|
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: 729.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 6 VNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 86 EMLTVFTHLQQMETKLRRLEQEMgkeenfsnaATYEKLLADYDQLQLDYKDQGGYQYEADIRSILSGLGFPVETHQTTIS 165
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKL---------AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFV 245
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 246 GNYSKYLDLKSALYEQEIKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELLTRPLgDSKSASFHFDIEKQ 325
Cdd:COG0488 232 GNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPR-RDKTVEIRFPPPER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 326 SGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANL 405
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 TSSKRVLNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEI 485
Cdd:COG0488 391 DPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446524828 486 LENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEK 535
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-536 |
6.67e-121 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 369.61 E-value: 6.67e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWDemlTVFT 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLD---TVIM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 93 -HLQQMETKLRR----LEQEMgKEENFSNAATYEKLLADYDqlqldykdqgGYQYEADIRSILSGLGFPVETHQTTISTL 167
Cdd:PRK15064 88 gHTELWEVKQERdriyALPEM-SEEDGMKVADLEVKFAEMD----------GYTAEARAGELLLGVGIPEEQHYGLMSEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGN 247
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 248 YSKYLDLKSALYEQEIKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELltrplGDSKSAS-----FHFDI 322
Cdd:PRK15064 237 YDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKL-----EEVKPSSrqnpfIRFEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 323 EKQSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQ 402
Cdd:PRK15064 312 DKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 ANLTSSKRVLNELWDEY--PLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK15064 392 AYDFENDLTLFDWMSQWrqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 481 NSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEKK 536
Cdd:PRK15064 472 ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-642 |
4.91e-114 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 355.03 E-value: 4.91e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWD----------EMLTVFTHLqqmetkLRRLEQEMGkeenfsnaatyEKLLADYDQLQLDYKDQGGYQYEADIRSIL 150
Cdd:PRK11147 81 GTVYDfvaegieeqaEYLKRYHDI------SHLVETDPS-----------EKNLNELAKLQEQLDHHNLWQLENRINEVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 SGLGFPVEThqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLV 230
Cdd:PRK11147 144 AQLGLDPDA---ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 231 TQVYEISNKESRRFVGNYSKYLDLKsalyeQEIKRYEKQQDE-----IAKLEDFVQKNIaRASTTK-----RA-----QS 295
Cdd:PRK11147 221 TRIVDLDRGKLVSYPGNYDQYLLEK-----EEALRVEELQNAefdrkLAQEEVWIRQGI-KARRTRnegrvRAlkalrRE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 296 RRKQLDRMelltrplgdsKSASFHFDIEKQSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKS 375
Cdd:PRK11147 295 RSERREVM----------GTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 376 IVNKLQLLHGDVAFGSNVSVGYYDQEQANLTSSKRVLNELWDEyplqpEKEI------RTILG---NFLFTGDDVLKPVS 446
Cdd:PRK11147 365 MLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEG-----KQEVmvngrpRHVLGylqDFLFHPKRAMTPVK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFI-NRVTTTVVELSTEGAQEY 525
Cdd:PRK11147 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 526 LGDY-DYYVEKKNEMIERAAfeQQEQQENQAPVQKTVAQEKLNYLEEKERKQLErQRTRKIEELEQNIVSLEEEIATled 604
Cdd:PRK11147 520 VGGYhDARQQQAQYLALKQP--AVKKKEEAAAPKAETVKRSSKKLSYKLQRELE-QLPQLLEDLEAEIEALQAQVAD--- 593
|
650 660 670
....*....|....*....|....*....|....*....
gi 446524828 605 qlclPEIYA-DYEKASEITTKKQTLQEQLEACMAEWEEL 642
Cdd:PRK11147 594 ----ADFFSqPHEQTQKVLADLADAEQELEVAFERWEEL 628
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-536 |
2.30e-110 |
|
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: 343.07 E-value: 2.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWDemlTVFTHLQQMETKLRRLEQEMGK--EENfsnaATYEKLLADYDQLQLDYKDQGGYQYEADIRSILSGLGFPVE 158
Cdd:TIGR03719 83 KTVRE---NVEEGVAEIKDALDRFNEISAKyaEPD----ADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 159 thQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:TIGR03719 156 --DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 239 KESRRFVGNYSKYLDLKSALYEQEIKRYEKQQDEIAKLEDFVQKNI-ARASTTKRAQSRRKQLDRMELLTRPlgdsKSAS 317
Cdd:TIGR03719 234 GRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPkGRQAKSKARLARYEELLSQEFQKRN----ETAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 318 FHFDIEKQSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGY 397
Cdd:TIGR03719 310 IYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 398 YDQEQANLTSSKRVLNELWD--EYPLQPEKEI--RTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:TIGR03719 390 VDQSRDALDPNKTVWEEISGglDIIKLGKREIpsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 474 PTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVveLSTEGAQE---YLGDYDYYVEKK 536
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFEGDSHvewFEGNFSEYEEDK 533
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-641 |
1.09e-105 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 333.68 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNT-GLETSltiwdemltVFT 92
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpALPQP---------ALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 93 HLQQMETKLRRLEQEM--GKEENFSNA-ATYEKLLadyDQLQldykdqgGYQYEADIRSILSGLGFPVETHQTTISTLSG 169
Cdd:PRK10636 83 YVIDGDREYRQLEAQLhdANERNDGHAiATIHGKL---DAID-------AWTIRSRAASLLHGLGFSNEQLERPVSDFSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 170 GQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGNYS 249
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 250 KYLDLKSALYEQEIKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELLTRPLGDSksaSFHFDIEKQSG-- 327
Cdd:PRK10636 233 SFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDN---PFHFSFRAPESlp 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQAN-LT 406
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 407 SSKRVLNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEIL 486
Cdd:PRK10636 390 ADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 487 ENALIDYPGTLLFVSHDRYFInRVTTTVVELSTEGAQE-YLGDYDYYvekkNEMIERAAFEQQEQQENQAPVQKTVAQEK 565
Cdd:PRK10636 470 TEALIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEpFDGDLEDY----QQWLSDVQKQENQTDEAPKENNANSAQAR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 566 lnylEEKERKQLE-RQRT----RKIEELEQNIVSLEEEIATLEDQLCLPEIYADYEKA--SEITTKKQTLQEQLEACMAE 638
Cdd:PRK10636 545 ----KDQKRREAElRTQTqplrKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAelTACLQQQASAKSGLEECEMA 620
|
...
gi 446524828 639 WEE 641
Cdd:PRK10636 621 WLE 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-512 |
3.41e-102 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 321.68 E-value: 3.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 7 NGLSKLYGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWD 85
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 86 EmltVFTHLQQMETKLRRLEQEMgkeENFSNA-ATYEKLLADYDQLQ--LDYKDqgGYQYEADIRSILSGLGFPVEthQT 162
Cdd:PRK11819 90 N---VEEGVAEVKAALDRFNEIY---AAYAEPdADFDALAAEQGELQeiIDAAD--AWDLDSQLEIAMDALRCPPW--DA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESR 242
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 243 RFVGNYSKYLDLKSALYEQEIKRYEKQQDEIAKLEDFVQKNiARASTTK-----------RAQSRRKQLDRMELLTrPLG 311
Cdd:PRK11819 240 PWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQS-PKARQAKskarlaryeelLSEEYQKRNETNEIFI-PPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 312 DsksasfhfdiekQSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGS 391
Cdd:PRK11819 318 P------------RLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 392 NVSVGYYDQEQANLTSSKRVLNELWD--EYPLQPEKEI--RTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:PRK11819 386 TVKLAYVDQSRDALDPNKTVWEEISGglDIIKVGNREIpsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGN 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446524828 468 LLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTT 512
Cdd:PRK11819 466 VLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIAT 510
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-508 |
1.38e-75 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 255.94 E-value: 1.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 31 RIALVGRNGAGKSTLLKIIAGElSHDGgeiiKPKDVSIGYLAQN------TGLETSLTIWDEMltvfTHLQQMETKLRRL 104
Cdd:PLN03073 205 HYGLVGRNGTGKTTFLRYMAMH-AIDG----IPKNCQILHVEQEvvgddtTALQCVLNTDIER----TQLLEEEAQLVAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 105 EQEMGKEENFSNAATYEKLLADYDQL---------QLDYKDqgGYQYEADIRSILSGLGFPVETHQTTISTLSGGQKTRL 175
Cdd:PLN03073 276 QRELEFETETGKGKGANKDGVDKDAVsqrleeiykRLELID--AYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRI 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 176 ALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGNYSKYLDLK 255
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 256 SALYEQEIKRYEKQQDEIAKLEDFVQK---NIARASTTkraQSRRKQLDRMELLTRPLGDSkSASFHFDI-EKQSGNDVL 331
Cdd:PLN03073 434 EEQLKNQQKAFESNERSRSHMQAFIDKfryNAKRASLV---QSRIKALDRLGHVDAVVNDP-DYKFEFPTpDDRPGPPII 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDEDPII-EHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQAN-LTSSK 409
Cdd:PLN03073 510 SFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDgLDLSS 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDEYPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENA 489
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
|
490
....*....|....*....
gi 446524828 490 LIDYPGTLLFVSHDRYFIN 508
Cdd:PLN03073 670 LVLFQGGVLMVSHDEHLIS 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-253 |
3.46e-74 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 247.29 E-value: 3.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQ-NTGLETS 80
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQhQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWDEMltvfthlqqmetklrrleqemgkeenfsnaatyeklladydqlqLDYKDQGGyqyEADIRSILSGLGFPVETH 160
Cdd:COG0488 394 KTVLDEL--------------------------------------------RDGAPGGT---EQEVRGYLGRFLFSGDDA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKE 240
Cdd:COG0488 427 FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG 506
|
250
....*....|...
gi 446524828 241 SRRFVGNYSKYLD 253
Cdd:COG0488 507 VREYPGGYDDYLE 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-583 |
3.23e-61 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 212.62 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 333 VKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQaNLTSSKRVL 412
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP-PLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 413 N-------ELW-------------DEYPLQPEK------------------EIRTILGNFLFTGDDVLKPVSSLSGGQKA 454
Cdd:COG0488 80 DtvldgdaELRaleaeleeleaklAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVE 534
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446524828 535 KKNEMIERAAfeqqeqqenqapvqktVAQEKLnyleEKERKQLERQRTR 583
Cdd:COG0488 240 QRAERLEQEA----------------AAYAKQ----QKKIAKEEEFIRR 268
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
331-518 |
7.75e-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: 188.81 E-value: 7.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQeqanltsskr 410
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 vlnelwdeyplqpekeirtilgnflftgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180
....*....|....*....|....*...
