPHM---TVYDNIAFglklrkvPKDEIDERVREvaellqiehlldrkpkqLSGGQRQRVALGRAIVREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 467 NLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHD 503
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKrlqqRLGTTTIYVTHD 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-514 |
2.85e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.23 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLLN------GDVS-FGSNV------- 393
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF-NRLLELNeearveGEVRlFGRNIyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 394 -----SVGY-------------YDQ-----EQANLTSSKRVLNE----------LWDEyplqpekeIRTILGNFlftgdd 440
Cdd:PRK14267 81 ievrrEVGMvfqypnpfphltiYDNvaigvKLNGLVKSKKELDErvewalkkaaLWDE--------VKDRLNDY------ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 441 vlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYpgTLLFVSHDRYFINRVTTTV 514
Cdd:PRK14267 147 ----PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFelkkEY--TIVLVTHSPAQAARVSDYV 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-221 |
2.92e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.78 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KPKDvsigyLAQNTGLETSLTIWDEMLTVFTHL 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPIS-----QYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 95 QQ--METKLRRLEQEMGKE-ENFSNEATYERLLADydqlqlnykdqgGYQYEADIRSilsglgfpvethqttiSTLSGGQ 171
Cdd:cd03248 104 LQdnIAYGLQSCSFECVKEaAQKAHAHSFISELAS------------GYDTEVGEKG----------------SQLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524801 172 KTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSH 221
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-486 |
3.21e-08 |
|
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: 54.80 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 341 DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSN-----------VSVGYYDQEQANLTSSK 409
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlrRQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 410 RVLNELWDE-YPLQPEKEIRTILGNFLFT-------GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:cd03252 93 RDNIALADPgMSMERVIEAAKLAGAHDFIselpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
....*
gi 446524801 482 SKEIL 486
Cdd:cd03252 173 SEHAI 177
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-198 |
3.77e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSH---------DGGEIIKPKDVSIGYLAQNTGLETSLTIWDEM 87
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnftgtilaNNRKPTKQILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 LTVfthlqqmetKLRRLEQEMGKEENFsneatyerLLADydqlqlnykdqggyqyeadirSILSGLGFP----VETHQTT 163
Cdd:PLN03211 162 VFC---------SLLRLPKSLTKQEKI--------LVAE---------------------SVISELGLTkcenTIIGNSF 203
|
170 180 190
....*....|....*....|....*....|....*
gi 446524801 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-198 |
3.99e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD---------GGEIIKPKDVSI--GYLAQNTGLETSLTIwD 85
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgsgsvllNGMPIDAKEMRAisAYVQQDDLFIPTLTV-R 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 86 EMLTVFTHLqqmetklrRLEQEMGKEENfsneatYERLLADYDQLQLnykdqggyQYEADIRsilsgLGFPvethqTTIS 165
Cdd:TIGR00955 118 EHLMFQAHL--------RMPRRVTKKEK------RERVDEVLQALGL--------RKCANTR-----IGVP-----GRVK 165
|
170 180 190
....*....|....*....|....*....|...
gi 446524801 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:TIGR00955 166 GLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-234 |
4.00e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNtgLETSLT 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL--------FERQS--IKKDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWDEMLTVFTHLQQMETKLrRLEQEMGKEENFSNEATyerllaDYDQLqlnykdqggyqyeADIRSILSGLGFPVethqt 162
Cdd:PRK13540 71 TYQKQLCFVGHRSGINPYL-TLRENCLYDIHFSPGAV------GITEL-------------CRLFSLEHLIDYPC----- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 163 tiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD---IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVY 234
Cdd:PRK13540 126 --GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEY 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
373-515 |
4.41e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 373 LKSIVNKLPLLNgDVSFGSNVSVGyydQEQANLTSSKRV-----LNELWDEYPLQPEkeirTILGNFlftgddvlkpVSS 447
Cdd:PTZ00265 1297 LFSIVSQEPMLF-NMSIYENIKFG---KEDATREDVKRAckfaaIDEFIESLPNKYD----TNVGPY----------GKS 1358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG----TLLFVSHDRYFINRVTTTVV 515
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAHRIASIKRSDKIVV 1430
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
343-490 |
4.50e-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: 54.86 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 343 NPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLL------NGDVSFGSNVSVGYYDQEQANLtsskrVLNELW 416
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSegkikhSGRISFSSQFSWIMPGTIKENI-----IFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 417 DEYPLQ---------------PEKEiRTILGNFLFTgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL- 480
Cdd:cd03291 125 DEYRYKsvvkacqleeditkfPEKD-NTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVf 193
|
170
....*....|
gi 446524801 481 NSKEILENAL 490
Cdd:cd03291 194 TEKEIFESCV 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-267 |
4.89e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII------------AGELSHDGGEIIKPKdvsigy 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 laqntgletsltiwdemltvfthlqqmeTKLRRLEQEMG---KEENFSNEATYERLLADydqLQLN-YKDQggYQYEADI 146
Cdd:PRK14239 79 ----------------------------TDTVDLRKEIGmvfQQPNPFPMSIYENVVYG---LRLKgIKDK--QVLDEAV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 147 RSILSGLGFPVET----HQTTIStLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVS 220
Cdd:PRK14239 126 EKSLKGASIWDEVkdrlHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVT 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446524801 221 HDryfldklVTQVYEISNKESRRFVGNYSKYLDLKSALYEQEMKRYE 267
Cdd:PRK14239 205 RS-------MQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETE 244
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
331-502 |
5.65e-08 |
|
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: 53.91 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENP----IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvnkLPLLNGDvsfGSNVSVGYYDQEQANLt 406
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRML---AGLLEPD---AGFATVDGFDVVKEPA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 407 SSKRVLNELWDEYPLQPEKEIRTILGNF---------------------LFTGDDVLKPVSSLSGGQKARLALAKLMMQK 465
Cdd:cd03266 75 EARRRLGFVSDSTGLYDRLTARENLEYFaglyglkgdeltarleeladrLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 466 SNLLILDEPTNHLDLNSKEILENALIDYPG---TLLFVSH 502
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-199 |
6.23e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIA-------GELSHDGGEIIK--PKDVS--IGYLA 72
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIQHyaSKEVArrIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLETSLTIwdemltvfthlqqmetklrrleQEMGKEENFSNEATYERLLAdydqlqlnykdqggyQYEADIRSILSG 152
Cdd:PRK10253 88 QNATTPGDITV----------------------QELVARGRYPHQPLFTRWRK---------------EDEEAVTKAMQA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 153 LGFPVETHQtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK10253 131 TGITHLADQ-SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
6.39e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.47 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KPKDVS---IGYLAQNT 75
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILfdgKPIDYSrkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 76 GLetsltiwdemltVFthlQQMETKLrrleqemgkeenFSnEATYERLLADYDQLQLNYKdqggyQYEADIRSILSGLGF 155
Cdd:PRK13636 85 GM------------VF---QDPDNQL------------FS-ASVYQDVSFGAVNLKLPED-----EVRKRVDNALKRTGI 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 156 PVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13636 132 EHLKDKPT-HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
6.94e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.71 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNtglE 78
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE--------WIFKD---E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 TSLTIWDEMLTVFTHLQQMETKLRRLEQ------EMGKEENFSN----EATYERLLAdYDQLQLNYKDQGGYQYEADIRS 148
Cdd:PRK13651 72 KNKKKTKEKEKVLEKLVIQKTRFKKIKKikeirrRVGVVFQFAEyqlfEQTIEKDII-FGPVSMGVSKEEAKKRAAKYIE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 149 ILsglGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQ-YLQGypGAILIVSHD 222
Cdd:PRK13651 151 LV---GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNlNKQG--KTIILVTHD 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
7.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKI------------IAGELSHDGGEIIKpKDVS- 67
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFK-MDVIe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 ----IGYLAQNTGLETSLTIWDEMltvfthlqQMETKLRRLEQemgkeenfSNEATYERLLADYDQLQL--NYKDQggyq 141
Cdd:PRK14247 80 lrrrVQMVFQIPNPIPNLSIFENV--------ALGLKLNRLVK--------SKKELQERVRWALEKAQLwdEVKDR---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 142 yeadirsilsgLGFPVethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIV 219
Cdd:PRK14247 140 -----------LDAPA-------GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLV 201
|
..
gi 446524801 220 SH 221
Cdd:PRK14247 202 TH 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-502 |
8.24e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.89 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 326 SGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKL----P--------LLNG-DVsFGSN 392
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRMndliPgarvegeiLLDGeDI-YDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 393 VS-------VGY------------YDqeqaNLT--------SSKRVLNE----------LWDEYplqpekeirtilgnfl 435
Cdd:COG1117 85 VDvvelrrrVGMvfqkpnpfpksiYD----NVAyglrlhgiKSKSELDEiveeslrkaaLWDEV---------------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 436 ftgDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENaLI-----DYpgTLLFVSH 502
Cdd:COG1117 145 ---KDRLKkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEE-LIlelkkDY--TIVIVTH 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
340-479 |
9.30e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLTSSKRVLNELWDEY 419
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--------EKRMNDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 420 PLQP------------------EKEIRTILGNflftGDDVL--------KPvSSLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:PRK11000 85 ALYPhlsvaenmsfglklagakKEEINQRVNQ----VAEVLqlahlldrKP-KALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
....*.
gi 446524801 474 PTNHLD 479
Cdd:PRK11000 160 PLSNLD 165
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-201 |
9.45e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.80 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAE--TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIGYLaqnTGLETS 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPL---EDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIWDEMLTVFthlqqMETklrrLEQEMGKEENFSNEATYERLLAdydqlqlnykDQGGyqyeadirsilsglgfpveth 160
Cdd:cd03369 84 LTIIPQDPTLF-----SGT----IRSNLDPFDEYSDEEIYGALRV----------SEGG--------------------- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 161 qttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03369 124 ----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
322-504 |
9.97e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.57 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 322 IEKQSGNDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQE 401
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD--------GQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKRVLNELWDEYPL------------------QPEKEIRTILgnflftgDDVLKPV----------SSLSGGQK 453
Cdd:PRK09452 78 ITHVPAENRHVNTVFQSYALfphmtvfenvafglrmqkTPAAEITPRV-------MEALRMVqleefaqrkpHQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL--------IdypgTLLFVSHDR 504
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELkalqrklgI----TFVFVTHDQ 205
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-222 |
1.06e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 52.71 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 32 IALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWDEMLTV------FTHLQQMETKLRR-- 103
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYRIerrqgeFAEFLEAKPSERKea 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 104 LEQEMGKEenfsneaTYERLLADYDQLQLNYKDQ-----GGYQYEADIRSILSGLGfpvethqtTISTLSGGQKTRLALG 178
Cdd:COG0419 106 LKRLLGLE-------IYEELKERLKELEEALESAleelaELQKLKQEILAQLSGLD--------PIETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524801 179 KLLltkpdLLILDepTNHLDIETLTWLEQYLQgypgAILIVSHD 222
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-514 |
1.09e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 21 NIKLEVQTKDRIALVGRNGAGKS----TLLKII---AGELSHDG-------GEIIKPKDVSIGYLAQNTGLETSLtIWDE 86
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKmllrrrsRQVIELSEQSAAQMRHVRGADMAM-IFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 87 MLT----VFTHLQQMETKLRrLEQEMGKEENFsneATYERLLadyDQLQLnykdqggyqyeADIRSILSGlgFPvetHQt 162
Cdd:PRK10261 113 PMTslnpVFTVGEQIAESIR-LHQGASREEAM---VEAKRML---DQVRI-----------PEAQTILSR--YP---HQ- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 163 tistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHDryfldklVTQVYEISN 238
Cdd:PRK10261 169 ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHD-------MGVVAEIAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 239 KesrrfvgnyskyldlksalyeqEMKRYEKQQDEIAKLEdfvqkNIARAST---TKRAQSRRKQLDRMELLTRP-----L 310
Cdd:PRK10261 238 R----------------------VLVMYQGEAVETGSVE-----QIFHAPQhpyTRALLAAVPQLGAMKGLDYPrrfplI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 311 GDSKSASFHFDIEKQS---GNDVLQVNDATIGYD-----------ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI 376
Cdd:PRK10261 291 SLEHPAKQEPPIEQDTvvdGEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 377 VNKLPLLNGDVSFGSnvsvgyydQEQANLTSSK-----RVLNELW-DEY-PLQPEKEI-----RTILGNFLFTGDDVLKP 444
Cdd:PRK10261 371 LRLVESQGGEIIFNG--------QRIDTLSPGKlqalrRDIQFIFqDPYaSLDPRQTVgdsimEPLRVHGLLPGKAAAAR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 445 VSSL------------------SGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTL----LFVSH 502
Cdd:PRK10261 443 VAWLlervgllpehawryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISH 522
|
570
....*....|..
gi 446524801 503 DRYFINRVTTTV 514
Cdd:PRK10261 523 DMAVVERISHRV 534
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-479 |
1.39e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS------------VGYYDQEQANLT 406
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPsrarharqrvgvVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 407 SSKRVLneLWDEYPLQPEKEIRTI---LGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13537 97 VRENLL--VFGRYFGLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-479 |
1.40e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDV---------------SFGSNVS 394
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQEQ--------ANLTSSKRVLNelwdeyplQPEKEI-RTIlgnflftgDDVL----------KPVSSLSGGQKAR 455
Cdd:PRK13638 81 TVFQDPEQqifytdidSDIAFSLRNLG--------VPEAEItRRV--------DEALtlvdaqhfrhQPIQCLSHGQKKR 144
|
170 180
....*....|....*....|....