gi 446524828 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 |
6.02e-54 |
|
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: 181.11 E-value: 6.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQntgletslti 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 wdemltvfthlqqmetklrrleqemgkeenfsnaatyeklladydqlqldykdqggyqyeadirsilsglgfpvethqtt 163
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 164 istLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKE 240
Cdd:cd03221 71 ---LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-252 |
3.93e-39 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 151.20 E-value: 3.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLEtslti 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYD----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVFTHLQQMETKlrrleqemgkeenfsnaatyekllADYDQLqldykdqggyqyeadIRSILSGLGFPVETHQTT 163
Cdd:PRK15064 395 FENDLTLFDWMSQWRQE------------------------GDDEQA---------------VRGTLGRLLFSQDDIKKS 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRR 243
Cdd:PRK15064 436 VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
....*....
gi 446524828 244 FVGNYSKYL 252
Cdd:PRK15064 516 FSGTYEEYL 524
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-510 |
2.67e-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: 136.96 E-value: 2.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG---GEI-IKPKDV---------- 66
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVlLDGRDLlelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 67 SIGYLAQNTglETSLTiwdeMLTVfthLQQMETKLRRLeqemgkeeNFSNAATYEKLLADYDQLQLDykdQGGYQYeadi 146
Cdd:COG1123 84 RIGMVFQDP--MTQLN----PVTV---GDQIAEALENL--------GLSRAEARARVLELLEAVGLE---RRLDRY---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 147 rsilsglgfpveTHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:COG1123 140 ------------PHQ-----LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 223 ryfldklvtqvyeisnkesrrfvgnyskyLDLKSALyeqeikryekqQDEIAKLEDFVqknIARASTTKRAQSRRKQLDR 302
Cdd:COG1123 203 -----------------------------LGVVAEI-----------ADRVVVMDDGR---IVEDGPPEEILAAPQALAA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 303 MELLTRPLGDSKSASfhfdiekQSGNDVLQVKDATIGYDED-----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIV 377
Cdd:COG1123 240 VPRLGAARGRAAPAA-------AAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 378 NKLQLLHGDVAF-GSNVS-------------VGY-----YDQeqanLTSSKRVLNELwdEYPLQ-----PEKEIRTILGN 433
Cdd:COG1123 313 GLLRPTSGSILFdGKDLTklsrrslrelrrrVQMvfqdpYSS----LNPRMTVGDII--AEPLRlhgllSRAERRERVAE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 434 FLftgDDV-LKP------VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILeNALIDY---PG-TLLFVS 501
Cdd:COG1123 387 LL---ERVgLPPdladryPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVsVQAQIL-NLLRDLqreLGlTYLFIS 462
|
570
....*....|...
gi 446524828 502 HD----RYFINRV 510
Cdd:COG1123 463 HDlavvRYIADRV 475
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-240 |
2.92e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS----------IGYLA 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYlDGKPLSampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLetsltiWDEmlTVfthlqqmetklrrleqemgkEENFSNAATYEKLLADYDQLqldykdqggyqyeadiRSILSG 152
Cdd:COG4619 81 QEPAL------WGG--TV--------------------RDNLPFPFQLRERKFDRERA----------------LELLER 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 153 LGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVSHDRYFLDK 228
Cdd:COG4619 117 LGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIER 196
|
250
....*....|..
gi 446524828 229 LVTQVYEISNKE 240
Cdd:COG4619 197 VADRVLTLEAGR 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-238 |
1.32e-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: 127.60 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS----IGYLA 72
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepIRDAREDyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLETSLTIWdEMLTVFTHLQQMETKLRRLEQEMgkeenfsnaatyeklladyDQLQLdykdqGGYqyeADIRsilsg 152
Cdd:COG4133 82 HADGLKPELTVR-ENLRFWAALYGLRADREAIDEAL-------------------EAVGL-----AGL---ADLP----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 153 lgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP---GAILIVSHDRYFLDKl 229
Cdd:COG4133 129 -----------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA- 196
|
....*....
gi 446524828 230 vTQVYEISN 238
Cdd:COG4133 197 -ARVLDLGD 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-240 |
8.62e-32 |
|
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: 123.43 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI--------IKPKDV--SIGYLA 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREArrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLETSLTIWdEMLTVFTHLQQMEtklrrleqemgkeenfsnaatyeklladydqlqldykdqgGYQYEADIRSILSG 152
Cdd:COG4555 81 DERGLYDRLTVR-ENIRYFAELYGLF----------------------------------------DEELKKRIEELIEL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 153 LGFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRYFLDKL 229
Cdd:COG4555 120 LGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEAL 198
|
250
....*....|.
gi 446524828 230 VTQVYEISNKE 240
Cdd:COG4555 199 CDRVVILHKGK 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
4.93e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.32 E-value: 4.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SIGYLAQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIWdEMLTVFTHLQQMETKLRRleqemgkeenfsnaATYEKLLadyDQLQL-DYKDQggyqyeadirsilsg 152
Cdd:COG1131 81 EPALYPDLTVR-ENLRFFARLYGLPRKEAR--------------ERIDELL---ELFGLtDAADR--------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 153 lgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSHD 222
Cdd:COG1131 128 ----------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-304 |
8.08e-31 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 127.98 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTgLEtslt 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ-LE---- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 iwdemltvftHLQQMETKLRRLEQEMGKEenfsnaatYEKLLADYdqlqldykdqggyqyeadirsiLSGLGFPVETHQT 162
Cdd:PRK10636 387 ----------FLRADESPLQHLARLAPQE--------LEQKLRDY----------------------LGGFGFQGDKVTE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESR 242
Cdd:PRK10636 427 ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 243 RFVGNYSKYLDLKSALYEQEIKRYEKQQDEIAKLEDfVQKNIARASTTKRAQSR--RKQLDRME 304
Cdd:PRK10636 507 PFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSAQ-ARKDQKRREAELRTQTQplRKEIARLE 569
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
331-517 |
1.68e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS----------VGYYD 399
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLSampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 QE--------QANLTSSKRVLNELWDEyplqpeKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:COG4619 81 QEpalwggtvRDNLPFPFQLRERKFDR------ERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 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 |
7.10e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.27 E-value: 7.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVS-----VGYYDQeqa 403
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 NLTSSKR--------VLNELWDEYPL--QPEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARLALAKLMM 463
Cdd:COG1121 83 RAEVDWDfpitvrdvVLMGRYGRRGLfrRPSRADREAV-------DEALervgledladRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 464 QKSNLLILDEPTNHLDLNSKEILEN---ALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
2.06e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.73 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQN 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETS--LTIWDemlTVFTHLQQMETKLRRLeqemGKEEnfsNAATYEKLladyDQLQL-DYKDQggyqyeadirsils 151
Cdd:COG1121 84 AEVDWDfpITVRD---VVLMGRYGRRGLFRRP----SRAD---REAVDEAL----ERVGLeDLADR-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 glgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSHDRYFLDK 228
Cdd:COG1121 136 -----------PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVRE 204
|
....*
gi 446524828 229 LVTQV 233
Cdd:COG1121 205 YFDRV 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
332-510 |
5.03e-29 |
|
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: 114.94 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVS-----VGYYDQ-EQAN 404
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFGKPLEkerkrIGYVPQrRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 405 LTSSKRVLnEL----------WDEYPLQPEKEI------RTILGNFLftgddvLKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:cd03235 81 RDFPISVR-DVvlmglyghkgLFRRLSKADKAKvdealeRVGLSELA------DRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 469 LILDEPTNHLDLNSKEI---LENALIDYPGTLLFVSHD----RYFINRV 510
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHDlglvLEYFDRV 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-238 |
5.57e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 113.26 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SIGYLAQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkEPEEVkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLetsltiwDEMLTVFTHLQqmetklrrleqemgkeenfsnaatyeklladydqlqldykdqggyqyeadirsilsgl 153
Cdd:cd03230 81 EPSL-------YENLTVRENLK---------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 154 gfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRYFLDKLV 230
Cdd:cd03230 96 -------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLC 162
|
....*...
gi 446524828 231 TQVYEISN 238
Cdd:cd03230 163 DRVAILNN 170
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
234-318 |
7.73e-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: 109.97 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 234 YEISNKESRRFVGNYSKYLDLKSALYEQEIKRYEKQQDEIAKLEDFVQKNIARASTTKRAQSRRKQLDRMELLTRPLGDS 313
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 446524828 314 KSASF 318
Cdd:pfam12848 81 PKLRF 85
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-230 |
8.43e-29 |
|
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: 115.53 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlasLSRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIWDemlTV----FTHlqqmetkLRRLEQEMGKEEnfsnAATYEKLladyDQLQL-DYKDQggyqyeadi 146
Cdd:COG1120 81 PQEPPAPFGLTVRE---LValgrYPH-------LGLFGRPSAEDR----EAVEEAL----ERTGLeHLADR--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 147 rsilsglgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:COG1120 134 ----------------PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
250
....*....|...
gi 446524828 223 -----RYFlDKLV 230
Cdd:COG1120 198 lnlaaRYA-DRLV 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
344-589 |
9.60e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 117.91 E-value: 9.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEqANLTSSKRV------------ 411
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQE-PQLDPEKTVrenveegvaevk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 412 -----LNELWDEYPLQPEK---------EIRTI--------LGNFLFTGDDVLK------PVSSLSGGQKARLALAKLMM 463
Cdd:PRK11819 100 aaldrFNEIYAAYAEPDADfdalaaeqgELQEIidaadawdLDSQLEIAMDALRcppwdaKVTKLSGGERRRVALCRLLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 464 QKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEKKnemiera 543
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK------- 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446524828 544 afeqqeqqenqapvQKTVAQEklnyleekERKQLERQRTRKiEELE 589
Cdd:PRK11819 253 --------------AKRLAQE--------EKQEAARQKALK-RELE 275
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-251 |
3.12e-27 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 116.37 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQN-TGLETSLT 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSrDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWdemltvfthlqqmetklrrleqemgkeENFSNAAtyeklladyDQLQLdykdqGGYQYEAdiRSILSGLGFPVETHQT 162
Cdd:PRK11819 405 VW---------------------------EEISGGL---------DIIKV-----GNREIPS--RAYVGRFNFKGGDQQK 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQV--YEiSNKE 240
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHIlaFE-GDSQ 520
|
250
....*....|.
gi 446524828 241 SRRFVGNYSKY 251
Cdd:PRK11819 521 VEWFEGNFQEY 531
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
330-529 |
4.34e-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: 109.11 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVsvgyydqeQANLTSS 408
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPI--------RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 KRVLNELWDEYPLQPEkeiRTILGNFLF---------TGDDVL-------------KPVSSLSGGQKARLALAKLMMQKS 466
Cdd:COG4133 74 RRRLAYLGHADGLKPE---LTVRENLRFwaalyglraDREAIDealeavglagladLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 467 NLLILDEPTNHLDLNSKEILENALIDYP---GTLLFVSHDryfinrvtttvvELSTEGAQEY-LGDY 529
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQ------------PLELAAARVLdLGDF 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-239 |
1.01e-26 |
|
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: 108.39 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 5 QVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----IGYLAQNTGLE 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEkerkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 79 TS--LTIWDEMLTVFTHLQQMETKLRRleqemgkeenfsnaATYEKLLADYDQLQL-DYKDQggyqyeadirsilsglgf 155
Cdd:cd03235 81 RDfpISVRDVVLMGLYGHKGLFRRLSK--------------ADKAKVDEALERVGLsELADR------------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 156 pvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQyLQGYPGAILIVSHDRYFLDKLVT 231
Cdd:cd03235 129 -------QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHDLGLVLEYFD 200
|
....*...