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLD 168
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-210 |
1.52e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KP-KDVSIGYLAQNTGL- 77
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgRPlSSLSHSVLRQGVAMv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 78 -ETSLTIWDEMLTVFThlqqmetkLRRleqemgkeeNFSNEATYERLladyDQLQLnykdqggyqyeAD-IRSILSGLGF 155
Cdd:PRK10790 421 qQDPVVLADTFLANVT--------LGR---------DISEEQVWQAL----ETVQL-----------AElARSLPDGLYT 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 156 PVETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQ 210
Cdd:PRK10790 469 PLGEQG---NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT----EQAIQ 516
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
361-504 |
1.77e-07 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 53.65 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 361 LVGPNGIGKSTLLKsivnklpLLNG--DVSFGSnvsVGYYDQEQANLTSSKRVLNELWDEYPL----------------- 421
Cdd:TIGR01187 1 LLGPSGCGKTTLLR-------LLAGfeQPDSGS---IMLDGEDVTNVPPHLRHINMVFQSYALfphmtveenvafglkmr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 422 -QPEKEI----RTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG- 495
Cdd:TIGR01187 71 kVPRAEIkprvLEALRLVQLEEFADRKP-HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEq 149
|
170
....*....|..
gi 446524801 496 ---TLLFVSHDR 504
Cdd:TIGR01187 150 lgiTFVFVTHDQ 161
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-201 |
1.77e-07 |
|
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: 52.54 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVSIGYLAQNTGL---ETSL---TIW 84
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVDI---RDLNLRWLRSQIGLvsqEPVLfdgTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 85 DEMLtvfthlqqmetklrrleqeMGKeenfsNEATYERLLADYDQlqlnykdqggyqyeADIRSILSGLgfPvETHQTTI 164
Cdd:cd03249 95 ENIR-------------------YGK-----PDATDEEVEEAAKK--------------ANIHDFIMSL--P-DGYDTLV 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 165 ----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03249 134 gergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-201 |
1.93e-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: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 13 YGAET--ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYLAQNTGLeT 79
Cdd:cd03252 10 YKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlVDGHDLAladpawlrrqVGVVLQENVL-F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 80 SLTIWDEMltvftHLQQMETKLRRLEqemgkeenfsnEATyeRLLADYD---QLQLNYKDQGGYQyeadirsilsGLGfp 156
Cdd:cd03252 89 NRSIRDNI-----ALADPGMSMERVI-----------EAA--KLAGAHDfisELPEGYDTIVGEQ----------GAG-- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524801 157 vethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03252 139 ----------LSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-198 |
1.97e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.08 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG-----GEIIKPKDVS-----IGYLAQNTGLETSlTIWDE 86
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGslkinGIELRELDPEswrkhLSWVGQNPQLPHG-TLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 87 MLtvfthlqqmetklrrleqeMGKEEnfSNEATYERLLADYDQLQLNYKDQGGYQYEADIRSIlsglgfpvethqttisT 166
Cdd:PRK11174 443 VL-------------------LGNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAA----------------G 485
|
170 180 190
....*....|....*....|....*....|..
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
348-510 |
2.02e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.20 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 348 HVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSVGyydqeqanltsSKRVLNELW--------DE 418
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdGQDITGL-----------SGRELRPLRrrmqmvfqDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 419 Y-PLQPEKEIRTILG-----NFLFTGDDVLKPVSSL------------------SGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:COG4608 105 YaSLNPRMTVGDIIAeplriHGLASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 475 TNHLD-------LNSKEILENALidypG-TLLFVSHD----RYFINRV 510
Cdd:COG4608 185 VSALDvsiqaqvLNLLEDLQDEL----GlTYLFISHDlsvvRHISDRV 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-490 |
2.09e-07 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 52.23 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDE-NPIIEHVTMRLTRGDSVALVGPNGIGKSTLLksivnklpllngdvsfgsNVSVGYYDQEQANLTSSKR 410
Cdd:cd03254 4 EFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLI------------------NLLMRFYDPQKGQILIDGI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNELwdeyplqPEKEIRTILG-----NFLFTG---------------DDVLKPV------------------------S 446
Cdd:cd03254 66 DIRDI-------SRKSLRSMIGvvlqdTFLFSGtimenirlgrpnatdEEVIEAAkeagahdfimklpngydtvlgengG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524801 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEAL 182
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
330-479 |
2.36e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 52.30 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKL-PLLNGDVSFGsnvsvgyyDQEqanLTSS 408
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTITVD--------GED---LTDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNELwdeyplqpEKEI------------RTILGNFLF---------------TGDDVLKPV----------SSLSGG 451
Cdd:COG1126 69 KKDINKL--------RRKVgmvfqqfnlfphLTVLENVTLapikvkkmskaeaeeRAMELLERVgladkadaypAQLSGG 140
|
170 180
....*....|....*....|....*....
gi 446524801 452 QKARLALAK-LMMqKSNLLILDEPTNHLD 479
Cdd:COG1126 141 QQQRVAIARaLAM-EPKVMLFDEPTSALD 168
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-542 |
2.59e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 329 DVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsIVNKL------PLLNGDV--------------- 387
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLielypeARVSGEVyldgqdifkmdviel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 388 -----------------SFGSNVSVGYydqEQANLTSSKRVLNEL--WDEYPLQPEKEIRTILGnflftgddvlKPVSSL 448
Cdd:PRK14247 81 rrrvqmvfqipnpipnlSIFENVALGL---KLNRLVKSKKELQERvrWALEKAQLWDEVKDRLD----------APAGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 449 SGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVVELSTEGAQEYL 526
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250
....*....|....*.
gi 446524801 527 GDYDYYVEKKNEMIER 542
Cdd:PRK14247 228 PTREVFTNPRHELTEK 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-240 |
2.62e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 33 ALVGRNGAGKSTLLKIIAGELSHDGGEII-----KPKDVS-------IGYLAQNTgLETSLTIWDEMLTVFTHLQQMETK 100
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDIIindshNLKDINlkwwrskIGVVSQDP-LLFSNSIKNNIKYSLYSLKDLEAL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 101 LRRLEQEMGKEENFSNEATYERLLADYD-QLQLNYKDQGG-------YQYEAD-----------IRSILSGLGFPVETH- 160
Cdd:PTZ00265 494 SNYYNEDGNDSQENKNKRNSCRAKCAGDlNDMSNTTDSNEliemrknYQTIKDsevvdvskkvlIHDFVSALPDKYETLv 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQY---LQGYPGAILIVSHDRYFLDKLVTQVYEIS 237
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRITIIIAHRLSTIRYANTIFVLS 653
|
...
gi 446524801 238 NKE 240
Cdd:PTZ00265 654 NRE 656
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
331-482 |
3.04e-07 |
|
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: 51.26 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN--PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS-VGYYD------- 399
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDIStIPLEDlrsslti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 --QEQANLTSSKRVLNELWDEYPlqpEKEIRTILgnflftgdDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03369 87 ipQDPTLFSGTIRSNLDPFDEYS---DEEIYGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
....*
gi 446524801 478 LDLNS 482
Cdd:cd03369 156 IDYAT 160
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-242 |
3.47e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.96 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIaGELSHDGGEIIKPKDVSigYLAQNtgletsltI 83
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVE--FFNQN--------I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMLTVfthlqqmeTKLRRLEQEMGKEENFSNEATYE------RLLADYDQLQLNYKDQGGYQyEADIRSILSGlgfpv 157
Cdd:PRK14258 77 YERRVNL--------NRLRRQVSMVHPKPNLFPMSVYDnvaygvKIVGWRPKLEIDDIVESALK-DADLWDEIKH----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 158 ETHQTTIStLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP----GAILIVSHDRYFLDKLVTQV 233
Cdd:PRK14258 143 KIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLSDFT 221
|
....*....
gi 446524801 234 YEISNKESR 242
Cdd:PRK14258 222 AFFKGNENR 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-201 |
3.57e-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: 53.76 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSigYLAQNTGLETSlTIWDEMLTVFTHlqqM 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--FSPQTSWIMPG-TIKDNIIFGLSY---D 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 98 ETKLRRLEQEMGKEENFSneatyerLLADYDQLQLNykdQGGYqyeadirsilsglgfpvethqttisTLSGGQKTRLAL 177
Cdd:TIGR01271 515 EYRYTSVIKACQLEEDIA-------LFPEKDKTVLG---EGGI-------------------------TLSGGQRARISL 559
|
170 180
....*....|....*....|....
gi 446524801 178 GKLLLTKPDLLILDEPTNHLDIET 201
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-503 |
3.59e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.79 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDEN----PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF------GSNVSVGYYDQ 400
Cdd:COG4525 4 LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 401 EQAnLTSSKRVLNELwdEYPLQ----PEKEIRTILGNFL-------FTGddvlKPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:COG4525 84 KDA-LLPWLNVLDNV--AFGLRlrgvPKAERRARAEELLalvgladFAR----RRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524801 470 ILDEPTNHLDLNSKEILENALIDYPG----TLLFVSHD 503
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQrtgkGVFLITHS 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-198 |
3.65e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.92 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQ 73
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlshvPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 74 NTGLetsltiwdemltvFTHlqqmetklrrleqeMGKEENFSNEATYERLLADYDQLQLNykdqggyqyeaDIRSILSGL 153
Cdd:PRK11607 99 SYAL-------------FPH--------------MTVEQNIAFGLKQDKLPKAEIASRVN-----------EMLGLVHMQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524801 154 GFPV-ETHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11607 141 EFAKrKPHQ-----LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-198 |
3.85e-07 |
|
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: 53.48 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTK--DRIALVGRNGAGKSTLLKIIAGELSHDGGE-IIKPKDV--SIGYLAQNTGL 77
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRpgECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSIltNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 78 ETSLTIWDEMLTVFTHLqQMETKLRRL-EQEMGKEENFSNEATYERLLADYdqlqlnykdqggyqyeadirsiLSGlgfp 156
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHL-YLYARLRGVpAEEIEKVANWSIQSLGLSLYADR----------------------LAG---- 2069
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 157 vethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:TIGR01257 2070 ---------TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
332-480 |
4.14e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 51.62 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsNVSVGYYDQE---------- 401
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATTPSRelakrlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKRVLNEL--WDEYP-----LQPE-KEI--RTIlgNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:COG4604 82 QENHINSRLTVRELvaFGRFPyskgrLTAEdREIidEAI--AYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
....*....
gi 446524801 472 DEPTNHLDL 480
Cdd:COG4604 160 DEPLNNLDM 168
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
331-517 |
4.62e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSivnkLPLLNGDVSFGSNVSVGYYDQEQANLTSSKR 410
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRV----LNLLETPDSGQLNIAGHQFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 VLNE----LWDEYPLQPEkeiRTILGNFLFTGDDVLKPVSS-------------------------LSGGQKARLALAKL 461
Cdd:COG4161 79 LLRQkvgmVFQQYNLWPH---LTVMENLIEAPCKVLGLSKEqarekamkllarlrltdkadrfplhLSGGQQQRVAIARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 462 MMQKSNLLILDEPTNHLDLN-SKEILE--NALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEiTAQVVEiiRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
328-504 |
5.01e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.03 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI-----------------VNKLPLLNGDV--- 387
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVaglekptegqifidgedVTHRSIQQRDIcmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 388 ----------SFGSNVSVGYYDQEQANLTSSKRVLN--ELWDeyplqpekeirtiLGNFlftGDdvlKPVSSLSGGQKAR 455
Cdd:PRK11432 84 fqsyalfphmSLGENVGYGLKMLGVPKEERKQRVKEalELVD-------------LAGF---ED---RYVDQISGGQQQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLDLNSKEILENALID----YPGTLLFVSHDR 504
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
326-592 |
5.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 326 SGNDVLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsIVNKLPL---------------LNGDVS 388
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISK-LINGLLLpddnpnskitvdgitLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 389 FGSNVSVGYYDQEQANLTSSKRVLNELwdEYPLQ----PEKEIRTILgnflftgDDVLKPV----------SSLSGGQKA 454
Cdd:PRK13640 80 WDIREKVGIVFQNPDNQFVGATVGDDV--AFGLEnravPRPEMIKIV-------RDVLADVgmldyidsepANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKE----ILENALIDYPGTLLFVSHDryfINRVTTTVVELSTEGAQEYLGDYD 530
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEqilkLIRKLKKKNNLTVISITHD---IDEANMADQVLVLDDGKLLAQGSP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 531 YYVEKKNEMIERAELeqqesDVP-VQKVVaqeklNYLEEKERKQLERQRTRkiEELEQSIVEL 592
Cdd:PRK13640 228 VEIFSKVEMLKEIGL-----DIPfVYKLK-----NKLKEKGISVPQEINTE--EKLVQYLCQL 278
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
345-503 |
6.68e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSVgyYDQEQANLTSSKRV------------ 411
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQ--MDEEARAKLRAKHVgfvfqsfmlipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 LNELWD---------EYPLQPEKEIRTILGNfLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS 482
Cdd:PRK10584 103 LNALENvelpallrgESSRQSRNGAKALLEQ-LGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*
gi 446524801 483 KEILENALI----DYPGTLLFVSHD 503
Cdd:PRK10584 182 GDKIADLLFslnrEHGTTLILVTHD 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
159-199 |
6.81e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 6.81e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446524801 159 THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK10982 384 GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-503 |
6.97e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNGDV--SFGSnVSV-GY--YDQEQANLtssKR---VL---NE 414
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIK-------MLTGILvpTSGE-VRVlGYvpFKRRKEFA---RRigvVFgqrSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 415 LWDEYPLQ------------PEKEIRTILGNF--LFTGDDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:COG4586 107 LWWDLPAIdsfrllkaiyriPDAEYKKRLDELveLLDLGELLdTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180
....*....|....*....|....*...