gi 446524828 232 QVYEISNK 239
Cdd:cd03235 201 RVLLLNRT 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
330-503 |
1.29e-26 |
|
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: 108.98 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS----------VGYY 398
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQA---NLTsskrVLnelwdE------YPLQP------EKEIRTIlgnflftgDDVL----------KPVSSLSGGQK 453
Cdd:COG1120 81 PQEPPapfGLT----VR-----ElvalgrYPHLGlfgrpsAEDREAV--------EEALertglehladRPVDELSGGER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSK-EILE--NALIDYPG-TLLFVSHD 503
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQlEVLEllRRLARERGrTVVMVLHD 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-195 |
4.24e-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: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYLAQNTGLETSLTIWDEM 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlLDGQDLTdderkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 88 ltvfthlqqmetKLRRLEQEMGKEEnfsnaatyeklladydqlqldykdqggyqYEADIRSILSGLGFPVETHQT---TI 164
Cdd:pfam00005 81 ------------RLGLLLKGLSKRE-----------------------------KDARAEEALEKLGLGDLADRPvgeRP 119
|
170 180 190
....*....|....*....|....*....|.
gi 446524828 165 STLSGGQKTRLALGKLLLTKPDLLILDEPTN 195
Cdd:pfam00005 120 GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-233 |
4.93e-26 |
|
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: 106.15 E-value: 4.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigylaqntgletslTI 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------------------TF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WD-EMLTVFTHLQQMETKLRR--LEQEMGKEENFSNAATYeklladydqLQLDYKdqggyqyeaDIRSILSGLGFPVETH 160
Cdd:cd03268 60 DGkSYQKNIEALRRIGALIEApgFYPNLTARENLRLLARL---------LGIRKK---------RIDEVLDVVGLKDSAK 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 161 QtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP---GAILIVSHDRYFLDKLVTQV 233
Cdd:cd03268 122 K-KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRI 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
332-517 |
5.22e-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: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVafgsnvsvgyydqeqanltsskRV 411
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------------LI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 412 LNELWDEYPLqpeKEIRTILGnFLFtgddvlkpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI 491
Cdd:cd00267 59 DGKDIAKLPL---EELRRRIG-YVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180
....*....|....*....|....*....
gi 446524828 492 DYPG---TLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd00267 125 ELAEegrTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-238 |
1.14e-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: 105.24 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 5 QVNGLSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYL 71
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlVDGKDLTklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTglETSL---TIWDEMLTVFTHLQ----QMETKLRRLEQEMGKEEnfsnaatyeklLADYDqlqldykdqggyqyea 144
Cdd:cd03225 81 FQNP--DDQFfgpTVEEEVAFGLENLGlpeeEIEERVEEALELVGLEG-----------LRDRS---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 dirsilsglgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSH 221
Cdd:cd03225 132 -------------------PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTH 192
|
250
....*....|....*..
gi 446524828 222 DRYFLDKLVTQVYEISN 238
Cdd:cd03225 193 DLDLLLELADRVIVLED 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-223 |
4.30e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.15 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII----------KPKDVSIGYLAQ 73
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLetsltiwdemltvFTHLQQME------TKLRRLEQEMgkeenfsnAATYEKLLadyDQLQLDykdqggyqyeadir 147
Cdd:COG1118 83 HYAL-------------FPHMTVAEniafglRVRPPSKAEI--------RARVEELL---ELVQLE-------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 148 silsGLG--FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI---ETL-TWLEQYLQGYPGAILIVSH 221
Cdd:COG1118 125 ----GLAdrYP---SQ-----LSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELrRWLRRLHDELGGTTVFVTH 192
|
..
gi 446524828 222 DR 223
Cdd:COG1118 193 DQ 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
332-503 |
8.85e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.74 E-value: 8.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVafgsnvsvgYYDQEqaNLTSSKRv 411
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---------LLDGK--DLASLSP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 412 lnelwdeyplqpeKEIRTILGnFLFTGDDVL-------KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSK 483
Cdd:cd03214 69 -------------KELARKIA-YVPQALELLglahladRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIaHQI 134
|
170 180
....*....|....*....|...
gi 446524828 484 EILE--NALIDYPG-TLLFVSHD 503
Cdd:cd03214 135 ELLEllRRLARERGkTVVMVLHD 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-238 |
3.51e-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: 107.16 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGY 70
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLRrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTgletsltiwdemltvftHLqqMETKLR---RLeqemGKEEnfsnaATYEKLLADYDQLQLDykdqggyqyeADIR 147
Cdd:COG4987 414 VPQRP-----------------HL--FDTTLRenlRL----ARPD-----ATDEELWAALERVGLG----------DWLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 148 SILSGLGFPV-ETHqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGypGAILIVSHD 222
Cdd:COG4987 456 ALPDGLDTWLgEGG----RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeqalLADLLEALAG--RTVLLITHR 529
|
250
....*....|....*.
gi 446524828 223 RYFLDKlVTQVYEISN 238
Cdd:COG4987 530 LAGLER-MDRILVLED 544
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
331-502 |
2.47e-23 |
|
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: 97.07 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsivnklqLLhgdvafgsnvsVGYYDQEQANLtss 408
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLK-------LL-----------LRLYDPTSGEI--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 krvlneLWDEYPLQ--PEKEIRTILG-----NFLFTGD--DVLkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03228 60 ------LIDGVDLRdlDLESLRKNIAyvpqdPFLFSGTirENI-----LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180
....*....|....*....|....*
gi 446524828 480 LNSKEILENALIDYPG--TLLFVSH 502
Cdd:cd03228 129 PETEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
6.65e-23 |
|
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: 96.35 E-value: 6.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 5 QVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYLAQ 73
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlasLSPKELArkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NtgletsltiwdemltvfthLQQMETklrrleqemgkeenfsnaatyeklladydqlqLDYKDQGgyqyeadirsilsgl 153
Cdd:cd03214 81 A-------------------LELLGL--------------------------------AHLADRP--------------- 94
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 154 gfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:cd03214 95 ----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
331-503 |
9.79e-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: 95.54 E-value: 9.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVSvgyydqeqANLTSSK 409
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIK--------KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDEYPLQPEkeirtilgnflFTGDDVLKpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENA 489
Cdd:cd03230 73 RRIGYLPEEPSLYEN-----------LTVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170
....*....|....*..
gi 446524828 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 |
1.38e-22 |
|
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: 96.38 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS----------VGYY 398
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQANLTSSKRVLNELwdEYPL----QPEKEIRTILGNFL-FTGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03225 81 FQNPDDQFFGPTVEEEV--AFGLenlgLPEEEIEERVEEALeLVGLEGLrdRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 472 DEPTNHLDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
300-515 |
3.54e-22 |
|
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: 101.45 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 300 LDRM-ELLTRPLgDSKSASFHFDIEKQSGNdvLQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI 376
Cdd:COG2274 445 LERLdDILDLPP-EREEGRSKLSLPRLKGD--IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 377 VNKLQLLHGDVAF-GSNV----------SVGYYDQEQA--------NLTsskrvlneLWDEYPlqPEKEIRTILgnfLFT 437
Cdd:COG2274 522 LGLYEPTSGRILIdGIDLrqidpaslrrQIGVVLQDVFlfsgtireNIT--------LGDPDA--TDEEIIEAA---RLA 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 438 G--DDVLK-------PV----SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:COG2274 589 GlhDFIEAlpmgydtVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH 668
|
250
....*....|...
gi 446524828 503 DRYFINRVTTTVV 515
Cdd:COG2274 669 RLSTIRLADRIIV 681
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-251 |
3.86e-22 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 101.48 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQN--TGLETSLTIWDEMLTVF 91
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHhvDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 92 THLqqMETKLRRLEQEMGKEENFSNAATYeklladydqlqldykdqggyqyeadirsilsglgfpvethqttisTLSGGQ 171
Cdd:PLN03073 600 PGV--PEQKLRAHLGSFGVTGNLALQPMY---------------------------------------------TLSGGQ 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 172 KTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISNKESRRFVGNYSKY 251
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-238 |
4.13e-22 |
|
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: 93.08 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 5 QVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSigylaqntgletslti 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 wdemltvfthlqqmETKLRRLEQEMGkeenfsnaatyeklladydqlqldykdqggyqyeadirsilsglgfpvethqtT 163
Cdd:cd00267 65 --------------KLPLEELRRRIG-----------------------------------------------------Y 77
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPgAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:cd00267 78 VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASrerlLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-223 |
5.90e-22 |
|
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: 94.51 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQN 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDEMLTVFTHLQQMETKLRRLEQEMgkeenfsnaatyEKLLADYDQLQldykdqggyqyeadiRSilsglg 154
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVREL------------LELVGLEGLLN---------------RY------ 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 155 fpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILI-VSHDR 223
Cdd:cd03259 128 ---------PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqreLGITTIyVTHDQ 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-222 |
5.93e-22 |
|
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: 94.88 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY----GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS---------- 67
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfDGKDLLklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 ---IGYLAQNTGleTSLtiwDEMLTVFTHLqqMETkLRRLEQEMGKEENfsnaatYEKLLADYDQLQLDykdqggyqyEA 144
Cdd:cd03257 81 rkeIQMVFQDPM--SSL---NPRMTIGEQI--AEP-LRIHGKLSKKEAR------KEAVLLLLVGVGLP---------EE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 DIRSilsglgFPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVS 220
Cdd:cd03257 138 VLNR------YP---HE-----LSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFIT 203
|
..