gi 446524801 480 LNSKEILENALIDY----PGTLLFVSHD 503
Cdd:COG4586 187 VVSKEAIREFLKEYnrerGTTILLTSHD 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-503 |
7.00e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 337 TIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLP------LLNGDVSFGSNVSVGYYDQeqanLTSSKR 410
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNdkvsgyRYSGDVLLGGRSIFNYRDV----LEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 V--LNELWDEYPLQ---------------PEKEIR-------TILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKS 466
Cdd:PRK14271 103 VgmLFQRPNPFPMSimdnvlagvrahklvPRKEFRgvaqarlTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524801 467 NLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHD 503
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
331-504 |
7.10e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.62 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS--------VGYYDQE 401
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVSrlhardrkVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QA---------NLTSSKRVLnelwdeyplqPEKE------IRTILGNFLftgdDVLK--------PvSSLSGGQKARLAL 458
Cdd:PRK10851 83 YAlfrhmtvfdNIAFGLTVL----------PRRErpnaaaIKAKVTQLL----EMVQlahladryP-AQLSGGQKQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 459 AKLMMQKSNLLILDEPTNHLDLN-SKEI---LENALIDYPGTLLFVSHDR 504
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQvRKELrrwLRQLHEELKFTSVFVTHDQ 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-201 |
7.24e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 50.57 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGylaqntGLETSlTIwdemltvftH 93
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL------ID------GVDIS-KI---------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 94 LQQMETKLRRLEQEmgkEENFS----------NEATYERLLADYDQLQLNykdqggyqyeADIRSILSGLGFPVETHQtt 163
Cdd:cd03244 73 LHDLRSRISIIPQD---PVLFSgtirsnldpfGEYSDEELWQALERVGLK----------EFVESLPGGLDTVVEEGG-- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524801 164 iSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03244 138 -ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
331-515 |
7.56e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 50.72 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLPLLNGDVSF-GSN--------------- 392
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFkGQDllelepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 393 -----------VSVGYYDQEQANLTSSKRVLNELWDeypLQPEKEIRTIL------GNFLFTGDDVlkpvsSLSGGQKAR 455
Cdd:TIGR01978 81 lafqypeeipgVSNLEFLRSALNARRSARGEEPLDL---LDFEKLLKEKLalldmdEEFLNRSVNE-----GFSGGEKKR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLDLNS-KEILE--NALIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDAlKIVAEgiNRLREPDRSFLIITHYQRLLNYIKPDYV 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
328-503 |
7.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.27 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLLN-GDVS-FGSNVS---------- 394
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-NGIYLPQrGRVKvMGREVNaenekwvrsk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQEQANLTSSKRVlnelWDEYPLQPEkeirtilgNFLFTGDDVL-----------------KPVSSLSGGQKARLA 457
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTV----WDDVAFGPV--------NMGLDKDEVErrveealkavrmwdfrdKPPYHLSYGQKKRVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524801 458 LAKLMMQKSNLLILDEPTNHLDLNSKEILE---NALIDYPGTLLFVSHD 503
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMeilDRLHNQGKTVIVATHD 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-198 |
8.15e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 9 LSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDV---SIgylaQNTgletSLTIW 84
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGEDVthrSI----QQR----DICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 85 DEMLTVFTHLQQMETKLRRLE-QEMGKEEnfSNEATYERL-LADYDQLQLNYKDQggyqyeadirsilsglgfpvethqt 162
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKmLGVPKEE--RKQRVKEALeLVDLAGFEDRYVDQ------------------------- 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 446524801 163 tistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11432 137 ----ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-200 |
8.60e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 50.57 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHdGGEIIKPKDVSIGYL----- 71
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRV-GGEEIRLKPDRDGELvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 72 AQNTGLETSLT-------IWDEMlTVfthLQQ-METKLRRLEqeMGKEENfsnEATYERLLADYdqlqlnykdqggyqye 143
Cdd:COG4598 88 RQLQRIRTRLGmvfqsfnLWSHM-TV---LENvIEAPVHVLG--RPKAEA---IERAEALLAKV---------------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 144 adirsilsGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:COG4598 143 --------GLA---DKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
353-503 |
8.62e-07 |
|
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: 49.28 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 353 LTRGDSVALVGPNGIGKSTLLKSIvnklpllnGDVSFGSNVSVGYYDQEQANLTSSkrvlnelwdeyplQPEKEIRTIlg 432
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGVKAGCIVA-------------AVSAELIFT-- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 433 nflftgddvlkpVSSLSGGQKARLALAKLM----MQKSNLLILDEPTNHLDLNSKEILENALIDY---PGTLLFVSHD 503
Cdd:cd03227 75 ------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHL 140
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
332-480 |
8.67e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgsnvsvgyyDQEQANLTSSKRV 411
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL---------DAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 LNELwdEY-PLQ-PEKEIRTI-----LGNFLFTG-------------DDV-----LKP-----VSSLSGGQKARLALAKL 461
Cdd:PRK10575 84 ARKV--AYlPQQlPAAEGMTVrelvaIGRYPWHGalgrfgaadrekvEEAislvgLKPlahrlVDSLSGGERQRAWIAML 161
|
170
....*....|....*....
gi 446524801 462 MMQKSNLLILDEPTNHLDL 480
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDI 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-221 |
8.75e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIgylaQNT--GLETS 80
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlIDGQEMRF----ASTtaALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 81 LTIwdemltVFTHLQqmetklrrLEQEMGKEENFsneatyerLLAdydqlQLNYK----DQGGYQYEAdiRSILSGLGFP 156
Cdd:PRK11288 81 VAI------IYQELH--------LVPEMTVAENL--------YLG-----QLPHKggivNRRLLNYEA--REQLEHLGVD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 157 VEThQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSH 221
Cdd:PRK11288 132 IDP-DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH 198
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
331-479 |
8.78e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSivnkLPLL----NGDVSFGSNvsvgYYDQEQANLT 406
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLemprSGTLNIAGN----HFDFSKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 407 SSKRVLNE----LWDEYPLQP---------EKEIRtILG----NFLFTGDDVLK-----------PVSsLSGGQKARLAL 458
Cdd:PRK11124 75 KAIRELRRnvgmVFQQYNLWPhltvqqnliEAPCR-VLGlskdQALARAEKLLErlrlkpyadrfPLH-LSGGQQQRVAI 152
|
170 180
....*....|....*....|.
gi 446524801 459 AKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALD 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
325-590 |
9.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 325 QSGNDVLQVNDATIGYD---ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP-------LLNGDVSFGSNVS 394
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaetssvVIRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQEQAN-LTSSKRVLNELW---DEYPLQPEKEirtilgnfLFTGDDVLKPVS---SLSGGQKARLALAKLMMQKSN 467
Cdd:PLN03232 689 WIFNATVRENiLFGSDFESERYWraiDVTALQHDLD--------LLPGRDLTEIGErgvNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 468 LLILDEPTNHLDLNSKEILENALIDYP---GTLLFVSHDRYFINRVTTTVveLSTEGAQEYLGDYDyYVEKKNEMIER-- 542
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDSCMKDElkgKTRVLVTNQLHFLPLMDRII--LVSEGMIKEEGTFA-ELSKSGSLFKKlm 837
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 543 -------AELEQQESDVPVQKVVAQEKLNYLEEKERKQLERQRTRKI----EELEQSIV 590
Cdd:PLN03232 838 enagkmdATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVlvkqEERETGII 896
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
331-490 |
9.92e-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: 52.22 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDE--NPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvnkLPLLNGD-------VSFGS------NVSV 395
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEgeiqidgVSWNSvtlqtwRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 396 GYYDQE--------QANLTSSKRVLN-ELWDeypLQPEKEIRTILGNFLFTGDDVLKPVSS-LSGGQKARLALAKLMMQK 465
Cdd:TIGR01271 1295 GVIPQKvfifsgtfRKNLDPYEQWSDeEIWK---VAEEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSK 1371
|
170 180
....*....|....*....|....*
gi 446524801 466 SNLLILDEPTNHLDLNSKEILENAL 490
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-502 |
1.02e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSvgyydQEQANLTS-SKRV-LNELWDEYPLQ 422
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdGVDIT-----DKKVKLSDiRKKVgLVFQYPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 423 PE---KEIRTILGNFLFTGDDVLKPVSS-------------------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK13637 98 EEtieKDIAFGPINLGLSEEEIENRVKRamnivgldyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180
....*....|....*....|....*...
gi 446524801 481 NSK-EILEnaLI-----DYPGTLLFVSH 502
Cdd:PRK13637 178 KGRdEILN--KIkelhkEYNMTIILVSH 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
329-503 |
1.08e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 329 DVLQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVS-FGSNVS-------VGYYD 399
Cdd:PRK15056 5 AGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 QEQaNLTSSKRVLNE---LWDEYP-----LQPEKEIRTILGNFLFTGDDV---LKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK15056 85 QSE-EVDWSFPVLVEdvvMMGRYGhmgwlRRAKKRDRQIVTAALARVDMVefrHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524801 469 LILDEPTNHLDLNSKE---ILENALIDYPGTLLFVSHD 503
Cdd:PRK15056 164 ILLDEPFTGVDVKTEAriiSLLRELRDEGKTMLVSTHN 201
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
332-519 |
1.21e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.50 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYD-ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLLNG--DVSFGSnVSVGYYDQEQANLTSS 408
Cdd:PRK13657 336 EFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLIN-------LLQRvfDPQSGR-ILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNELWDEYPL------------QP---EKEIRTILG-----NFLFTGDDVLKPV-----SSLSGGQKARLALAKLMM 463
Cdd:PRK13657 408 RRNIAVVFQDAGLfnrsiednirvgRPdatDEEMRAAAEraqahDFIERKPDGYDTVvgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 464 QKSNLLILDEPTNHLDLNSKEILENALIDypgtllfVSHDRyfinrvTTTVV--ELST 519
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDE-------LMKGR------TTFIIahRLST 532
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
329-491 |
1.22e-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: 51.94 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 329 DVLQVNDATIGYD--ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFG-----SNVS-----VG 396
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgksilTNISdvhqnMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 397 YYDQEQA--NLTSSKRVLnELWDEYPLQPEKEIRTI-------LGNFLFTgdDVLkpVSSLSGGQKARLALAKLMMQKSN 467
Cdd:TIGR01257 2016 YCPQFDAidDLLTGREHL-YLYARLRGVPAEEIEKVanwsiqsLGLSLYA--DRL--AGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180
....*....|....*....|....
gi 446524801 468 LLILDEPTNHLDLNSKEILENALI 491
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-198 |
1.47e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSiGYLAQNTGLET-- 79
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImLDGQDIT-HVPAENRHVNTvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 80 -SLTIWDEMlTVFthlQQMETKLRrleqeMGKeenFSNEATYERLLadyDQLQLnykdqggyqyeadIRsiLSGLGfpve 158
Cdd:PRK09452 93 qSYALFPHM-TVF---ENVAFGLR-----MQK---TPAAEITPRVM---EALRM-------------VQ--LEEFA---- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 159 thQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK09452 139 --QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-199 |
1.52e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGgeiiKPKDVSIgylaqnTGletSLT 82
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGG----APRGARV------TG---DVT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 83 IWDEMLTVFTHLQQmeTKLRRLEQEMGkEENFSNEATYERLLADYDQLQ----LNYKDqGGYQYEADIRSILSGLGfpve 158
Cdd:PRK13547 68 LNGEPLAAIDAPRL--ARLRAVLPQAA-QPAFAFSAREIVLLGRYPHARragaLTHRD-GEIAWQALALAGATALV---- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 159 thQTTISTLSGGQKTRLALGKLL---------LTKPDLLILDEPTNHLDI 199
Cdd:PRK13547 140 --GRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
328-517 |
1.64e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKL--PLLNGDVSFGSNVS--------VGY 397
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLekPSEGSIVVNGQTINlvrdkdgqLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 398 YDQEQANLTSSKRVLN----ELWD---------EYPLQ------PEKEIRTI--LGNFLFTGDDVLKPVSSLSGGQKARL 456
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVfqhfNLWShmtvlenvmEAPIQvlglskQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 457 ALAKLMMQKSNLLILDEPTNHLDLN-SKEILE--NALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPElVGEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-198 |
1.83e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDV-----S 67
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsAGKIWFSGHDItrLKNREVpflrrQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 IGYLAQNTGLETSLTIWDEMLTVFTHLQQMETKLRRleqemgkeenfsneatyeRLLADYDQLQLNYKDQGgyqyeadir 147
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRR------------------RVSAALDKVGLLDKAKN--------- 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 148 silsglgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK10908 134 -------FPIQ--------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-198 |
2.03e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSIGY 70
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrvvneLEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLetsltiWDEMlTVFthlQQME--TKLRRleqeMGKEEnfsneaTYERLLADYDQLQLnykdqGGYqyeADIRs 148
Cdd:PRK11650 81 VFQNYAL------YPHM-SVR---ENMAygLKIRG----MPKAE------IEERVAEAARILEL-----EPL---LDRK- 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 149 ilsglgfPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11650 132 -------PRE--------LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-503 |
2.10e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNG-------DVSF-----GSNVSVGYYDQEQA---- 403
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddeDISLlplhaRARRGIGYLPQEASifrr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 404 ---------------NLTSSKRV--LNELWDEYPLQpekEIRTILGNflftgddvlkpvsSLSGGQKARLALAKLMMQKS 466
Cdd:PRK10895 93 lsvydnlmavlqirdDLSAEQREdrANELMEEFHIE---HLRDSMGQ-------------SLSGGERRRVEIARALAANP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 467 NLLILDEPTNHLD----LNSKEILENaLIDYPGTLLFVSHD 503
Cdd:PRK10895 157 KFILLDEPFAGVDpisvIDIKRIIEH-LRDSGLGVLITDHN 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-227 |
2.16e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 49.30 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSH--DGGEII-KPKDVsigylaqnTGLETsltiwDEM------ 87
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILlDGEDI--------LELSP-----DERaragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 88 -----------LTVFTHLQQMETKLRRLEQEMGKEENFSNEATYE-RLLADYDQLQLNYkdqggyqyeadirsilsglGF 155
Cdd:COG0396 81 lafqypveipgVSVSNFLRTALNARRGEELSAREFLKLLKEKMKElGLDEDFLDRYVNE-------------------GF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 156 pvethqttistlSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY--PG-AILIVSHDRYFLD 227
Cdd:COG0396 142 ------------SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDrGILIITHYQRILD 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-503 |
2.18e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 349 VTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVsVGYYDQEQANLtsSKRVLNELWDEY-PLQPEKE 426
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDL-LKADPEAQKLL--RQKIQIVFQNPYgSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 427 IRTILGNFLFTGDDV-----------------LKPVSS------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK 483
Cdd:PRK11308 111 VGQILEEPLLINTSLsaaerrekalammakvgLRPEHYdryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180
....*....|....*....|....
gi 446524801 484 EILENALIDYPGTL----LFVSHD 503
Cdd:PRK11308 191 AQVLNLMMDLQQELglsyVFISHD 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-222 |
2.20e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 9 LSKLY---GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIagelshdgGEIIKPKDvsigylaqntgleTSLTIWD 85
Cdd:PRK14246 13 ISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--------NRLIEIYD-------------SKIKVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 86 EMLTVFTHLQQMETKlrRLEQEMGKEENFSNEATYerlLADYDQLQLNYKDQGgYQYEADIRSI----LSGLGFPVETH- 160
Cdd:PRK14246 72 KVLYFGKDIFQIDAI--KLRKEVGMVFQQPNPFPH---LSIYDNIAYPLKSHG-IKEKREIKKIveecLRKVGLWKEVYd 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 161 --QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:PRK14246 146 rlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
344-514 |
2.22e-06 |
|
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: 49.12 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 344 PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKsIVNKL--PLlNGDVS-FGSNVS-------------VGYYDQeQANLTS 407
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLerPT-SGSVLvDGTDLTllsgkelrkarrrIGMIFQ-HFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 SKRVLNELwdEYPLQ----PEKEIR---TILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:cd03258 96 SRTVFENV--ALPLEiagvPKAEIEervLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 481 NS-KEILE-----NALIDYpgTLLFVSHDRYFINRVTTTV 514
Cdd:cd03258 174 ETtQSILAllrdiNRELGL--TIVLITHEMEVVKRICDRV 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
326-488 |
2.38e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 326 SGNDVLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLK----------------------------- 374
Cdd:PRK10789 309 EGRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSliqrhfdvsegdirfhdipltklqldswr 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 375 ---SIVNKLPLLNGDvSFGSNVSVGYYDQEQANLTSSKRVLNELWDEYPL----QPEKEIRTILgnflftgddvlkpvss 447
Cdd:PRK10789 389 srlAVVSQTPFLFSD-TVANNIALGRPDATQQEIEHVARLASVHDDILRLpqgyDTEVGERGVM---------------- 451
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524801 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EILEN 488
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHN 493
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
330-530 |
2.47e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.40 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLL------NGDVSF-GSNVsvgyYDQEQ 402
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCF-NRLNDLipgfrvEGKVTFhGKNL----YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 403 ANLTSSKRVLNELWDEYPLQpekeiRTILGNFLF-------TGD-------------------DVLKPV-SSLSGGQKAR 455
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPFP-----KSIYDNIAYgaringyKGDmdelverslrqaalwdevkDKLKQSgLSLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYpgTLLFVSHDRYFINRVTTTV----VELSTEGAQE-YL 526
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDpistLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTaffnVELTEGGGRYgYL 237
|
....
gi 446524801 527 GDYD 530
Cdd:PRK14243 238 VEFD 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
153-201 |
2.49e-06 |
|
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: 48.20 E-value: 2.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 153 LGFPVETHQTTISTLSGG--QKtrLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03215 91 LDLSVAENIALSSLLSGGnqQK--VVLARWLARDPRVLILDEPTRGVDVGA 139
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-222 |
2.70e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGYLAQNTGLETSltiwdemltvfthlqqme 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI------VGDYAIPANLKKI------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 99 TKLRRLEQEMGKEENFSN----EATYERLLAdYDQLQLNYKDQGGYQyeaDIRSILSGLGFPVETHQTTISTLSGGQKTR 174
Cdd:PRK13645 83 KEVKRLRKEIGLVFQFPEyqlfQETIEKDIA-FGPVNLGENKQEAYK---KVPELLKLVQLPEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524801 175 LALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHN 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
346-503 |
2.91e-06 |
|
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: 49.00 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVN-KLP-----LLNGD----------VSFgSNVSVGYYDQEQANLT-SS 408
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPtsggvILEGKqitepgpdrmVVF-QNYSLLPWLTVRENIAlAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 409 KRVLNELwdeyplqPEKEIRTILGNFLFT---GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEI 485
Cdd:TIGR01184 80 DRVLPDL-------SKSERRAIVEEHIALvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|..
gi 446524801 486 LENALI----DYPGTLLFVSHD 503
Cdd:TIGR01184 153 LQEELMqiweEHRVTVLMVTHD 174
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
346-503 |
2.97e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgsnvsVGYydqeQANLTSSKRVLNELWDEYPLQ--- 422
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI-----AGY----HITPETGNKNLKKLRKKVSLVfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 423 PEKEI--RTILG-------NFLFTGDDV-------LKPVS-----------SLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PRK13641 94 PEAQLfeNTVLKdvefgpkNFGFSEDEAkekalkwLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190
....*....|....*....|....*....|.
gi 446524801 476 NHLDLNSKEILENALIDYPG---TLLFVSHD 503
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-218 |
3.03e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.35 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 15 AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkdVSIGylaqntgletsltiwdEMLTVFTHL 94
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK------VTVG----------------DIVVSSTSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 95 QQmetKLRRLEQEMGKEENFSNEATYERLLadYDQLQLNYKDQGGYQYEAD--IRSILSGLGFPVETHQTTISTLSGGQK 172
Cdd:PRK13643 76 QK---EIKPVRKKVGVVFQFPESQLFEETV--LKDVAFGPQNFGIPKEKAEkiAAEKLEMVGLADEFWEKSPFELSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524801 173 TRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILI 218
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQTVVLV 200
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-82 |
3.17e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 3.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIgyLAQNTGLETSLT 82
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV--IAISAGLSGQLT 101
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-198 |
3.28e-06 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 49.41 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 34 LVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQNTGLetsltiwdemltvFTHLQQMETKLRRL 104
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMldgedvtnvPPHLRHINMVFQSYAL-------------FPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 105 E-QEMGKEEnfsneaTYERLLADYDQLQLNykdqggyqyeadirsilsglgfpvETHQTTISTLSGGQKTRLALGKLLLT 183
Cdd:TIGR01187 68 KmRKVPRAE------IKPRVLEALRLVQLE------------------------EFADRKPHQLSGGQQQRVALARALVF 117
|
170
....*....|....*
gi 446524801 184 KPDLLILDEPTNHLD 198
Cdd:TIGR01187 118 KPKILLLDEPLSALD 132
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-503 |
3.36e-06 |
|
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: 48.90 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 356 GDSVALVGPNGIGKSTLLKSIVNKL------------------------------PLLNGDVSfgSNVSVGYYDQEQANL 405
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddppdwdeildefrgselqnyftKLLEGDVK--VIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 TSSKRVLNELWDEYPLQPE----KEIRTILGNflftgddvlkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-- 479
Cdd:cd03236 104 KGKVGELLKKKDERGKLDElvdqLELRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDik 173
|
170 180
....*....|....*....|....*.
gi 446524801 480 --LNSKEILENaLIDYPGTLLFVSHD 503
Cdd:cd03236 174 qrLNAARLIRE-LAEDDNYVLVVEHD 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
349-515 |
3.88e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.59 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 349 VTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLP------LLNGDVSFGSNVSVGyydQEQA----------------NLT 406
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEqpeagtIRVGDITIDTARSLS---QQKGlirqlrqhvgfvfqnfNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 407 SSKRVLNELWdEYPLQPEKEI--------RTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:PRK11264 98 PHRTVLENII-EGPVIVKGEPkeeataraRELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 479 DLN-SKEILEN--ALIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:PRK11264 176 DPElVGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-198 |
3.99e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.03 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 16 ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkDVSIGYLAQNTGLETSLTIWDEMLTVFthlq 95
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP-----NSKITVDGITLTAKTVWDIREKVGIVF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 96 qmetklrrleqemgkeENFSNE---ATYErlladyDQLQLNYKDQGGYQYEAD--IRSILSGLGFpVETHQTTISTLSGG 170
Cdd:PRK13640 91 ----------------QNPDNQfvgATVG------DDVAFGLENRAVPRPEMIkiVRDVLADVGM-LDYIDSEPANLSGG 147
|
170 180
....*....|....*....|....*...
gi 446524801 171 QKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
332-479 |
4.00e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKL-------PLLNGDVSFGSNV--SVGYYDQEQ 402
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgTILANNRKPTKQIlkRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 403 ---ANLT--------SSKRVLNELW-DEYPLQPEKEI---------RTILGNFLFTGddvlkpvssLSGGQKARLALAKL 461
Cdd:PLN03211 150 ilyPHLTvretlvfcSLLRLPKSLTkQEKILVAESVIselgltkceNTIIGNSFIRG---------ISGGERKRVSIAHE 220
|
170
....*....|....*...
gi 446524801 462 MMQKSNLLILDEPTNHLD 479
Cdd:PLN03211 221 MLINPSLLILDEPTSGLD 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
345-479 |
4.01e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP---------LLNG---DVSFGSNVSvGYYDQE----------- 401
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGmpiDAKEMRAIS-AYVQQDdlfiptltvre 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 ----------QANLTSSKRVL--NELWDEYPLQPEKEirTILGnflftgddVLKPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:TIGR00955 119 hlmfqahlrmPRRVTKKEKRErvDEVLQALGLRKCAN--TRIG--------VPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170
....*....|
gi 446524801 470 ILDEPTNHLD 479
Cdd:TIGR00955 189 FCDEPTSGLD 198
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-229 |
4.02e-06 |
|
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: 49.23 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 24 LEVQTKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWDEMLTVFTHL------QQ 96
Cdd:COG3593 17 LSIELSDDLtVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSRLLRLLlkeedkEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 97 METKLRRLEQEMGKE-ENFSNE-ATYERLLADYDQLQLNYKdqggyqyEADIRSILSGLGFPVET-HQTTISTLSGGQKT 173
Cdd:COG3593 97 LEEALEELNEELKEAlKALNELlSEYLKELLDGLDLELELS-------LDELEDLLKSLSLRIEDgKELPLDRLGSGFQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 174 R--LALGKLLL-----TKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHDRYFLDKL 229
Cdd:COG3593 170 LilLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-223 |
4.10e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGgeiikpkDVSIGYLAQNTgleTSLTIWDEMLTVFTh 93
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-------DIQIDGVSWNS---VPLQKWRKAFGVIP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 94 lqqmetklrrleqemgkEENFSNEATYERLLADYDQlqlnYKDQGGYQY--EADIRSILSglGFPVETHQTTIS---TLS 168
Cdd:cd03289 84 -----------------QKVFIFSGTFRKNLDPYGK----WSDEEIWKVaeEVGLKSVIE--QFPGQLDFVLVDggcVLS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 169 GGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-QGYPGAILIVSHDR 223
Cdd:cd03289 141 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
160-510 |
4.75e-06 |
|
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: 49.68 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 160 HQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQyLQGYPG-AILIVSHDryfLDkLVtqvy 234
Cdd:COG4172 155 HQ-----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaQILDLLKD-LQRELGmALLLITHD---LG-VV---- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 235 eisnkesRRFVgnyskyldlksalyeqemkryekqqDEIAkledfVQKN--IARASTTKR--AQSR----RKQLD-RMEL 305
Cdd:COG4172 221 -------RRFA-------------------------DRVA-----VMRQgeIVEQGPTAElfAAPQhpytRKLLAaEPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 306 LTRPLGDSKSAsfhfdiekqsgndVLQVNDATIGY-----------DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLK 374
Cdd:COG4172 264 DPRPVPPDAPP-------------LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 375 SIvnkLPLLN--GDVSFGsnvsvgyyDQEQANLTSS------KRV----------LN------ELWDEyPL--------- 421
Cdd:COG4172 331 AL---LRLIPseGEIRFD--------GQDLDGLSRRalrplrRRMqvvfqdpfgsLSprmtvgQIIAE-GLrvhgpglsa 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 422 -QPEKEIRTILgnflftgDDV-LKPVS------SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLnS--KEILEnALI 491
Cdd:COG4172 399 aERRARVAEAL-------EEVgLDPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SvqAQILD-LLR 469
|
410 420
....*....|....*....|....*..