gi 446524828 221 HD 222
Cdd:cd03257 204 HD 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
339-514 |
7.02e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 339 GYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQA-----NLTSSKRVLN 413
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpdslPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 414 ELWDEYPL--QPEKEIRTILGNFL--FTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILEN 488
Cdd:NF040873 81 GRWARRGLwrRLTRDDRAAVDDALerVGLADLAGrQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 446524828 489 ALIDYPG---TLLFVSHDRYFINRVTTTV 514
Cdd:NF040873 161 LLAEEHArgaTVVVVTHDLELVRRADPCV 189
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
331-515 |
7.97e-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: 99.84 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsNVSVGYYDQEQ-ANLTS 407
Cdd:COG4987 334 LELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDlRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 408 skrVLNE---LWDEyplqpekeirTILGNFLFTGDD--------VLKPV---------------------SSLSGGQKAR 455
Cdd:COG4987 413 ---VVPQrphLFDT----------TLRENLRLARPDatdeelwaALERVglgdwlaalpdgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 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 |
8.23e-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: 91.94 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKL-----------QLLHGDVAFGSNVSVGYYDQEqANLTSSKRVLNE 414
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsptegtilldgQDLTDDERKSLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 415 LWD----EYPLQPEKEIRTI-----LGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:pfam00005 80 LRLglllKGLSKREKDARAEealekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
332-519 |
1.77e-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: 92.71 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDEDP-IIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNV--------SVGYYDQE- 401
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QANLTSSKrVLNELW---DEYPLQPEKeIRTILGNF-LFTGDDVLkPVSsLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03226 81 DYQLFTDS-VREELLlglKELDAGNEQ-AETVLKDLdLYALKERH-PLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524828 478 LDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELST 519
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-238 |
1.91e-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: 94.10 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGA----ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDV-----S 67
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpVTRRRRkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 IGYLAQNTglETSLtiwDEMLTVFTHLqqMETklrrleqemgkeenfsnaatyeklladydqlqldYKDQGGYQYEADIR 147
Cdd:COG1124 81 VQMVFQDP--YASL---HPRHTVDRIL--AEP----------------------------------LRIHGLPDREERIA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 148 SILSGLGFPVET-----HQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILI 218
Cdd:COG1124 120 ELLEQVGLPPSFldrypHQ-----LSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLF 194
|
250 260
....*....|....*....|
gi 446524828 219 VSHDRYFLDKLVTQVYEISN 238
Cdd:COG1124 195 VSHDLAVVAHLCDRVAVMQN 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-240 |
2.27e-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: 93.17 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS-----IGYL 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLRelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTglETSL---TIWDEMLtvFThlqqmetkLRRL---EQEMgkeenfsnAATYEKLLADYDqLQlDYKDQggyqyead 145
Cdd:COG1122 81 FQNP--DDQLfapTVEEDVA--FG--------PENLglpREEI--------RERVEEALELVG-LE-HLADR-------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 146 irsilsglgfpvETHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHD 222
Cdd:COG1122 131 ------------PPHE-----LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHD 193
|
250
....*....|....*...
gi 446524828 223 RYFLDKLVTQVYEISNKE 240
Cdd:COG1122 194 LDLVAELADRVIVLDDGR 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-487 |
2.81e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQtKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDvsigy 70
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELR-PGEVhALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrSPRD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 lAQNTGLEtslTIWDEmLTVFTHLQQMET-KLRRLEQEMGKeenfsnaatyeklladydqlqLDYKDQggyqyEADIRSI 149
Cdd:COG1129 76 -AQAAGIA---IIHQE-LNLVPNLSVAENiFLGREPRRGGL---------------------IDWRAM-----RRRAREL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 150 LSGLGFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----------IETLTwlEQylqgypG-AILI 218
Cdd:COG1129 125 LARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTereverlfriIRRLK--AQ------GvAIIY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 219 VSHdryFLDklvtQVYEISnkesrrfvgnyskyldlksalyeqeikryekqqDEIAKLED--FVqkniarasttkrAQSR 296
Cdd:COG1129 196 ISH---RLD----EVFEIA---------------------------------DRVTVLRDgrLV------------GTGP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 297 RKQLDRMELLTRPLGDSKSASFHfDIEKQSGNDVLQVKDATIGydedPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI 376
Cdd:COG1129 224 VAELTEDELVRLMVGRELEDLFP-KRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 377 --VNKLQ----LLHG-DVAFGS-----------------------NVSVgyydQEQANLTSSKRVLNELWdeypLQPEKE 426
Cdd:COG1129 299 fgADPADsgeiRLDGkPVRIRSprdairagiayvpedrkgeglvlDLSI----RENITLASLDRLSRGGL----LDRRRE 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 427 ------------IRTilgnflftgDDVLKPVSSLSGG--QKArlALAKLMMQKSNLLILDEPTNHLDLNSK-EILE 487
Cdd:COG1129 371 ralaeeyikrlrIKT---------PSPEQPVGNLSGGnqQKV--VLAKWLATDPKVLILDEPTRGIDVGAKaEIYR 435
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
345-541 |
3.97e-21 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 98.01 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLK--------SIVNKLQLLH------GD------VAFGSNVSVGYYDQEQAN 404
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidGIPKNCQILHveqevvGDdttalqCVLNTDIERTQLLEEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 405 LTSSKRVLN--------------------------------ELWDEYplQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQ 452
Cdd:PLN03073 272 LVAQQRELEfetetgkgkgankdgvdkdavsqrleeiykrlELIDAY--TAEARAASILAGLSFTPEMQVKATKTFSGGW 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 453 KARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYY 532
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTF 429
|
....*....
gi 446524828 533 VEKKNEMIE 541
Cdd:PLN03073 430 ERTREEQLK 438
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
330-545 |
5.56e-21 |
|
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: 92.61 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVN-------KLQLLHGDVAFGSNV---SVGYYD 399
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgSILIDGEDVRKEPREarrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 QEQ---ANLTSSK--RVLNELWDEYPLQPEKEIRTILGNFLFtgDDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:COG4555 81 DERglyDRLTVREniRYFAELYGLFDEELKKRIEELIELLGL--EEFLdRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 474 PTNHLDLNSKEILEN---ALIDYPGTLLFVSHDRYFINRVTTTVVELStEGAQEYLGDYDYYVEKKNEMIERAAF 545
Cdd:COG4555 159 PTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
297-503 |
7.45e-21 |
|
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: 96.66 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 297 RKQLDRMELLTRPLGDSKSASFHFDIEKQSGNDVLQVKDATIGYDEDPII-EHVNMRLTRGDSVALVGPNGIGKSTLLKS 375
Cdd:TIGR02868 301 RAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 376 IVNKLQLLHGDVAFGSnVSVGYYDQ-----------EQANLTSSKrVLNELWDEYPLQPEKEIRTI-----LGNFLFTGD 439
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDG-VPVSSLDQdevrrrvsvcaQDAHLFDTT-VRENLRLARPDATDEELWAAlervgLADWLRALP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 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 ... |
11-233 |
1.03e-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: 90.78 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 11 KLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDV--SIGYLAQNTGLE-TSL 81
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpIKAKERrkSIGYVMQDVDYQlFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 TIWDEMLtvfthlqqmetklrrleqeMGKEENFSNAATYEKLLADYDQLQLDykdqggyqyeadirsilsglgfpvETHQ 161
Cdd:cd03226 88 SVREELL-------------------LGLKELDAGNEQAETVLKDLDLYALK------------------------ERHP 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 162 TTistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD---IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQV 233
Cdd:cd03226 125 LS---LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-222 |
1.84e-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: 96.06 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYLAQNTGL-ETS----L 81
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqIDPASLrrQIGVVLQDVFLfSGTirenI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 TIWDEMLTvfthLQQMETKLRRLEqemgkeenfsnaatyekLLADYDQLQLdykdqgGYQyeadirSILSGLGfpvethq 161
Cdd:COG2274 570 TLGDPDAT----DEEIIEAARLAG-----------------LHDFIEALPM------GYD------TVVGEGG------- 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 162 ttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:COG2274 610 ---SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-194 |
2.73e-20 |
|
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: 89.80 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------IGYL 71
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIwdemltvfthlqqmetklrrleqemgkEENFsnaatyekLLADYDQLQLDYKDQGGYQYEAdirsils 151
Cdd:cd03224 81 PEGRRIFPELTV---------------------------EENL--------LLGAYARRRAKRKARLERVYEL------- 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524828 152 glgFPV--ETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:cd03224 119 ---FPRlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
303-515 |
2.76e-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: 94.82 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 303 MELLTRPLGDSKSASfhfDIEKQSGNDVLQVKDATIGYDED-PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ 381
Cdd:COG4988 312 FALLDAPEPAAPAGT---APLPAAGPPSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 382 LLHGDVAFGsNVSVGYYDQEQ--------------------ANLTSSK---------RVLNE--LWDEYPLQPEKeIRTI 430
Cdd:COG4988 389 PYSGSILIN-GVDLSDLDPASwrrqiawvpqnpylfagtirENLRLGRpdasdeeleAALEAagLDEFVAALPDG-LDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 431 LGNflfTGddvlkpvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFIN 508
Cdd:COG4988 467 LGE---GG-------RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLA 536
|
....*..
gi 446524828 509 RVTTTVV 515
Cdd:COG4988 537 QADRILV 543
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-222 |
3.52e-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: 89.28 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTK---DRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQNtglets 80
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 ltiwdemLTVFTHL---QQMETKLRRLEQemgKEENFSnaatYEKLLadyDQLQLDykdQGGYQYeadirsilsglgfpv 157
Cdd:cd03297 84 -------YALFPHLnvrENLAFGLKRKRN---REDRIS----VDELL---DLLGLD---HLLNRY--------------- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 158 ethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:cd03297 129 ------PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
3.73e-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: 94.44 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYL 71
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASWRrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLeTSLTIWDEMLtvfthlqqmetklrrleqeMGKEEnfsnaATYEKLLADYDQLQLDykdqggyqyeADIRSILS 151
Cdd:COG4988 417 PQNPYL-FAGTIRENLR-------------------LGRPD-----ASDEELEAALEAAGLD----------EFVAALPD 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 152 GLgfpvethQTTI----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYpgAILIVSHD 222
Cdd:COG4988 462 GL-------DTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGR--TVILITHR 531
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
5.93e-20 |
|
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: 88.72 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDV---------SIGYL 71
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSIrtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQntgletSLTIWDEmLTVFTHLQQMeTKLRRLEQEMGKEEnfsnaatyekLLADYDQLQL-DYKDqggyqyeadirsil 150
Cdd:cd03263 81 PQ------FDALFDE-LTVREHLRFY-ARLKGLPKSEIKEE----------VELLLRVLGLtDKAN-------------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 151 sglgfpvethqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:cd03263 129 -----------KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-238 |
8.90e-20 |
|
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: 88.32 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------- 67
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDISklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 ---IGYLAQNTGLETSLTIwdemltvfthlqqmetklrrleqemgkEENFSnaatyeklladydqLQLDYKDQGGYQYEA 144
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTA---------------------------LENVE--------------LPLLLAGVPKKERRE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 DIRSILSGLGFPvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVS 220
Cdd:cd03255 120 RAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVT 198
|
250
....*....|....*...