gi 446524801 492 D----YPGTLLFVSHD----RYFINRV 510
Cdd:COG4172 470 DlqreHGLAYLFISHDlavvRALAHRV 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-304 |
5.00e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSH--DGGEIIKPkdvSIGYLAQNTGLETSlTIWDEMLtvfthlqq 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG---SVAYVPQVSWIFNA-TVRENIL-------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 97 metklrrleqemgkeenFSNEATYERLLADYDQLQLnykdqggyQYEADIrsilsglgFP----VETHQTTIStLSGGQK 172
Cdd:PLN03232 701 -----------------FGSDFESERYWRAIDVTAL--------QHDLDL--------LPgrdlTEIGERGVN-ISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 173 TRLALGKLLLTKPDLLILDEPTNHLDIETL-----TWLEQYLQGypGAILIVSHDRYFL---DKLVTqVYEISNKESRRF 244
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAhqvfdSCMKDELKG--KTRVLVTNQLHFLplmDRIIL-VSEGMIKEEGTF 823
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 245 VgNYSKYLDLKSALYEQEMKRYEKQQ-----DEIAKLEDFVQKNIA--RASTTKRAQSRRKQLDRME 304
Cdd:PLN03232 824 A-ELSKSGSLFKKLMENAGKMDATQEvntndENILKLGPTVTIDVSerNLGSTKQGKRGRSVLVKQE 889
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-221 |
5.13e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTllkiIAGELSHdggeiikpkdvsigyLAQNTGleTSLTIWDEMLTVFTHlQQM 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST----VAALLQN---------------LYQPTG--GQVLLDGVPLVQYDH-HYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 98 ETKLRRLEQE---MGKeeNFSNEATYERLLADYDQLQLNYKDQGGYQYEAdirsilsglGFPvETHQTTI----STLSGG 170
Cdd:TIGR00958 554 HRQVALVGQEpvlFSG--SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM---------EFP-NGYDTEVgekgSQLSGG 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 171 QKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQGYPGA----ILIVSH 221
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSRasrtVLLIAH 672
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-198 |
5.14e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.47 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDV-----SIGYLAQNT------------ 75
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvLSEETVwdvrrQVGMVFQNPdnqfvgatvqdd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 76 ---GLETSLTIWDEMLtvfthlqqmetklRRLEQEMgKEENFSNEATYErlladydqlqlnykdqggyqyeadirsilsg 152
Cdd:PRK13635 103 vafGLENIGVPREEMV-------------ERVDQAL-RQVGMEDFLNRE------------------------------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524801 153 lgfPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13635 138 ---P--------HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-201 |
5.25e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.62 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 33 ALVGRNGAGKSTLLKIIAG--ELSHDGGEII---KPKDVS----IGYLAQNTGLETSLTIwdemltvfthlqqmetklrr 103
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAGrkTAGVITGEILingRPLDKNfqrsTGYVEQQDVHSPNLTV-------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 104 leqemgkeenfsneatYERLLadydqlqlnykdqggyqYEADIRSilsglgfpvethqttistLSGGQKTRLALGKLLLT 183
Cdd:cd03232 97 ----------------REALR-----------------FSALLRG------------------LSVEQRKRLTIGVELAA 125
|
170
....*....|....*...
gi 446524801 184 KPDLLILDEPTNHLDIET 201
Cdd:cd03232 126 KPSILFLDEPTSGLDSQA 143
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-198 |
5.35e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 48.90 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG---ELSHDGGEII-KPKDVS------- 67
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILfDGEDLLklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 -------IGYLAQNTGleTSLtiwDEMLTVFTHLqqMETkLRRLeQEMGKEEnfSNEATYERLladyDQLQLNykdqggy 140
Cdd:COG0444 81 rkirgreIQMIFQDPM--TSL---NPVMTVGDQI--AEP-LRIH-GGLSKAE--ARERAIELL----ERVGLP------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 141 QYEADIRSilsglgFPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG0444 139 DPERRLDR------YP---HE-----LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-479 |
5.78e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.55 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKLPLLNGdvsfgSNVSVGYYDQEQANLTSSKR----------- 410
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHM-NALLIPSE-----GKVYVDGLDTSDEENLWDIRnkagmvfqnpd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 411 ---VLNELWDEYPLQPE------KEIRTILgnflftgDDVLKPVSS----------LSGGQKARLALAKLMMQKSNLLIL 471
Cdd:PRK13633 96 nqiVATIVEEDVAFGPEnlgippEEIRERV-------DESLKKVGMyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIF 168
|
....*...
gi 446524801 472 DEPTNHLD 479
Cdd:PRK13633 169 DEPTAMLD 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
331-503 |
6.59e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF------GSNVSVGYYDQEQAN 404
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 405 LTSSKRVLN-----ELWDEYPLQPEKEIRTILGNFLFTGDDVlKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK11248 82 LPWRNVQDNvafglQLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 446524801 480 LNSKEILENALI----DYPGTLLFVSHD 503
Cdd:PRK11248 161 AFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
330-490 |
6.64e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLPLLNGDVSFgSNVSVGYYDQEQ-ANL- 405
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILF-KGESILDLEPEErAHLg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 -----------------------TSSKRVLNELWDEYPLQPEKEIRTILG----NFLFTGDDVLKpvsSLSGGQKARLAL 458
Cdd:CHL00131 86 iflafqypieipgvsnadflrlaYNSKRKFQGLPELDPLEFLEIINEKLKlvgmDPSFLSRNVNE---GFSGGEKKRNEI 162
|
170 180 190
....*....|....*....|....*....|..
gi 446524801 459 AKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGI 194
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
443-509 |
7.11e-06 |
|
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: 46.93 E-value: 7.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 443 KPVSSLSGGQKARLALAKLMMQKS--NLLILDEPTNHLDLNSKEILENA---LIDYPGTLLFVSHDRYFINR 509
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLDVLSS 154
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-194 |
7.67e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 47.80 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------IGY 70
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLfGGTDLTgldeheiarlgIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 71 LAQNTGLETSLTIWDEML-------TVFTHLqqmetkLRRLEQEMgkeenfsnEATYERLLadyDQLQLnykdqggyqye 143
Cdd:COG4674 90 KFQKPTVFEELTVFENLElalkgdrGVFASL------FARLTAEE--------RDRIEEVL---ETIGL----------- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 144 ADIRSILSGLgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:COG4674 142 TDKADRLAGL-------------LSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
325-590 |
8.10e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 325 QSGNDVLQVNDATIGYD---ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNgDVSFGSNVSVGYYDQE 401
Cdd:PLN03130 609 EPGLPAISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-DASVVIRGTVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 Q--ANLTSSKRVLNELwdeyPLQPEKEIRTILGNFLFTGDDVLkPVSSL----------SGGQKARLALAKLMMQKSNLL 469
Cdd:PLN03130 688 SwiFNATVRDNILFGS----PFDPERYERAIDVTALQHDLDLL-PGGDLteigergvniSGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 470 ILDEPTNHLDLN-SKEILENALIDYPG--TLLFVSHDRYFINRVTTTVV-------------ELSTEGA-----QEYLGD 528
Cdd:PLN03130 763 IFDDPLSALDAHvGRQVFDKCIKDELRgkTRVLVTNQLHFLSQVDRIILvhegmikeegtyeELSNNGPlfqklMENAGK 842
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 529 YDYYVEKKNEmieraELEQQESDVPVQKVVAQEKLNYLEEKERKQLERQRTRKIEELEQSIV 590
Cdd:PLN03130 843 MEEYVEENGE-----EEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVV 899
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-490 |
8.10e-06 |
|
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: 47.49 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVS-VGYYD------- 399
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISkIGLHDlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 400 --QEQANLTSSKRV----LNELWDEYPLQPEKE--IRTILGNFLFTGDDVLKPV-SSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:cd03244 83 ipQDPVLFSGTIRSnldpFGEYSDEELWQALERvgLKEFVESLPGGLDTVVEEGgENLSVGQRQLLCLARALLRKSKILV 162
|
170 180
....*....|....*....|
gi 446524801 471 LDEPTNHLDLNSKEILENAL 490
Cdd:cd03244 163 LDEATASVDPETDALIQKTI 182
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-201 |
8.61e-06 |
|
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: 47.93 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 12 LYGAeTILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIgylaqntgleTSLTIWDEMLTVf 91
Cdd:cd03291 47 LVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISF----------SSQFSWIMPGTI- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 92 thlqqmetklrrleqemgkEENFSNEATYErlladydqlQLNYKDQ-GGYQYEADIrsilsgLGFPvETHQTTIS----T 166
Cdd:cd03291 115 -------------------KENIIFGVSYD---------EYRYKSVvKACQLEEDI------TKFP-EKDNTVLGeggiT 159
|
170 180 190
....*....|....*....|....*....|....*
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-197 |
9.08e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 47.69 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEI--IKPKDVSIGYLAQNTGLETSL------TIWDEMLT 89
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLddVKFRKLLIRNGEFGDSAKLILyygtsrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 90 VFTHL-QQMETKLRRLEQEMGKEENFSNEATYerLLADYDQLQLNYKDQGGYQYEAdIRSILSGLgFP------------ 156
Cdd:COG3950 94 KLERLkEEYFSRLDGYDSLLDEDSNLREFLEW--LREYLEDLENKLSDELDEKLEA-VREALNKL-LPdfkdiridrdpg 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 157 ----VETHQTTIS--TLSGGQKTRLAL--------------GKLLLTKPDLLILDEPTNHL 197
Cdd:COG3950 170 rlviLDKNGEELPlnQLSDGERSLLALvgdlarrlaelnpaLENPLEGEGIVLIDEIDLHL 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
345-503 |
1.17e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.57 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLksivNKLPLLNGDVS-----FGSNVS--------------VGYYDQEQ--- 402
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLM----NILGCLDKPTSgtyrvAGQDVAtldadalaqlrrehFGFIFQRYhll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 403 ANLTSSKRVlnelwdEYPL---QPEKEIRTILGNFLFT----GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PRK10535 99 SHLTAAQNV------EVPAvyaGLERKQRLLRAQELLQrlglEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190
....*....|....*....|....*....|..
gi 446524801 476 NHLDLNSKE----ILENaLIDYPGTLLFVSHD 503
Cdd:PRK10535 173 GALDSHSGEevmaILHQ-LRDRGHTVIIVTHD 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-479 |
1.38e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGY-DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLL-------------------------KSIVNK---- 379
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgevlikgepikydkKSLLEVrktv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 380 ------------LPLLNGDVSFGS-NVSVGYYDQEQANLTSSKRVLNELWDEyplqpekeirtilgnflftgddvlKPVS 446
Cdd:PRK13639 81 givfqnpddqlfAPTVEEDVAFGPlNLGLSKEEVEKRVKEALKAVGMEGFEN------------------------KPPH 136
|
170 180 190
....*....|....*....|....*....|...
gi 446524801 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13639 137 HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
344-503 |
1.45e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 46.91 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 344 PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIvNKL--PLlNGDVSF-GSNV----------SVGYYDQE--------- 401
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLiePT-SGEIFIdGEDIreqdpvelrrKIGYVIQQiglfphmtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 QANLTSSKRVLNelWdeyplqPEKEIRTilgnflfTGDDVLKPV------------SSLSGGQKARLALAKLMMQKSNLL 469
Cdd:cd03295 93 EENIALVPKLLK--W------PKEKIRE-------RADELLALVgldpaefadrypHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524801 470 ILDEPTNHLDLNSKEILENALIDYP----GTLLFVSHD 503
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-221 |
1.51e-05 |
|
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: 48.21 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 16 ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTgletsltiwdeMLTVFTHLQ 95
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRP-----------YMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 96 QMETKLRRLEQemgKEENFSnEATYERLLadyDQLQLNY--KDQGGYQYEADIRSILSGlgfpvethqttistlsgGQKT 173
Cdd:TIGR00954 534 QIIYPDSSEDM---KRRGLS-DKDLEQIL---DNVQLTHilEREGGWSAVQDWMDVLSG-----------------GEKQ 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 174 RLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSH 221
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
332-518 |
1.54e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDEnpIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQANLtssKRV 411
Cdd:PRK10908 6 HVSKAYLGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL---RRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 LNELWDEYPLQPEkeiRTILGNFLF-------TGDDVLKPVSS-----------------LSGGQKARLALAKLMMQKSN 467
Cdd:PRK10908 81 IGMIFQDHHLLMD---RTVYDNVAIpliiagaSGDDIRRRVSAaldkvglldkaknfpiqLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524801 468 LLILDEPTNHLDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-60 |
1.76e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 1.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI 60
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
448-503 |
2.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 2.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE--NALIDYPGTLLFVSHD 503
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
300-519 |
2.13e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.51 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 300 LDRM-ELLTRPLgdsksasfhfDIEKQSGNDVLQVNDATI-------GYD-ENPIIEHVTMRLTRGDSVALVGPNGIGKS 370
Cdd:COG5265 329 MERMfDLLDQPP----------EVADAPDAPPLVVGGGEVrfenvsfGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 371 TLLK-----------SIvnklpLLNG----DVSFGS---------------NVSVGY---YDQEQANltsskrvlnelwd 417
Cdd:COG5265 399 TLARllfrfydvtsgRI-----LIDGqdirDVTQASlraaigivpqdtvlfNDTIAYniaYGRPDAS------------- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 418 eyplqpEKEIRTI-----LGNF---LFTGDDV------LKpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS- 482
Cdd:COG5265 461 ------EEEVEAAaraaqIHDFiesLPDGYDTrvgergLK----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTe 530
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446524801 483 KEILEnalidypgTLLFVSHDRyfinrvtTTVV---ELST 519
Cdd:COG5265 531 RAIQA--------ALREVARGR-------TTLViahRLST 555
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
349-492 |
2.16e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 349 VTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP--------LLNGDVSFGSNVSvgyyDQEQA-------------NLTS 407
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEELQASNIR----DTERAgiaiihqelalvkELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 SKRVL--NEL-------WDEYPLQPEKEIRTilgnfLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:PRK13549 100 LENIFlgNEItpggimdYDAMYLRAQKLLAQ-----LKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170
....*....|....