gi 446524828 221 HDRyFLDKLVTQVYEISN 238
Cdd:cd03255 199 HDP-ELAEYADRIIELRD 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-222 |
1.05e-19 |
|
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: 88.30 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQ 73
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIWDemltvfthlqqmetklrrleqemgkeenfsNAAtyeklladydqLQLDYKDQGGYQYEADIRSILS-- 151
Cdd:cd03293 81 QDALLPWLTVLD------------------------------NVA-----------LGLELQGVPKAEARERAEELLElv 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 GLG-----FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:cd03293 120 GLSgfenaYP---HQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
1.19e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 88.99 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGY 70
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETSLTIWDemltvfthlqqmetklrrleqemgkeenfsNAAtyeklladydqLQLDYKDQGGYQYEADIRSIL 150
Cdd:COG1116 85 VFQEPALLPWLTVLD------------------------------NVA-----------LGLELRGVPKAERRERARELL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 S--GLG-----FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET---L-TWLEQYLQGYPGAILIV 219
Cdd:COG1116 124 ElvGLAgfedaYP---HQ-----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerLqDELLRLWQETGKTVLFV 195
|
...
gi 446524828 220 SHD 222
Cdd:COG1116 196 THD 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
331-518 |
1.37e-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: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDV-AFGSNVSvgyydqeQANLTS- 407
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlVDGKDIT-------KKNLREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 408 SKRV-------LNEL-----WDE---YPLQ---PEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARLALA 459
Cdd:COG1122 74 RRKVglvfqnpDDQLfaptvEEDvafGPENlglPREEIRERV-------EEALelvglehladRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 460 KLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
328-502 |
1.54e-19 |
|
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: 88.60 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsivnklqLLHGDV--AFGSNVSV---------- 395
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS-------LITGDLppTYGNDVRLfgerrggedv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 396 -------GYYDQE-QANLTSSKRVLN----------ELWDEYPLQPEKEIRTILGnfLFTGDDVL-KPVSSLSGGQKARL 456
Cdd:COG1119 74 welrkriGLVSPAlQLRFPRDETVLDvvlsgffdsiGLYREPTDEQRERARELLE--LLGLAHLAdRPFGTLSQGEQRRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 457 ALAKLMMQKSNLLILDEPTNHLDLNSKE-ILE--NALIDYPG-TLLFVSH 502
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARElLLAllDKLAAEGApTLVLVTH 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-222 |
2.45e-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: 91.65 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----IKPKDVS-------IGYL 71
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgVPVSSLDqdevrrrVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSlTIWDEMLtvfthlqqmetklrrleqeMGKEEnfsnaATYEKLLADYDQLQLdykdqggyqyEADIRSILS 151
Cdd:TIGR02868 415 AQDAHLFDT-TVRENLR-------------------LARPD-----ATDEELWAALERVGL----------ADWLRALPD 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 152 GLGFPVETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET-LTWLEQYLQGYPG-AILIVSHD 222
Cdd:TIGR02868 460 GLDTVLGEGG---ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAALSGrTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-233 |
3.71e-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: 86.49 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVS--IGYLAQNTGLeTSLTIWDEm 87
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqLDPADLRrnIGYVPQDVTL-FYGTLRDN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 88 LTVFTHLQQMETKLRRLEqemgkeenFSNAATYEKLLADYDQLQLDykdQGGYQyeadirsilsglgfpvethqttistL 167
Cdd:cd03245 98 ITLGAPLADDERILRAAE--------LAGVTDFVNKHPNGLDLQIG---ERGRG-------------------------L 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHdRYFLDKLVTQV 233
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRI 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-223 |
4.88e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQN 74
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrFHGTDVSrlhardrkVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDEM---LTVFThlqqmetklRRleqemgkeENFSNAATYEKLLADYDQLQLDYKdqggyqyeADirsils 151
Cdd:PRK10851 83 YALFRHMTVFDNIafgLTVLP---------RR--------ERPNAAAIKAKVTQLLEMVQLAHL--------AD------ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 152 glGFPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHDR 223
Cdd:PRK10851 132 --RYP--------AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
1.38e-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: 85.18 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------IGYL 71
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGEDITglppheiarlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIWDE-MLTVFTHLQQMETKLRRLEQEmgkeenfsnAATYEKLLADYDQLQLdykdqggyqyeADIRSIL 150
Cdd:cd03219 81 FQIPRLFPELTVLENvMVAAQARTGSGLLLARARREE---------REARERAEELLERVGL-----------ADLADRP 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 151 SGlgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT---NHLDIETLTWLEQYL--QGYpgAILIVSHD 222
Cdd:cd03219 141 AG-------------ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELreRGI--TVLLVEHD 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-230 |
1.53e-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: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-------------IKPKDVSIGY 70
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLetsltiwdemltvFTHLqqmetklrrleqemgkeenfsnaatyeklladydqlqldykdqggyqyeadirSIL 150
Cdd:cd03229 81 VFQDFAL-------------FPHL-----------------------------------------------------TVL 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 SGLGFPvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ------GYpgAILIVSHD-- 222
Cdd:cd03229 95 ENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaqlGI--TVVLVTHDld 162
|
250
....*....|
gi 446524828 223 --RYFLDKLV 230
Cdd:cd03229 163 eaARLADRVV 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-231 |
1.65e-18 |
|
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: 89.27 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYL 71
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladADADSWrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLeTSLTIWDEMltvfthlqqmetklrRLEQEMGKEENFSNAATyeklLADYDQLqldykdqggyqyeadIRSILS 151
Cdd:TIGR02857 402 PQHPFL-FAGTIAENI---------------RLARPDASDAEIREALE----RAGLDEF---------------VAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 GLGFPVETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYpgAILIVSHDR---Y 224
Cdd:TIGR02857 447 GLDTPIGEGG---AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeaevLEALRALAQGR--TVLLVTHRLalaA 521
|
....*..
gi 446524828 225 FLDKLVT 231
Cdd:TIGR02857 522 LADRIVV 528
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
331-502 |
1.77e-18 |
|
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: 83.42 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsNVSVGYYDqeqanltss 408
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWD--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 krvLNELWDE--YPLQPEKeirtilgnfLFTG---DDVLkpvsslSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK 483
Cdd:cd03246 71 ---PNELGDHvgYLPQDDE---------LFSGsiaENIL------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180
....*....|....*....|..
gi 446524828 484 EILENALIDYP---GTLLFVSH 502
Cdd:cd03246 133 RALNQAIAALKaagATRIVIAH 154
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
2.10e-18 |
|
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: 82.86 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigylaqntgletsltI 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI----------------------L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDemltvfthlqqmetklrrleqemGKEENFSNAAtyeklladydqlqlDYKDQGgyqyeadIRSIlsglgfpvetHQtt 163
Cdd:cd03216 59 VD-----------------------GKEVSFASPR--------------DARRAG-------IAMV----------YQ-- 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 164 istLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-----QGypGAILIVSH 221
Cdd:cd03216 83 ---LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrlraQG--VAVIFISH 140
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
2.46e-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: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-------------IG 69
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDISglseaelyrlrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 70 YLAQNTGLETSLTIWDE-MLTVFTHLQQMETKLRRLeqemgkeenfsnaaTYEKL----LADYDQLqldykdqggyqyea 144
Cdd:cd03261 81 MLFQSGALFDSLTVFENvAFPLREHTRLSEEEIREI--------------VLEKLeavgLRGAEDL-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 dirsilsglgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQY---LQGYPGA-ILIVS 220
Cdd:cd03261 133 ----------YPAE--------LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLtSIMVT 194
|
..
gi 446524828 221 HD 222
Cdd:cd03261 195 HD 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
331-503 |
2.55e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.34 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVS---------VGYYDQ 400
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVArdpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 EQA---NLTSsKRVLNELWDEYPLqPEKEIRTILGNFL-FTG-DDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:COG1131 81 EPAlypDLTV-RENLRFFARLYGL-PRKEARERIDELLeLFGlTDAAdRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 446524828 475 TNHLDLNSKEILENALIDYPG---TLLFVSHD 503
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-221 |
3.59e-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: 83.18 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigyLAQNTGLETSLTI 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV----------RWNGTPLAEQRDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVFTHLQQMETKLRRLEqemgkeenfsNAATYEKLLADYDQLQLDYKDQGGyqyeadirsiLSGLgfpvetHQTT 163
Cdd:TIGR01189 71 PHENILYLGHLPGLKPELSALE----------NLHFWAAIHGGAQRTIEDALAAVG----------LTGF------EDLP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSH 221
Cdd:TIGR01189 125 AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
331-503 |
3.78e-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: 84.09 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDV-AFGSNVS-------------VG 396
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDISglseaelyrlrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 YYDQeQANLTSSKRVLNELwdEYPLQ-----PEKEIRTI----LGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSN 467
Cdd:cd03261 81 MLFQ-SGALFDSLTVFENV--AFPLRehtrlSEEEIREIvlekLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524828 468 LLILDEPTNHLD-LNSKEILEnaLI-----DYPGTLLFVSHD 503
Cdd:cd03261 157 LLLYDEPTAGLDpIASGVIDD--LIrslkkELGLTSIMVTHD 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
330-510 |
3.92e-18 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 83.71 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDED----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS---------- 394
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLLklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 ---VGYYDQE-QANLTSSKRV---LNE-LWDEYPLQPEKEIRTILGNFLF---TGDDVLK--PvSSLSGGQKARLALAKL 461
Cdd:cd03257 81 rkeIQMVFQDpMSSLNPRMTIgeqIAEpLRIHGKLSKKEARKEAVLLLLVgvgLPEEVLNryP-HELSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 462 MMQKSNLLILDEPTNHLD-LNSKEILEnaLID-----YPGTLLFVSHD----RYFINRV 510
Cdd:cd03257 160 LALNPKLLIADEPTSALDvSVQAQILD--LLKklqeeLGLTLLFITHDlgvvAKIADRV 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-502 |
4.34e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 87.76 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQV-NGLSKLYGAETILANiKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkdvsigylaqntgLET 79
Cdd:PRK10938 1 MSSLQIsQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-----------------RQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 80 SLT-IWdemLTVFTHLQQM-ETKLRRLEQEM---GKEENFSNAAtyeklladyDQLQLDYKDQGGYQYEADIRSILSGLG 154
Cdd:PRK10938 63 QFShIT---RLSFEQLQKLvSDEWQRNNTDMlspGEDDTGRTTA---------EIIQDEVKDPARCEQLAQQFGITALLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 155 FPvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGypgailiVSHDRYFLDKLVTQVY 234
Cdd:PRK10938 131 RR-------FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS-------LHQSGITLVLVLNRFD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 235 EISNkesrrFVGNYSKYLDLksALYEQEIKRYEKQQDEIAKLedfvqkniarasttkrAQSrrKQLDRMELltrPLGDSK 314
Cdd:PRK10938 197 EIPD-----FVQFAGVLADC--TLAETGEREEILQQALVAQL----------------AHS--EQLEGVQL---PEPDEP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 315 SASFHFDiekqSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIV--------NKLQL---- 382
Cdd:PRK10938 249 SARHALP----ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysNDLTLfgrr 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 383 --------------------LHGDVAFGSNV----------SVGYYDQeqanLTSSKRVLNELWdeyplqpekeiRTILG 432
Cdd:PRK10938 325 rgsgetiwdikkhigyvsssLHLDYRVSTSVrnvilsgffdSIGIYQA----VSDRQQKLAQQW-----------LDILG 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 433 NFLFTGDdvlKPVSSLSGGQKaRLAL-AKLMMQKSNLLILDEPTNHLD-LNSKEILE--NALIDYPGT-LLFVSH 502
Cdd:PRK10938 390 IDKRTAD---APFHSLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLDpLNRQLVRRfvDVLISEGETqLLFVSH 460
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
330-488 |
4.42e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-----------GSNVSVGYY 398
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdiddpdvaEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQANLTSSKRVlnELWdeyplqpekeiRTILGNFLFTGDDVLK----------PVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK13539 82 NAMKPALTVAENL--EFW-----------AAFLGGEELDIAAALEavglaplahlPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180
....*....|....*....|
gi 446524828 469 LILDEPTNHLDLNSKEILEN 488
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAE 168
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
331-481 |
4.56e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQE--------- 401
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QANLTS---SKRVL--------NELWDEYPLQPEKEIRTILGNflfTGDDVL--KPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK11231 83 QHHLTPegiTVRELvaygrspwLSLWGRLSAEDNARVNQAMEQ---TRINHLadRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170
....*....|...