gi 446524801 479 DLNSKEILENALID 492
Cdd:PRK13549 175 TESETAVLLDIIRD 188
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-198 |
2.18e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 46.52 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYLAQNT----------- 75
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITISkenlkeirkkIGIIFQNPdnqfigatved 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 76 ----GLEtsltiwDEMLTvfthLQQMETKLRRLEQEMGKEENFSNEATYerlladydqlqlnykdqggyqyeadirsils 151
Cdd:PRK13632 104 diafGLE------NKKVP----PKKMKDIIDDLAKKVGMEDYLDKEPQN------------------------------- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524801 152 glgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13632 143 ---------------LSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
167-246 |
2.24e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHDryfldklVTQVYEISNKESRRF 244
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN-------LAQAARISDRAALFF 236
|
..
gi 446524801 245 VG 246
Cdd:PRK14271 237 DG 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
348-475 |
2.27e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 348 HVTMRLTRGDSVALVGPNGIGKSTLLK-----------SIvnklpLLNG-DVSFGS------------------------ 391
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKilyglyqpdsgEI-----LIDGkPVRIRSprdaialgigmvhqhfmlvpnltv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 392 --NVSVGYYDQEQA--NLTSSKRVLNELWDEYPLqpekEIrtilgnflftgdDVLKPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:COG3845 98 aeNIVLGLEPTKGGrlDRKAARARIRELSERYGL----DV------------DPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
....*...
gi 446524801 468 LLILDEPT 475
Cdd:COG3845 162 ILILDEPT 169
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
2.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.72 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigylaqntglet 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 80 sltIWDEMLTvfthlqqmETKLRRLEQEMG------KEENFSneATYERLLAdYDQLQLNYKDQggyQYEADIRSILSGL 153
Cdd:PRK13652 63 ---IRGEPIT--------KENIREVRKFVGlvfqnpDDQIFS--PTVEQDIA-FGPINLGLDEE---TVAHRVSSALHML 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 154 GFPvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP 213
Cdd:PRK13652 126 GLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-198 |
2.48e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELshdggeiiKPKdvsigylaqntglETSLTIWDEMLTVfthlQQME 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL--------QPT-------------SGTVTIGERVITA----GKKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 99 TKLRRLEQEMGKEENFSN----EATYERLLAdYDQLQLNYKDQggyQYEADIRSILSGLGFPVETHQTTISTLSGGQKTR 174
Cdd:PRK13634 78 KKLKPLRKKVGIVFQFPEhqlfEETVEKDIC-FGPMNFGVSEE---DAKQKAREMIELVGLPEELLARSPFELSGGQMRR 153
|
170 180
....*....|....*....|....
gi 446524801 175 LALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
448-552 |
3.12e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 47.10 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHDRYFINRVTTTVVELStEGAQ 523
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeavkASGISMVLTSHWPEVIEDLSDKAIWLE-NGEI 247
|
90 100 110
....*....|....*....|....*....|..
gi 446524801 524 EYLGDYDYYVEKKNE---MIERAELEQQESDV 552
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEgvsEVEKECEVEVGEPI 279
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
353-479 |
4.24e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 353 LTRGDSVALVGPNGIGKSTLLKsivnklpLLNGDV--SFGSnvsvgyYDQEqanlTSSKRVL-----NELWDEYPLQPEK 425
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------ILSGELipNLGD------YEEE----PSWDEVLkrfrgTELQNYFKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 426 EIRTIL--------------------------GNFlftgDDVLK----------PVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK13409 159 EIKVVHkpqyvdlipkvfkgkvrellkkvderGKL----DEVVErlglenildrDISELSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 446524801 470 ILDEPTNHLD 479
Cdd:PRK13409 235 FFDEPTSYLD 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
167-240 |
4.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 4.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-----QGYpgAILIVSHDRYFLDKLVTQVYEISNKE 240
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLydlnkEGI--TIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-227 |
4.39e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD--GGEiIKPKDVSIGYLaqnTGLET 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGD-ILFKGESILDL---EPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 80 SltiwdeMLTVFTHLQqmetklrrleqeMGKEENFSNEATYERLLADYDQLQLNYKDQGGYQYEADIRSILSGLGF-PVE 158
Cdd:CHL00131 82 A------HLGIFLAFQ------------YPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMdPSF 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 159 THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ---YLQGYPGAILIVSHDRYFLD 227
Cdd:CHL00131 144 LSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEginKLMTSENSIILITHYQRLLD 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-221 |
5.03e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 4 LQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKI------------IAGELSHDGGEIIKPK-DVS--- 67
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlipgarVEGEILLDGEDIYDPDvDVVelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 68 --IGYLAQ-----------NT--GL---------------ETSLT---IWDEmltVFTHLQQmetklrrleqemgkeenf 114
Cdd:COG1117 92 rrVGMVFQkpnpfpksiydNVayGLrlhgikskseldeivEESLRkaaLWDE---VKDRLKK------------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 115 sneatyerlladydqlqlnykdqggyqyeadirsilSGLGfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:COG1117 151 ------------------------------------SALG------------LSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
250 260 270
....*....|....*....|....*....|....*
gi 446524801 195 NHLD------IETLTW-L-EQYlqgypgAILIVSH 221
Cdd:COG1117 183 SALDpistakIEELILeLkKDY------TIVIVTH 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-222 |
5.23e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLY----GAETILANIKLEVQTKDRIALVGRNGAGKST-------LLK---IIAGELSHDGGEIIKPKDV 66
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAangRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 67 SIGYLAQNtglETSLTIWDEMLTVFTHL----QQMETKLrrLEQEMGKEENFsNEATyeRLLadyDQLQLNykdqggyqy 142
Cdd:PRK09473 90 ELNKLRAE---QISMIFQDPMTSLNPYMrvgeQLMEVLM--LHKGMSKAEAF-EESV--RML---DAVKMP--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 143 EADIRSILsglgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILI 218
Cdd:PRK09473 150 EARKRMKM----YPHE--------FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIM 217
|
....
gi 446524801 219 VSHD 222
Cdd:PRK09473 218 ITHD 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-529 |
5.46e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 148 SILSGLGFPVETHQTTISTLSGGQKTRLALGKLLltKPDLL----ILDEPTNHL---DIETLTWLEQYLQGYPGAILIVS 220
Cdd:PRK00635 458 SILIDLGLPYLTPERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 221 HDRYFLdKLVTQVYEIS------------NKESRRFVGNySKYLDLKSALYEQEMKRYEKQQDEIAKLedfvqkNIARAS 288
Cdd:PRK00635 536 HDEQMI-SLADRIIDIGpgagifggevlfNGSPREFLAK-SDSLTAKYLRQELTIPIPEKRTNSLGTL------TLSKAT 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 289 TTK-RAQSRRKQLDRMELLTRPLGDSKSASFhfdiekqsgNDVL---------QVNDATIGYDENPI--IEHVTMRLTrG 356
Cdd:PRK00635 608 KHNlKDLTISLPLGRLTVVTGVSGSGKSSLI---------NDTLvpaveefieQGFCSNLSIQWGAIsrLVHITRDLP-G 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 357 DSVALVGPNGIGKSTLLKSIVNKLP------LLNGDVSFgsNVSVGYYDQEQA---------------NLTSSKRVLNEL 415
Cdd:PRK00635 678 RSQRSIPLTYIKAFDDLRELFAEQPrskrlgLTKSHFSF--NTPLGACAECQGlgsitttdnrtsipcPSCLGKRFLPQV 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 416 WDeyPLQPEKEIRTILG-------NFLFT--------------GDDVL---KPVSSLSGGQKARLALAKLMM---QKSNL 468
Cdd:PRK00635 756 LE--VRYKGKNIADILEmtayeaeKFFLDepsihekihalcslGLDYLplgRPLSSLSGGEIQRLKLAYELLapsKKPTL 833
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 469 LILDEPTNHL---DLNSKEILENALIDYPGTLLFVSHDRYFInRVTTTVVELSTEGAQeyLGDY 529
Cdd:PRK00635 834 YVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELGPEGGN--LGGY 894
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-503 |
7.17e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 45.10 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNG-DVSFGSNVSVGYYDQEQ 402
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILApdsgevLWDGePLDPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 403 AnLTSSKRVLNELwdEYPLQ----PEKEIRTILgnflftgDDVL----------KPVSSLSGG--QKARLALAklMMQKS 466
Cdd:COG4152 81 G-LYPKMKVGEQL--VYLARlkglSKAEAKRRA-------DEWLerlglgdranKKVEELSKGnqQKVQLIAA--LLHDP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524801 467 NLLILDEPTNHLD-LNSkEILENALIDY--PG-TLLFVSHD 503
Cdd:COG4152 149 ELLILDEPFSGLDpVNV-ELLKDVIRELaaKGtTVIFSSHQ 188
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
165-198 |
9.07e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 9.07e-05
10 20 30
....*....|....*....|....*....|....
gi 446524801 165 STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
448-515 |
1.01e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 1.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-222 |
1.16e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 16 ETILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkDVSiGY--------LAQNTGL----ETSL 81
Cdd:COG4586 33 REVEAvdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV----RVL-GYvpfkrrkeFARRIGVvfgqRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 tIWDemLTVfthlqqMETklRRLEQEMGKEEnfsnEATYERLLADYDQLqLnykdqggyqyeaDIRSILsglgfpvethQ 161
Cdd:COG4586 108 -WWD--LPA------IDS--FRLLKAIYRIP----DAEYKKRLDELVEL-L------------DLGELL----------D 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 162 TTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVSHD 222
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeaiREFLKEYNRERGTTILLTSHD 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-198 |
1.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.31 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpkdvsigylaqnTGLETSLT--IWDEMLTVFTHLQQ 96
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV------------DGLDTSDEenLWDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 97 METKLRR--LEQEMG-KEENFSNEATYERLLADYdqlqlNYKDQGGYQYEADirsilsglgfpvETHqttisTLSGGQKT 173
Cdd:PRK13633 94 PDNQIVAtiVEEDVAfGPENLGIPPEEIRERVDE-----SLKKVGMYEYRRH------------APH-----LLSGGQKQ 151
|
170 180
....*....|....*....|....*
gi 446524801 174 RLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
314-495 |
1.22e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 314 KSASFHFDIEKqsgnDVlqvndatigydenPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI----------------- 376
Cdd:PTZ00265 386 KNVRFHYDTRK----DV-------------EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIerlydptegdiiindsh 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 377 ----------------VNKLPLLNGDvSFGSNVSVGYYD------------------QEQANLTSSKRV----------- 411
Cdd:PTZ00265 449 nlkdinlkwwrskigvVSQDPLLFSN-SIKNNIKYSLYSlkdlealsnyynedgndsQENKNKRNSCRAkcagdlndmsn 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 412 ------LNELWDEYPLQPEKEI-----RTILGNFLFTGDD-----VLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PTZ00265 528 ttdsneLIEMRKNYQTIKDSEVvdvskKVLIHDFVSALPDkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
|
250 260
....*....|....*....|
gi 446524801 476 NHLDLNSKEILENALIDYPG 495
Cdd:PTZ00265 608 SSLDNKSEYLVQKTINNLKG 627
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-194 |
1.33e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 5 QVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIA-------GELSHDGGEIIKPK---DVS--IGYLA 72
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarkiqqGRVEVLGGDMADARhrrAVCprIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QntGLETSL--TiwdemLTVFthlqqmetklrrleqemgkeEN---FSneatyeRLLAdydqlqlnykdQGGYQYEADIR 147
Cdd:NF033858 83 Q--GLGKNLypT-----LSVF--------------------ENldfFG------RLFG-----------QDAAERRRRID 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 148 SIL--SGLG-F---PVethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:NF033858 119 ELLraTGLApFadrPA-------GKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
443-503 |
1.42e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.83 E-value: 1.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 443 KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTnhLDLNSKEILE-NALID-----YPGTLLFVSHD 503
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA--AGLNPKETKElDELIAelrneHNVTVLLIEHD 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-200 |
1.54e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.07 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 2 ILLQVNALSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLkiiagelSHDGGeIIKPK--DVSIG--YLA 72
Cdd:PRK13631 20 IILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLV-------THFNG-LIKSKygTIQVGdiYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 73 QNTGLETSltiwdemltVFTHLQQMETKLRRLEQEMGkeenfsneatyerLLADYDQLQLnYKDQ------------GGY 140
Cdd:PRK13631 92 DKKNNHEL---------ITNPYSKKIKNFKELRRRVS-------------MVFQFPEYQL-FKDTiekdimfgpvalGVK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 141 QYEADIRS--ILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK13631 149 KSEAKKLAkfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
328-486 |
1.66e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.97 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGY--DENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgSNVSVgyydqEQANL 405
Cdd:PRK13648 5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY-NNQAI-----TDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 406 TSSKRVLNELWDeyplQPEKE-IRTI--------LGNFLFTGDDVLKPVS-----------------SLSGGQKARLALA 459
Cdd:PRK13648 79 EKLRKHIGIVFQ----NPDNQfVGSIvkydvafgLENHAVPYDEMHRRVSealkqvdmleradyepnALSGGQKQRVAIA 154
|
170 180
....*....|....*....|....*..