gi 446524828 469 LILDEPTNHLDLN 481
Cdd:PRK11231 160 VLLDEPTTYLDIN 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-222 |
5.35e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTiwdemLTVft 92
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLP-----LTV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 93 hlqqmetklRRLeQEMGKeenFSNAATYEKLLADyDQLQLDykdqggyqyEADIRSILSGLgfpvETHQttISTLSGGQK 172
Cdd:NF040873 75 ---------RDL-VAMGR---WARRGLWRRLTRD-DRAAVD---------DALERVGLADL----AGRQ--LGELSGGQR 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 173 TRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSHD 222
Cdd:NF040873 126 QRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-221 |
5.94e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 81.66 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET--ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGY 70
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdLDLESLrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLeTSLTIWdemltvfthlqqmetklrrleqemgkeENFsnaatyeklladydqlqldykdqggyqyeadirsil 150
Cdd:cd03228 81 VPQDPFL-FSGTIR---------------------------ENI------------------------------------ 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 151 sglgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSH 221
Cdd:cd03228 97 ----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
331-515 |
6.05e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 81.85 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVsvgyyDQEQANLTSSK 409
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDL-----TDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDEYPLQPEKeirTILGNFLFtgddvlkpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILE-- 487
Cdd:cd03229 76 RRIGMVFQDFALFPHL---TVLENIAL----------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRal 142
|
170 180 190
....*....|....*....|....*....|
gi 446524828 488 -NALIDYPG-TLLFVSHDRYFINRVTTTVV 515
Cdd:cd03229 143 lKSLQAQLGiTVVLVTHDLDEAARLADRVV 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
331-490 |
1.26e-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: 81.64 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGS---NVSVGYYDQEQANLTS 407
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 408 SKRVLNELWDEYPLQpekEIRTILGNFLFTGDDVLK----------PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:TIGR01189 81 LPGLKPELSALENLH---FWAAIHGGAQRTIEDALAavgltgfedlPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|...
gi 446524828 478 LDLNSKEILENAL 490
Cdd:TIGR01189 158 LDKAGVALLAGLL 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-200 |
1.50e-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: 81.86 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTkDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------IGYLAQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIWdEMLTVFTHLQQMETKLRRleqemgkeenfsnaATYEKLLadyDQLQL-DYKDQggyqyeadirsilsg 152
Cdd:cd03264 80 EFGVYPNFTVR-EFLDYIAWLKGIPSKEVK--------------ARVDEVL---ELVNLgDRAKK--------------- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 153 lgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:cd03264 127 ----------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
1.80e-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: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS---------IGy 70
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfDGRDITglpphriarLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LA---QNTGLETSLTIWDEMLtVFTHLQQMETKLRRLEQ--EMGKEENFSNAATYEkLLadyDQLQLdykdqggyqyeAD 145
Cdd:COG0411 81 IArtfQNPRLFPELTVLENVL-VAAHARLGRGLLAALLRlpRARREEREARERAEE-LL---ERVGL-----------AD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 146 IRSILSGlgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT---NHLDIETLTWLEQYLQGYPG-AILIVSH 221
Cdd:COG0411 145 RADEPAG-------------NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEH 211
|
.
gi 446524828 222 D 222
Cdd:COG0411 212 D 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-244 |
2.60e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLS-KLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTgletslt 82
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRP------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 iwdemltvftHLQQmeTKLRRleqemgkeenfsnAATYEKLLADYDqlqldykdqggyqyEADIRSILS--GLGFPVE-- 158
Cdd:COG4178 436 ----------YLPL--GTLRE-------------ALLYPATAEAFS--------------DAELREALEavGLGHLAErl 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 159 -THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQG-YPGAILI-VSHdRYFLDKLVTQVYE 235
Cdd:COG4178 477 dEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTTVIsVGH-RSTLAAFHDRVLE 555
|
....*....
gi 446524828 236 ISNKESRRF 244
Cdd:COG4178 556 LTGDGSWQL 564
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
2.85e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigyLAQNTGLETSlti 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------LAGTAPLAEA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 wdemltvfthlqQMETKLrrleqeMgkeenFSNAatyeKLL---ADYDQLQLDYKdqGGYQYEAdiRSILSGLGFpVETH 160
Cdd:PRK11247 80 ------------REDTRL------M-----FQDA----RLLpwkKVIDNVGLGLK--GQWRDAA--LQALAAVGL-ADRA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----------IETLtWLEqylQGYpgAILIVSHD 222
Cdd:PRK11247 128 NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdlIESL-WQQ---HGF--TVLLVTHD 193
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
2.98e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.24 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------- 67
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlIDGQDISslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 ----IGYLAQNTGLETSLTIWDemltvfthlqqmetklrrleqemgkeenfsNAAtyeklladydqLQLDYKDQGGYQYE 143
Cdd:COG1136 84 rrrhIGFVFQFFNLLPELTALE------------------------------NVA-----------LPLLLAGVSRKERR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 144 ADIRSILSGLG-------FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGY 212
Cdd:COG1136 123 ERARELLERVGlgdrldhRP--------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNREL 194
|
250 260
....*....|....*....|....*.
gi 446524828 213 PGAILIVSHDRyFLDKLVTQVYEISN 238
Cdd:COG1136 195 GTTIVMVTHDP-ELAARADRVIRLRD 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-194 |
4.35e-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: 80.80 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------I 68
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITglpphriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 69 GYLAQNTGLETSLTIwdemltvfthlqqmetklrrleqemgkEENfsnaatyeklladydqLQLdykdqGGY------QY 142
Cdd:COG0410 81 GYVPEGRRIFPSLTV---------------------------EEN----------------LLL-----GAYarrdraEV 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 143 EADIRSILSgLgFPV--ETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:COG0410 113 RADLERVYE-L-FPRlkERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
4.50e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 83.22 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYL 71
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlLDGRDVTglppekrnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLetsltiwdemltvFTHLqqmeT---------KLRRleqeMGKEEnfsNAATYEKLLadyDQLQLDykdqggyqy 142
Cdd:COG3842 83 FQDYAL-------------FPHL----TvaenvafglRMRG----VPKAE---IRARVAELL---ELVGLE--------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 143 eadirsilsGLG--FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAI 216
Cdd:COG3842 127 ---------GLAdrYP---HQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITF 189
|
....*..
gi 446524828 217 LIVSHDR 223
Cdd:COG3842 190 IYVTHDQ 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
344-514 |
5.17e-17 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 80.23 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSvGYYDQEQA--------------NLTSS 408
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIS-KLSEKELAafrrrhigfvfqsfNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 KRVLNELwdEYPLQ----PEKEIRTILGNFLFT---GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL- 480
Cdd:cd03255 97 LTALENV--ELPLLlagvPKKERRERAEELLERvglGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSe 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 481 NSKEILE--NALIDYPG-TLLFVSHDRYFINRVTTTV 514
Cdd:cd03255 175 TGKEVMEllRELNKEAGtTIVVVTHDPELAEYADRII 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
331-502 |
5.26e-17 |
|
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: 79.28 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSvgyydQEQANLTS 407
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdGVPVS-----DLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 408 SKRVLNElwdeyplQPekeirtilgnFLFTG---DDVLKPvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSK 483
Cdd:cd03247 76 LISVLNQ-------RP----------YLFDTtlrNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDpITER 135
|
170 180
....*....|....*....|
gi 446524828 484 EILENALIDYPG-TLLFVSH 502
Cdd:cd03247 136 QLLSLIFEVLKDkTLIWITH 155
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-222 |
5.60e-17 |
|
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: 79.99 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQN 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDEMltvfthlqQMETKLRRLEQEMGKEENFSNAatyeKLLaDYDQLqLDYKdqggyqyeadirsilsglg 154
Cdd:cd03301 81 YALYPHMTVYDNI--------AFGLKLRKVPKDEIDERVREVA----ELL-QIEHL-LDRK------------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 155 fpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:cd03301 128 ---------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
331-504 |
5.64e-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: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS--------VGYYDQE 401
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QAN---LTSSKRVLnelwdeYPLQ----PEKEIRTILGNFLF-TGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03259 81 YALfphLTVAENIA------FGLKlrgvPKAEIRARVRELLElVGLEGLlnRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 472 DEPTNHLDLNSKEILENALIDYPG----TLLFVSHDR 504
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-222 |
6.02e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.97 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGY 70
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLAdwspaelarrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETSLTIwdemltvfthlqqmetklrrlEQ--EMGKEENFSNAATYEKLLADYdqLQldykdqggyqyEADIrS 148
Cdd:PRK13548 81 LPQHSSLSFPFTV---------------------EEvvAMGRAPHGLSRAEDDALVAAA--LA-----------QVDL-A 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 149 ILSGLGFPvethqttisTLSGGQKTRLALGKLL--LTKPD----LLILDEPTNHLDI----ETLTWLEQYLQGYPGAILI 218
Cdd:PRK13548 126 HLAGRDYP---------QLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIV 196
|
....
gi 446524828 219 VSHD 222
Cdd:PRK13548 197 VLHD 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
331-503 |
7.83e-17 |
|
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: 79.82 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF------GSNVSVGYYDQ 400
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 eQANLTSSKRVLNELwdEYPLQ----PEKEIRTIlgnflftGDDVLKPV----------SSLSGGQKARLALAKLMMQKS 466
Cdd:cd03293 81 -QDALLPWLTVLDNV--ALGLElqgvPKAEARER-------AEELLELVglsgfenaypHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 467 NLLILDEPTNHLDLNSKEILENALID----YPGTLLFVSHD 503
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-510 |
8.24e-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: 83.70 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG--ELSHDGGEIIKpkDVSI----GYLAQNTGL 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIY--HVALcekcGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 78 ETSLTIWDEMLTVFthlqqmETKLRRLEQEMGKEENFSNAATYEKLLADY-DQLQLD----YKDQGGYQYEADIRSILSG 152
Cdd:TIGR03269 79 GEPCPVCGGTLEPE------EVDFWNLSDKLRRRIRKRIAIMLQRTFALYgDDTVLDnvleALEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 153 LGFPVETHQTT--ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETL----TWLEQYLQGYPGAILIVSHDRYFL 226
Cdd:TIGR03269 153 IEMVQLSHRIThiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 227 DKLVTQVYEISNKESRRfVGN----YSKYLDLKSALyEQEikRYEKQQDEIAKLEDFvqkniarastTKRAQSrrkqLDR 302
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKE-EGTpdevVAVFMEGVSEV-EKE--CEVEVGEPIIKVRNV----------SKRYIS----VDR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 303 melltrplgdsksasfhfDIEKQSGNDVLQVKDATIgydedpiiehvnmrltrgdsVALVGPNGIGKSTLLKSIVNKLQL 382
Cdd:TIGR03269 295 ------------------GVVKAVDNVSLEVKEGEI--------------------FGIVGTSGAGKTTLSKIIAGVLEP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 383 LHGDVafgsNVSVGyydQEQANLTS--------SKRVLNELWDEYPLQPEkeiRTILGNF-----LFTGDD--------V 441
Cdd:TIGR03269 337 TSGEV----NVRVG---DEWVDMTKpgpdgrgrAKRYIGILHQEYDLYPH---RTVLDNLteaigLELPDElarmkaviT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 442 LKPV---------------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR03269 407 LKMVgfdeekaeeildkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSH 486
|
....*...
gi 446524828 503 DRYFINRV 510
Cdd:TIGR03269 487 DMDFVLDV 494
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
326-503 |
9.12e-17 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 80.02 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 326 SGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVSvgyydqeqan 404
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 405 lTSSKRVLNE-------------LWD--------EYPLQ-----PEKEIRTI---------LGNFLFtgddvLKPvSSLS 449
Cdd:COG1127 71 -GLSEKELYElrrrigmlfqggaLFDsltvfenvAFPLRehtdlSEAEIRELvleklelvgLPGAAD-----KMP-SELS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 450 GGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEIleNALI-----DYPGTLLFVSHD 503
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITSAVI--DELIrelrdELGLTSVVVTHD 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-222 |
9.30e-17 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 80.02 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-------------I 68
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlVDGQDITglsekelyelrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 69 GYLAQNTGLETSLTIWDEM---LTVFTHLQqmETKLRRLeqemgkeenfsnaaTYEKL----LADYDQLqldykdqggyq 141
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVafpLREHTDLS--EAEIREL--------------VLEKLelvgLPGAADK----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 142 yeadirsilsglgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----------IETLTwleqylQG 211
Cdd:COG1127 138 -------------MPSE--------LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavidelIRELR------DE 190
|
250
....*....|.
gi 446524828 212 YPGAILIVSHD 222
Cdd:COG1127 191 LGLTSVVVTHD 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-238 |
9.42e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 9.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQvnGLSKLYGAE-TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV---- 66
Cdd:COG2884 1 MIRFE--NVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrLKRREIpylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 67 -SIGYLAQNTGLETSLTIWDemltvfthlqqmetklrrleqemgkeenfsNAAtyeklLAdydqLQLDYKDQGgyQYEAD 145
Cdd:COG2884 79 rRIGVVFQDFRLLPDRTVYE------------------------------NVA-----LP----LRVTGKSRK--EIRRR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 146 IRSILS--GLG-----FPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ-----Gyp 213
Cdd:COG2884 118 VREVLDlvGLSdkakaLPHE--------LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEeinrrG-- 187
|
250 260
....*....|....*....|....*
gi 446524828 214 GAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:COG2884 188 TTVLIATHDLELVDRMPKRVLELED 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-517 |
1.24e-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: 79.85 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGY----DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSVGYYDQEQANL 405
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 -------TSS-------KRVLNE-LWDEYPLQPEKEIRTILgnflftgDDV-LKP------VSSLSGGQKARLALAKLMM 463
Cdd:COG1124 82 qmvfqdpYASlhprhtvDRILAEpLRIHGLPDREERIAELL-------EQVgLPPsfldryPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 464 QKSNLLILDEPTNHLDL-NSKEILeNALIDYPG----TLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG1124 155 LEPELLLLDEPTSALDVsVQAEIL-NLLKDLREerglTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-508 |
1.25e-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: 83.30 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 32 IALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvsigylaqntgletsltiWDEMLTVF--THLQQMETKLRrlEQEMG 109
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPS------------------WDEVLKRFrgTELQDYFKKLA--NGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 110 ---KEENFSNAATYEK-----LLADYDQL-QLDYkdqggYQYEADIRSILSglgfpvethqTTISTLSGGQKTRLALGKL 180
Cdd:COG1245 162 vahKPQYVDLIPKVFKgtvreLLEKVDERgKLDE-----LAEKLGLENILD----------RDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 181 LLTKPDLLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVY----------EISNKESRRfVG- 246
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHilygepgvygVVSKPKSVR-VGi 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 247 -NYskyldLKSALYEQEIK-RyekqQDEIakleDFvqkniarasttkRAQSRRKQLDRMELLTRPlgdsksasfhfDIEK 324
Cdd:COG1245 306 nQY-----LDGYLPEENVRiR----DEPI----EF------------EVHAPRREKEEETLVEYP-----------DLTK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNDVLQVKDATIgydedpiiehvnmrlTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSvgYYDQeqan 404
Cdd:COG1245 350 SYGGFSLEVEGGEI---------------REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIS--YKPQ---- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 405 ltsskrvlnELWDEYPLQPEKEIRTILGNFLFTG---DDVLKP----------VSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:COG1245 409 ---------YISPDYDGTVEEFLRSANTDDFGSSyykTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYLL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446524828 472 DEPTNHLDLNS--------KEILENalidYPGTLLFVSHDRYFIN 508
Cdd:COG1245 480 DEPSAHLDVEQrlavakaiRRFAEN----RGKTAMVVDHDIYLID 520
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-198 |
1.29e-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: 78.86 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KPKDVS----IGYLAQNTG 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgKPLDIAarnrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 77 LETSLTIWDEMLtvftHLQQMetklrrleQEMGKEENFSNAATY-EKL-LADYdqlqldykdqggyqyeADIRsilsglg 154
Cdd:cd03269 81 LYPKMKVIDQLV----YLAQL--------KGLKKEEARRRIDEWlERLeLSEY----------------ANKR------- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 155 fpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03269 126 ---------VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
577-642 |
1.36e-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: 1.36e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 577 LERQRTRKIEELEQNIVSLEEEIATLEDQLCLPEIYADYEKASEITTKKQTLQEQLEACMAEWEEL 642
Cdd:pfam16326 2 LSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDYEKLQELSAELEELEAELEELYERWEEL 67
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
1.81e-16 |
|
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: 79.36 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELsH--DGGEI--------------IKPK 64
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL-PptYGNDVrlfgerrggedvweLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 65 dvsIGY----LAQNtgLETSLTIWDEMLTVFthlqqmetklrrleqemgkeenFSNAATYEKlladYDQLQldykdqggy 140
Cdd:COG1119 80 ---IGLvspaLQLR--FPRDETVLDVVLSGF----------------------FDSIGLYRE----PTDEQ--------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 141 qyEADIRSILSGLGFpveTH--QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPG 214
Cdd:COG1119 120 --RERARELLELLGL---AHlaDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAP 194
|
....*..
gi 446524828 215 AILIVSH 221
Cdd:COG1119 195 TLVLVTH 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
328-503 |
2.04e-16 |
|
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: 82.64 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvnkLQLLHGDVAFGSNVSVGYYDQEQANL 405
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL---MGLLPHGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 T-SSKRV----------LNelwdeyPLQPEKEIRTILGNFLFTGDDVLKPVSS-----------------LSGGQKARLA 457
Cdd:COG1123 79 AlRGRRIgmvfqdpmtqLN------PVTVGDQIAEALENLGLSRAEARARVLElleavglerrldryphqLSGGQRQRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 458 LAKLMMQKSNLLILDEPTNHLD-LNSKEILE--NALIDYPG-TLLFVSHD 503
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDvTTQAEILDllRELQRERGtTVLLITHD 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
331-503 |
2.10e-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: 78.76 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQLLH------GDVAF-GSNVSVGYYD---- 399
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIpgapdeGEVLLdGKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 --------QE--------QANLTSSKRVLNELWDEyplQPEKEIRTILGNFLFTG--DDVLKPvSSLSGGQKARLALAKL 461
Cdd:cd03260 80 rrrvgmvfQKpnpfpgsiYDNVAYGLRLHGIKLKE---ELDERVEEALRKAALWDevKDRLHA-LGLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524828 462 MMQKSNLLILDEPTNHLDLNSKEILENALI----DYpgTLLFVSHD 503
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAelkkEY--TIVIVTHN 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
331-490 |
2.60e-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: 77.89 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED-----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSnvSVGYYDQEQanl 405
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 tsskrvlnelWdeypLQPEkeirTILGNFLFtG--------DDVLKPVS---------------------SLSGGQKARL 456
Cdd:cd03250 76 ----------W----IQNG----TIRENILF-GkpfdeeryEKVIKACAlepdleilpdgdlteigekgiNLSGGQKQRI 136
|
170 180 190
....*....|....*....|....*....|....*
gi 446524828 457 ALAKLMMQKSNLLILDEPTNHLDLN-SKEILENAL 490
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCI 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
331-502 |
2.60e-16 |
|
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: 78.03 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSVGYYDQEQA------ 403
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIgaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 -----NLTSSKRVlnELWDEYPLQPEKEIRTILGNFLFTGDDVLKpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:cd03268 81 pgfypNLTARENL--RLLARLLGIRKKRIDEVLDVVGLKDSAKKK-VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180
....*....|....*....|....*..