gi 446524801 460 KLMMQKSNLLILDEPTNHLDLNSKEIL 486
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNL 181
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
328-503 |
1.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.93 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDENPIIEH---VTMRLTRGDSVALVGPNGIGKSTLLKSI------VNKLPLLNGDVSFGSNV----- 393
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIdglfeeFEGKVKIDGELLTAENVwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 394 SVGYYDQEQANLTSSKRVLNEL---WDEYPLQPEKEIRTILGNFLFTG--DDVLKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVafgMENQGIPREEMIKRVDEALLAVNmlDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524801 469 LILDEPTNHLDLNSK----EILENALIDYPGTLLFVSHD 503
Cdd:PRK13642 162 IILDESTSMLDPTGRqeimRVIHEIKEKYQLTVLSITHD 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-222 |
1.70e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.95 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvsigylaqntgLETSLTIWDemltvfthlqqm 97
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-----------LLTEENVWD------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 98 etKLRRLEQEMGKEENFSNEATYErlladyDQLQLNYKDQGGYQYEADIR--SILSGLGFpVETHQTTISTLSGGQKTRL 175
Cdd:PRK13650 79 --IRHKIGMVFQNPDNQFVGATVE------DDVAFGLENKGIPHEEMKERvnEALELVGM-QDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524801 176 ALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQG----YPGAILIVSHD 222
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-510 |
1.77e-04 |
|
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: 43.89 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 330 VLQVNDATIGYDEN----PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP---LLNGDVSF------------- 389
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFdgedllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 390 ----GSNVS---------------VGyyDQ------------------------EQANLTSSKRVLnelwDEYPLQpeke 426
Cdd:COG0444 81 rkirGREIQmifqdpmtslnpvmtVG--DQiaeplrihgglskaeareraiellERVGLPDPERRL----DRYPHE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 427 irtilgnflftgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILEnaLI-----DYPGTLLFV 500
Cdd:COG0444 151 ---------------------LSGGMRQRVMIARALALEPKLLIADEPTTALDVtIQAQILN--LLkdlqrELGLAILFI 207
|
250
....*....|....
gi 446524801 501 SHD----RYFINRV 510
Cdd:COG0444 208 THDlgvvAEIADRV 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
507-640 |
1.81e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 507 INRVTTTVVELSTEgAQEYLGDYDYYVEKKNEMIERAELEQQE--------SDVPVQKVVAQEKLNYLEeKERKQLERQr 578
Cdd:TIGR02168 248 LKEAEEELEELTAE-LQELEEKLEELRLEVSELEEEIEELQKElyalaneiSRLEQQKQILRERLANLE-RQLEELEAQ- 324
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 579 trkIEELEQSIVELEEEIATLEDQlcLPEIYADYEKASEITTKKQTLQEQLETCMAEWEELH 640
Cdd:TIGR02168 325 ---LEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
2.26e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.57 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLL--------------KIIAGELSHDGGEIIKPKdvsIGYLAQNTGLET-SLTI 83
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvKVMGREVNAENEKWVRSK---VGLVFQDPDDQVfSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 WDEMltvfthlqqmetKLRRLEQEMGKEENFSNEATYERLLADYDqlqlnYKDQGGYQyeadirsilsglgfpvethqtt 163
Cdd:PRK13647 98 WDDV------------AFGPVNMGLDKDEVERRVEEALKAVRMWD-----FRDKPPYH---------------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 164 istLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD---IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13647 139 ---LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
363-502 |
2.29e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 363 GPNGIGKSTLLKSIVNKLPLLNGDVSFGS----NVSVGY--YDQEQANLTSSKRVLNEL--WDEYPLQPEKEIRTIlgnF 434
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNcninNIAKPYctYIGHNLGLKLEMTVFENLkfWSEIYNSAETLYAAI---H 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 435 LFTGDDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI---DYPGTLLFVSH 502
Cdd:PRK13541 110 YFKLHDLLdEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmkaNSGGIVLLSSH 181
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-503 |
2.50e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.88 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQANLTSskRVLNELWDEYPLQPE 424
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRN--QKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 425 keiRTILGNF---LFTGD-----------DVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK11629 102 ---FTALENVampLLIGKkkpaeinsralEMLAAVglehranhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180
....*....|....*....|....*..
gi 446524801 481 -NSKEILE--NALIDYPGT-LLFVSHD 503
Cdd:PRK11629 179 rNADSIFQllGELNRLQGTaFLVVTHD 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-201 |
2.55e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.53 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MIllQVNALSKLY----GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGylaqntG 76
Cdd:COG1135 1 MI--ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL------VD------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 LE-TSLTiwdemltvfthlqqmETKLRRLEQEMG----------------------KEENFSNEATYER---LLAdydql 130
Cdd:COG1135 67 VDlTALS---------------ERELRAARRKIGmifqhfnllssrtvaenvalplEIAGVPKAEIRKRvaeLLE----- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524801 131 qlnykdqggyqyeadirsiLSGLG-----FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG1135 127 -------------------LVGLSdkadaYP--------SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
166-207 |
2.84e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446524801 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ 207
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-198 |
3.00e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKdvSIGYLAQNTGLETSlTIWDEMLtvfthlqqm 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAWIMNA-TVRGNIL--------- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 98 etklrrleqemgkeenFSNEATYERLladYDQLQLNykdqggyQYEADIRSILSGLgfpvethQTTIS----TLSGGQKT 173
Cdd:PTZ00243 743 ----------------FFDEEDAARL---ADAVRVS-------QLEADLAQLGGGL-------ETEIGekgvNLSGGQKA 789
|
170 180
....*....|....*....|....*
gi 446524801 174 RLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PTZ00243 790 RVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-222 |
3.03e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.94 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLY--GAETI--LANIKLEVQTKDRIALVGRNGAGKSTLLKIIagelshdgGEIIKPKDVSIGYLAQNTGle 78
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPTSGTYRVAGQDVA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 79 tslTIWDEMLTvfthlqqmetKLRRleqemgkeENFSNEATYERLLADYDQLQlN------YKDQGGYQYEADIRSILSG 152
Cdd:PRK10535 74 ---TLDADALA----------QLRR--------EHFGFIFQRYHLLSHLTAAQ-NvevpavYAGLERKQRLLRAQELLQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 153 LGFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQyLQGYPGAILIVSHD 222
Cdd:PRK10535 132 LGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
167-199 |
3.10e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 3.10e-04
10 20 30
....*....|....*....|....*....|...
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
340-487 |
3.34e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.08 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 340 YDENPIIEhvtmrltRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQEQANlTSSKRV-------L 412
Cdd:PRK13634 24 YDVNVSIP-------SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLK-PLRKKVgivfqfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 413 NELWDEyplQPEKEIRTILGNFLFTGDDVLKPVS------------------SLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:PRK13634 96 HQLFEE---TVEKDICFGPMNFGVSEEDAKQKARemielvglpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170
....*....|....
gi 446524801 475 TNHLD-LNSKEILE 487
Cdd:PRK13634 173 TAGLDpKGRKEMME 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-198 |
3.35e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.82 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 33 ALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS-----IGYLAQNT---------------GLETSLTIWDE 86
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEklrkhIGIVFQNPdnqfvgsivkydvafGLENHAVPYDE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 87 MltvfthlqqmetklRRLEQEMGKEENFSNEATYERlladydqlqlnykdqggyqyeadirsilsglgfpvethqttiST 166
Cdd:PRK13648 119 M--------------HRRVSEALKQVDMLERADYEP------------------------------------------NA 142
|
170 180 190
....*....|....*....|....*....|..
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
442-503 |
3.46e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 3.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 442 LKPVSSLSGGQKARLALAKLMMqksnlLILDepTNHLDLNSKEILENALIDypgtLLFVSHD 503
Cdd:COG0419 153 LDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-223 |
3.84e-04 |
|
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: 43.66 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 13 YGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVSIGYLAQNTGL---ETSL 81
Cdd:COG5265 367 YDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGRILIDGQDI---RDVTQASLRAAIGIvpqDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 82 ---TIwdemltvfthlqqmetklrrleqemgkeenFSNEAtYERLLADYDQL----QLnykdqggyqyeADIRSILSGLg 154
Cdd:COG5265 444 fndTI------------------------------AYNIA-YGRPDASEEEVeaaaRA-----------AQIHDFIESL- 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 155 fPvETHQTTIS----TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQgypGAILIVSHDR 223
Cdd:COG5265 481 -P-DGYDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT----ERAIQ---AALREVARGR 544
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-199 |
4.00e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.85 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 3 LLQVNALSKLYGAETIL---------ANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIG--- 69
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELlIDDHPLHFGdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 70 YLAQNTGLetsltIWDEMLTVFTHLQQMETKLR---RLEQEMgkeenfSNEATYERLLADYDQLQLnYKDQGGYqyeadi 146
Cdd:PRK15112 84 YRSQRIRM-----IFQDPSTSLNPRQRISQILDfplRLNTDL------EPEQREKQIIETLRQVGL-LPDHASY------ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524801 147 rsilsglgFPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK15112 146 --------YP--------HMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
167-201 |
4.16e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.47 E-value: 4.16e-04
10 20 30
....*....|....*....|....*....|....*
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
353-503 |
4.32e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 353 LTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFgSNVSVGYydqeqanltsskrvlnelwdeyplQPEKeirtilg 432
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY------------------------KPQY------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 433 nflftgddvlkpvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPGTLLFVSHD 503
Cdd:cd03222 70 -------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-107 |
4.46e-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: 41.20 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 28 TKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpkdVSIGYLAQNTGLETSLTIWDEMLTVFTHLQQMETKLRRLEQE 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-198 |
4.51e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.42 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpKDVSIGYLAQNTGLETsltIWDEMLTVFthlQQME 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV-DDTLITSTSKNKDIKQ---IRKKVGLVF---QFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 99 TKLrrLEQEMGKEENFSNEatyerlladydqlqlNYkdqGGYQYEAD--IRSILSGLGFPVETHQTTISTLSGGQKTRLA 176
Cdd:PRK13649 96 SQL--FEETVLKDVAFGPQ---------------NF---GVSQEEAEalAREKLALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180
....*....|....*....|..
gi 446524801 177 LGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLD 177
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-199 |
4.66e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 32 IALVGRNGAGKSTL---LKII----AGELSHDGGEIIKPKDVsigylaqntgletsltiwdemltvfthlqqmETKLRRL 104
Cdd:PRK11308 44 LAVVGESGCGKSTLarlLTMIetptGGELYYQGQDLLKADPE-------------------------------AQKLLRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 105 EQEMgkeeNFSN-------EATYERLLADydQLQLNyKDQGGYQYEADIRSILSGLGFPVETHQTTISTLSGGQKTRLAL 177
Cdd:PRK11308 93 KIQI----VFQNpygslnpRKKVGQILEE--PLLIN-TSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAI 165
|
170 180
....*....|....*....|..
gi 446524801 178 GKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDV 187
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
166-222 |
5.09e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 5.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD-IETL-------TWLEQYlqgypgAILIVSHD 222
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLrieelmhELKEQY------TIIIVTHN 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
345-503 |
5.51e-04 |
|
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: 42.04 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 345 IIEHVTMRLTRGDSVALVGPNGIGKSTLLKsivnklpLL-------NGDVS-FGSNVS--------------VGYYDQ-E 401
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLG-------LLagldrptSGTVRlAGQDLFaldedararlrarhVGFVFQsF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 402 Q--ANLTSS-----------------------KRV-LNELWDEYPLQpekeirtilgnflftgddvlkpvssLSGGQKAR 455
Cdd:COG4181 100 QllPTLTALenvmlplelagrrdarararallERVgLGHRLDHYPAQ-------------------------LSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524801 456 LALAKLMMQKSNLLILDEPTNHLDL-NSKEILE-----NAliDYPGTLLFVSHD 503
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAaTGEQIIDllfelNR--ERGTTLVLVTHD 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
165-227 |
6.48e-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: 41.15 E-value: 6.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 165 STLSGGQKTRLALGKLLL--TKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRYFLD 227
Cdd:cd03238 86 STLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLS 153
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
329-503 |
6.76e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.03 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 329 DVLQVNDATIGYD---ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLP------LLNGDVSFGSNV-----S 394
Cdd:PRK13650 3 NIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEaesgqiIIDGDLLTEENVwdirhK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 395 VGYYDQEQAN----LTSSKRVLNELWDE-YPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK13650 83 IGMVFQNPDNqfvgATVEDDVAFGLENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524801 470 ILDEPTNHLD----LNSKEILENALIDYPGTLLFVSHD 503
Cdd:PRK13650 163 ILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-201 |
6.91e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.10 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQvnALSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpkdvsig 69
Cdd:PRK11153 1 MIELK--NISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVLVDGQDL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 70 ylaqntgleTSLTiwdemltvfthlqqmETKLRRLEQEMG---KEEN-------FSNEAtyerlLAdydqLQLNYKDqgg 139
Cdd:PRK11153 70 ---------TALS---------------EKELRKARRQIGmifQHFNllssrtvFDNVA-----LP----LELAGTP--- 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524801 140 yqyEADIRSI------LSGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:PRK11153 114 ---KAEIKARvtelleLVGLS---DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
446-502 |
6.94e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.17 E-value: 6.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 446 SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL------IDYPgtLLFVSH 502
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLerlareINIP--ILYVSH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
355-535 |
7.22e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.10 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 355 RGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSvgyydqeQANLTSSKRVLNELW---DEYPLQPEKEIRTI 430
Cdd:PRK13652 29 RNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPIT-------KENIREVRKFVGLVFqnpDDQIFSPTVEQDIA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 431 LG--NFLFTGDDVLKPVSS-----------------LSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE--N 488
Cdd:PRK13652 102 FGpiNLGLDEETVAHRVSSalhmlgleelrdrvphhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpQGVKELIDflN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524801 489 ALID-YPGTLLFVSHDryfinrvtttvVELSTEgaqeyLGDYDYYVEK 535
Cdd:PRK13652 182 DLPEtYGMTVIFSTHQ-----------LDLVPE-----MADYIYVMDK 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-222 |
8.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 8.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 164 ISTLSGGQKT------RLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAIlIVSHD 222
Cdd:PRK03918 786 LTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERrrklVDIMERYLRKIPQVI-IVSHD 853
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
332-549 |
8.35e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 332 QVNDATIGYDENPI---IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSVGYYDQE-QANLTS 407
Cdd:PRK13546 23 RMKDALIPKHKNKTffaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGlSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 408 SKRV-LNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEIL 486
Cdd:PRK13546 103 IENIeFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 487 ENALIDYP---GTLLFVSHDRYFINRVTTTVVELSTEGAQEYlGDYD----YYVEKKNEMIERAELEQQE 549
Cdd:PRK13546 183 LDKIYEFKeqnKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDdvlpKYEAFLNDFKKKSKAEQKE 251
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-479 |
1.06e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 355 RGDSVALVGPNGIGKSTLLKsivnklpLLNGDV--SFGSnvsvgyYDQEqanlTSSKRVLN-----ELWDEYPLQPEKEI 427
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALK-------ILSGELkpNLGD------YDEE----PSWDEVLKrfrgtELQDYFKKLANGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 428 RTILGN-------FLFTG---------------DDVL----------KPVSSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:COG1245 161 KVAHKPqyvdlipKVFKGtvrellekvdergklDELAeklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 446524801 476 NHLD 479
Cdd:COG1245 241 SYLD 244
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
327-484 |
1.12e-03 |
|
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: 40.49 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 327 GNDVLQVNDATIGydenPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsnvsvgyyDQEQANLT 406
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD--------GKPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 407 SSKRVLNELwdeyPLQPE---KE----IRTILGNFLFTgddvlkpvSSLSGG--QKArlALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03215 69 PRDAIRAGI----AYVPEdrkREglvlDLSVAENIALS--------SLLSGGnqQKV--VLARWLARDPRVLILDEPTRG 134
|
....*..
gi 446524801 478 LDLNSKE 484
Cdd:cd03215 135 VDVGAKA 141
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-61 |
1.14e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII 61
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIL 56
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
342-503 |
1.15e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.30 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 342 ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGsNVSVGYYDQEQANLTSSKRV-------LNE 414
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRPVRKRIgmvfqfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 415 LWDEyplQPEKEIR------------------TILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:PRK13646 98 LFED---TVEREIIfgpknfkmnldevknyahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190
....*....|....*....|....*....|.
gi 446524801 477 HLDLNSK----EILENALIDYPGTLLFVSHD 503
Cdd:PRK13646 175 GLDPQSKrqvmRLLKSLQTDENKTIILVSHD 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
164-328 |
1.20e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 164 ISTLSGGQKTRLALGKLLLT---KPDLLILDEPTNHL---DIETLTWLEQYL--QGYpgAILIVSHDRYFLdKLVTQVYE 235
Cdd:PRK00635 807 LSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLthQGH--TVVIIEHNMHVV-KVADYVLE 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 236 ISNKEsrrfvGNYSKYLdLKSALYEQ----------EMKRYEKQQDEIAKLEDFVQK-NIARASTTKRA-QSRRKQLD-- 301
Cdd:PRK00635 884 LGPEG-----GNLGGYL-LASCSPEElihlhtptakALRPYLSSPQELPYLPDPSPKpPVPADITIKNAyQHNLKHIDls 957
|
170 180 190
....*....|....*....|....*....|
gi 446524801 302 -RMELLTRPLGDSKSA--SFHFDIEKQSGN 328
Cdd:PRK00635 958 lPRNALTAVTGPSASGkhSLVFDILYAAGN 987
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
132-199 |
1.44e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.58 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 132 LNYKDQGGYQYEADIRSILSG----LGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK15439 365 LTHNRRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-198 |
1.69e-03 |
|
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: 40.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIKPKDV--------SIGYLAQNTGLetslti 83
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKVLIDGQDIAAMSRKelrelrrkKISMVFQSFAL------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 84 wdemltvFTHLQQMETKLRRLE-QEMGKEEnfsneatyeRLLADYDQLQL----NYKDQggyqyeadirsilsglgFPVE 158
Cdd:cd03294 114 -------LPHRTVLENVAFGLEvQGVPRAE---------REERAAEALELvgleGWEHK-----------------YPDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524801 159 thqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03294 161 --------LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-222 |
1.82e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 1 MILLQVNALSKLYGAETI----LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHdggeiikPKDVSIGYLAQNTg 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-------PGRVMAEKLEFNG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 77 letsltiwdemltvfTHLQQMETKLRRleQEMGKEENFSNEATYERLLADYD---QLQLNYK-DQGGYQYEADIRSI--L 150
Cdd:PRK11022 73 ---------------QDLQRISEKERR--NLVGAEVAMIFQDPMTSLNPCYTvgfQIMEAIKvHQGGNKKTRRQRAIdlL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 151 SGLGFP-------VETHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD-------IETLTWLEQYLQgypGAI 216
Cdd:PRK11022 136 NQVGIPdpasrldVYPHQ-----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQKEN---MAL 207
|
....*.
gi 446524801 217 LIVSHD 222
Cdd:PRK11022 208 VLITHD 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
331-480 |
1.90e-03 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 40.44 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLPLLNGDVSF-GSNVS-----------VG 396
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLdGEDILelspderaragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 397 Y---YDQEQANLTSS---KRVLNELWDE--YPLQPEKEIRTILGNFLFTGDDVLKPV-SSLSGGQKARLALAKLMMQKSN 467
Cdd:COG0396 81 LafqYPVEIPGVSVSnflRTALNARRGEelSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPK 160
|
170
....*....|...
gi 446524801 468 LLILDEPTNHLDL 480
Cdd:COG0396 161 LAILDETDSGLDI 173
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
448-479 |
2.05e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.60 E-value: 2.05e-03
10 20 30
....*....|....*....|....*....|..
gi 446524801 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-51 |
2.18e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 2.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446524801 3 LLQVNALSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG 51
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
346-492 |
2.96e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.16 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKSI------------VNKLPLLNGDVSFGSNVSVGYYDQEQANLTSSKRVLN 413
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLagmieptsgellIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 414 ELwdEYPL---------QPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKE 484
Cdd:PRK15112 109 IL--DFPLrlntdlepeQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
....*...
gi 446524801 485 ILENALID 492
Cdd:PRK15112 187 QLINLMLE 194
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
346-441 |
3.04e-03 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 39.67 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDS---VALVGPNGIGKSTLLKSIVNKLPLLNGDVSFGSNVSV-GYYDQEQANLTSSKRVL--NELWDEY 419
Cdd:pfam00931 5 VEKVIGKLSEKDEpgiVGIHGMGGVGKTTLAAQIFNDFDEVEGHFDSVAWVVVsKTFTISTLQQTILQNLGlsEDDWDNK 84
|
90 100
....*....|....*....|....*
gi 446524801 420 P-LQPEKEIRTIL--GNFLFTGDDV 441
Cdd:pfam00931 85 EeGELARKIRRALltKRFLLVLDDV 109
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-485 |
3.05e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 3.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446524801 440 DVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI 485
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKyEI 443
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
444-521 |
3.09e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 444 PVSSLSGGQKARLALAKLMMQKSN---LLILDEPTN--HLDlNSKEILE--NALIDYPGTLLFVSHDRYFInRVTTTVVE 516
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTglHFD-DIKKLLEvlQRLVDKGNTVVVIEHNLDVI-KTADYIID 903
|
....*
gi 446524801 517 LSTEG 521
Cdd:TIGR00630 904 LGPEG 908
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
167-231 |
3.25e-03 |
|
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: 38.51 E-value: 3.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET---------LTWLEQYLQGYPGAILIVSHDRYFLDKLVT 231
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
426-638 |
4.19e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.43 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 426 EIRTILGNFLFTGDDVL-------KPVSSLSggqkarLALAKLMMQKSNLL----ILDEPTNHLDLNSKEILENALIDYP 494
Cdd:pfam05911 577 ELSEVLQQFSATCNDVLsgkadleDFVLELS------HILDWISNHCFSLLdvssMEDEIKKHDCIDKVTLSENKVAQVD 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 495 GTLLFVSHDryfinrvtTTVVELSTEGAqeyLGDYDYYVEKKNEMIERAELEQQESdvpvQKVVAQEKLnyleEKERKQL 574
Cdd:pfam05911 651 NGCSEIDNL--------SSDPEIPSDGP---LVSGSNDLKTEENKRLKEEFEQLKS----EKENLEVEL----ASCTENL 711
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524801 575 ERQRTrKIEELEQSIVELEEEIATL-------EDQL-CLPEIYADYE-KASEITTKKQTLQEQLETCMAEWEE 638
Cdd:pfam05911 712 ESTKS-QLQESEQLIAELRSELASLkesnslaETQLkCMAESYEDLEtRLTELEAELNELRQKFEALEVELEE 783
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
346-624 |
5.12e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 346 IEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF-GSNVSVGYYDQEQANLTSSKRV-LNELWDEYPLQP 423
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNGQLTGIENIeLKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 424 EKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN-SKEILE--NALIDYPGTLLFV 500
Cdd:PRK13545 120 IKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTfTKKCLDkmNEFKEQGKTIFFI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 501 SHDRYFINRVTTTVVELSTEGAQEYlGD-------YDYYVEKKNEM-IERAELEQQESDVPVQKVVAQEKLNYLEEKER- 571
Cdd:PRK13545 200 SHSLSQVKSFCTKALWLHYGQVKEY-GDikevvdhYDEFLKKYNQMsVEERKDFREEQISQFQHGLLQEDQTGRERKRKk 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446524801 572 --KQLERQRTRKIEELEQSIVELEEEIATLEDQLCLPEIYADYEKASEITTKKQT 624
Cdd:PRK13545 279 gkKTSRKFKKKRVLITGVCIALLTGIISTGYYYKNLLPFNSENKYAEKVASKENV 333
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
536-640 |
5.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 536 KNEMIERAELEQQESDVpvqKVVAQEKLNYLEEKERKQlerQRTRKIEELEQSIVELEEEIATLEDQLCLPEIYADYEKA 615
Cdd:COG4717 64 RKPELNLKELKELEEEL---KEAEEKEEEYAELQEELE---ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL 137
|
90 100
....*....|....*....|....*
gi 446524801 616 SEITTKKQTLQEQLETCMAEWEELH 640
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELE 162
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
167-222 |
5.90e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.92 E-value: 5.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
434-508 |
6.07e-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: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 434 FLFTGDDVLKPVSSLSGGQKARLALAKLMM---QKSNLLILDEPTNHLD-LNSKEILE--NALIDYPGTLLFVSHDRYFI 507
Cdd:pfam13304 223 LLENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHpKLLRRLLEllKELSRNGAQLILTTHSPLLL 302
|
.
gi 446524801 508 N 508
Cdd:pfam13304 303 D 303
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
34-50 |
6.41e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.59 E-value: 6.41e-03
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
340-376 |
6.41e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.06 E-value: 6.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446524801 340 YD-ENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSI 376
Cdd:PRK11650 13 YDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV 50
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-87 |
6.86e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 6.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 36 GRNGAGKSTLLKIIAGELSHDGGEIIKpKDVSI--------GYLAQNTGLETSLTIWDEM 87
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-KNCNInniakpycTYIGHNLGLKLEMTVFENL 91
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
582-638 |
7.04e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 7.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524801 582 IEELEQSIVELEEEIATLEDQlclpEIYADYEKASEITTKKQTLQEQLETCMAEWEE 638
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKE----QDEASFERLAELRDELAELEEELEALKARWEA 465
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
331-389 |
8.77e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 38.37 E-value: 8.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524801 331 LQVNDATIGYDENPIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSF 389
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
328-503 |
9.14e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.07 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 328 NDVLQVNDATIGYDEN----PIIEHVTMRLTRGDSVALVGPNGIGKSTLLKSIVNKLPLLNGDVSFG-------SNVSVG 396
Cdd:PRK10261 10 RDVLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524801 397 YYDQEQANL----------------TS-------------SKRVLNELWDEYPLQPEK---------EIRTILGNFlftg 438
Cdd:PRK10261 90 LSEQSAAQMrhvrgadmamifqepmTSlnpvftvgeqiaeSIRLHQGASREEAMVEAKrmldqvripEAQTILSRY---- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 439 ddvlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN-SKEILEnaLI-----DYPGTLLFVSHD 503
Cdd:PRK10261 166 ------PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiQAQILQ--LIkvlqkEMSMGVIFITHD 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
445-504 |
9.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 9.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524801 445 VSSLSGGQKA------RLALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPG--TLLFVSHDR 504
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrrTNLKDIIEYSLKDSSDipQVIMISHHR 870
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
164-221 |
9.72e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 9.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524801 164 ISTLSGGQKT------RLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ-------GYPGAILIVSH 221
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEyslkdssDIPQVIMISHH 869
|
|
| |