gi 446524828 479 D-LNSKEILE--NALIDYPGTLLFVSH 502
Cdd:cd03268 158 DpDGIKELREliLSLRDQGITVLISSH 184
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-222 |
3.47e-16 |
|
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: 78.54 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQN 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDemlTVFTHLQQMETKLRRLEQEMgkeenfsnAATYEKLLadyDQLQLDykdqggyqyeadirsilsGLG 154
Cdd:cd03296 83 YALFRHMTVFD---NVAFGLRVKPRSERPPEAEI--------RAKVHELL---KLVQLD------------------WLA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 155 --FPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:cd03296 131 drYPAQ--------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-508 |
3.63e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 32 IALVGRNGAGKSTLLKIIAGELshdggeiiKPkdvsigylaqNTGLETSLTIWDEMLTVF--THLQQMETKLRrleqemg 109
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGEL--------IP----------NLGDYEEEPSWDEVLKRFrgTELQNYFKKLY------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 110 keENFSNAA---------------TYEKLLADYDQL-QLDYkdqggYQYEADIRSILSglgfpvethqTTISTLSGGQKT 173
Cdd:PRK13409 157 --NGEIKVVhkpqyvdlipkvfkgKVRELLKKVDERgKLDE-----VVERLGLENILD----------RDISELSGGELQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 174 RLALGKLLLTKPDLLILDEPTNHLDI-ETLT---WLEQYLQGYPgaILIVSHDRYFLDKLVTQV---------YEI--SN 238
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLDIrQRLNvarLIRELAEGKY--VLVVEHDLAVLDYLADNVhiaygepgaYGVvsKP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 239 KESRRFVGNYskyldLKSALYEQEIK-RyekqQDEIakledfvqkniaraSTTKRAQSRRKQLDRmeLLTRPlgdsksas 317
Cdd:PRK13409 298 KGVRVGINEY-----LKGYLPEENMRiR----PEPI--------------EFEERPPRDESERET--LVEYP-------- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 318 fhfDIEKQSGNDVLQVKDATIgydedpiiehvnmrlTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVafGSNVSVGY 397
Cdd:PRK13409 345 ---DLTKKLGDFSLEVEGGEI---------------YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 398 ---Y---DQE---QANLTSSKRVLNE--LWDEY--PLQPEKeirtilgnfLFTgddvlKPVSSLSGGQKARLALAKLMMQ 464
Cdd:PRK13409 405 kpqYikpDYDgtvEDLLRSITDDLGSsyYKSEIikPLQLER---------LLD-----KNVKDLSGGELQRVAIAACLSR 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 465 KSNLLILDEPTNHLDLNS--------KEILENAlidyPGTLLFVSHDRYFIN 508
Cdd:PRK13409 471 DADLYLLDEPSAHLDVEQrlavakaiRRIAEER----EATALVVDHDIYMID 518
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
310-502 |
3.70e-16 |
|
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: 82.09 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 310 LGDSKSASFHFDIEKQSGNDVLQVKDATIGYD-EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVa 388
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 389 fgsnvSVGYYDQEQANLTSSKRVLNELwdeyPLQPEKEIRTILGNFLF------TGDDVLKPV----------------- 445
Cdd:TIGR01193 532 -----LLNGFSLKDIDRHTLRQFINYL----PQEPYIFSGSILENLLLgakenvSQDEIWAACeiaeikddienmplgyq 602
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 446 -------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR01193 603 telseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-233 |
4.42e-16 |
|
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: 81.84 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDVS--IGYLAQNTGLetsltiwdem 87
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLlglyqptEGSVLLDGVDIrqIDPADLRrnIGYVPQDPRL---------- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 88 ltvFThlqqmeTKLRrleqemgkeENFsnaaTYEKLLADyDQLQLDYKDQGGYqyEADIRSILSGLGFPV-ETHQTtist 166
Cdd:TIGR03375 551 ---FY------GTLR---------DNI----ALGAPYAD-DEEILRAAELAGV--TEFVRRHPDGLDMQIgERGRS---- 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHDRYFLDkLVTQV 233
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSLLD-LVDRI 669
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
331-475 |
5.87e-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: 77.47 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS-----------VGYY 398
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQ---ANLTsskrVL-NELWDEYPLQPEKEIRTI---LGNFlftgdDVLK-----PVSSLSGGQKARLALAKLMMQKS 466
Cdd:cd03224 81 PEGRrifPELT----VEeNLLLGAYARRRAKRKARLervYELF-----PRLKerrkqLAGTLSGGEQQMLAIARALMSRP 151
|
....*....
gi 446524828 467 NLLILDEPT 475
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-198 |
5.89e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.73 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSIGYL 71
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtdLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLetsltiWDEMlTVFthlQQMET--KLRRL-EQEMGK--EEnfsnAAtyEKL-LADYdqlqLDYKdqggyqyead 145
Cdd:COG3839 81 FQSYAL------YPHM-TVY---ENIAFplKLRKVpKAEIDRrvRE----AA--ELLgLEDL----LDRK---------- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 146 irsilsglgfPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG3839 131 ----------P--------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
337-534 |
6.24e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 81.09 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 337 TIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANLtSSKRVLN--- 413
Cdd:PRK15064 8 TMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAF-EEFTVLDtvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 414 ----ELWdeyplQPEKEIRTILGNFLFTGDDVLK------------------------------------PVSSLSGGQK 453
Cdd:PRK15064 87 mghtELW-----EVKQERDRIYALPEMSEEDGMKvadlevkfaemdgytaearagelllgvgipeeqhygLMSEVAPGWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYV 533
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM 241
|
.
gi 446524828 534 E 534
Cdd:PRK15064 242 T 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-198 |
6.50e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.20 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS---------- 67
Cdd:COG1101 2 LELKNLSKTFNPGTvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKDVTklpeykraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 IGYLAQNTGLET--SLTIwdemltvfthLQQMETKLRRleqemGKEENFSNAATYEKlladydqlqldykdqggyqyEAD 145
Cdd:COG1101 82 IGRVFQDPMMGTapSMTI----------EENLALAYRR-----GKRRGLRRGLTKKR--------------------REL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 146 IRSILSGLGFPVETHQTT-ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG1101 127 FRELLATLGLGLENRLDTkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-222 |
9.21e-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: 79.00 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 22 IKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQntglETSLtiwde 86
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQ----EARL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 87 mltvFTHLQQMETKLRRLEQEMGKEENFSNAATYEKLladydqlqldykdqggyqyeadirsilsGLGFPVethQTTIST 166
Cdd:TIGR02142 87 ----FPHLSVRGNLRYGMKRARPSERRISFERVIELL----------------------------GIGHLL---GRLPGR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHS 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
331-490 |
9.77e-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: 75.99 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF---------GSNVSVGYYDQE 401
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfqrDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QANLTSSKRVLNELWDEYPLQPEKEIRTILGNFLFTG-DDVlkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGfEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 446524828 481 NSKEILENAL 490
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-198 |
1.04e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQtKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVS-IGYLAQNT 75
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVP-KGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgepLDPEDRRrIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 76 GLETSLTIWDEmLTVFTHLQQMETK--LRRLeqemgkeenfsnaatyEKLLadyDQLQL-DYKDQggyqyeadirsilsg 152
Cdd:COG4152 81 GLYPKMKVGEQ-LVYLARLKGLSKAeaKRRA----------------DEWL---ERLGLgDRANK--------------- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524828 153 lgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG4152 126 ----------KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-221 |
1.21e-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: 75.99 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigyLAQNTGLETSLTI 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----------LLNGGPLDFQRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVFTHLQQMETKLRRLEqemgkeenfsNAATYEKLLADYDQLQ-LDYKDQGGYQYEAdirsilsglgfpvethqt 162
Cdd:cd03231 71 IARGLLYLGHAPGIKTTLSVLE----------NLRFWHADHSDEQVEEaLARVGLNGFEDRP------------------ 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 163 tISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP---GAILIVSH 221
Cdd:cd03231 123 -VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-194 |
1.45e-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: 76.41 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----------IGYL 71
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrLDGEDITklppheraragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIWDEMLTVFThlqqmetKLRRLEQEMGKEenfsnaatyekLLADYDQLQldykdqggyqyeaDIRSILS 151
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLA-------ALPRRSRKIPDE-----------IYELFPVLK-------------EMLGRRG 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524828 152 GLgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:TIGR03410 130 GD-------------LSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
331-515 |
1.61e-15 |
|
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: 75.64 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLQLLHGDVAFGsnvsvgyyDQEQANLTSS 408
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK--------GEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 KRVLNEL---WdEYPLqpekEIRTIlgnflfTGDDVLKPVS-SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKE 484
Cdd:cd03217 73 ERARLGIflaF-QYPP----EIPGV------KNADFLRYVNeGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190
....*....|....*....|....*....|....
gi 446524828 485 ILENA---LIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:cd03217 142 LVAEVinkLREEGKSVLIITHYQRLLDYIKPDRV 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-200 |
1.97e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.21 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI---IKPKDVSIGYLAQ 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLE-TSLTIWDEMlTVFTHLQQMETKLRRLEQEMGKEENfsnaatyEKLLAdydQLQL-DYKDQggyqyeadirsils 151
Cdd:PRK11124 83 NVGMVfQQYNLWPHL-TVQQNLIEAPCRVLGLSKDQALARA-------EKLLE---RLRLkPYADR-------------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 152 glgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK11124 138 ---FPLH--------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-210 |
2.19e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.44 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDV--SIGYLAQNTGLeTSLT 82
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTLESLrrQIGVVPQDTFL-FSGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWDEMLtvfthlqqmetklrrleqeMGKEEnfsnaATYEKLLADYDQLQLDykdqggyqyeADIRSILSGLgfpvethQT 162
Cdd:COG1132 430 IRENIR-------------------YGRPD-----ATDEEVEEAAKAAQAH----------EFIEALPDGY-------DT 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 163 TI----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQ 210
Cdd:COG1132 469 VVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET----EALIQ 516
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-511 |
2.24e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQLLHGDVA-------FGSNVSvgyydQEQA 403
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRvegrvefFNQNIY-----ERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 NLTSSKRVLNELWDE---YPL---------------QPEKEIRTILGNFLFTGD-------DVLKPVSSLSGGQKARLAL 458
Cdd:PRK14258 82 NLNRLRRQVSMVHPKpnlFPMsvydnvaygvkivgwRPKLEIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 459 AKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPGTLLFVSHDRYFINRVT 511
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
331-518 |
2.43e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGdvafgsNVSVGYYDQEQANLTSSKR 410
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAG------TVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQPEKEIRTI--------LGNFLFTGDD-----------------VLKPVSSLSGGQKARLALAKLMMQK 465
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVvemgrtphRSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 466 SNLLILDEPTNHLDLNSK-EILENA--LIDYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQvRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-201 |
2.77e-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: 75.84 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGaETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQN 74
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDEMLTVFTHLQQMETKLRRLEQEMGKEENFSNAatyeklladydqlqLDYKDQggyqyeadirsilsglg 154
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHL--------------LNRKPE----------------- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524828 155 fpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03299 129 -----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-201 |
4.58e-15 |
|
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: 75.30 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIKPKDVS-------I 68
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLnglveptSGSVLIDGTDINKLKGKAlrqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 69 GYLAQNTGLETSLTIWDEMLTVFthLQQMETkLRRLEQEMGKEEnfsnaatYEKLLADYDQLQLDykdqggyqyeadirs 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGR--LGRRST-WRSLFGLFPKEE-------KQRALAALERVGLL--------------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 149 ilsglgfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03256 136 ---------DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPAS 179
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
330-487 |
5.98e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.09 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS------------- 394
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdGQDVTalrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYYDQeQANLTSSKRVL-NEL---------WdeyplqpekeiRTILGnfLFTGDDV----------------LKPVSSL 448
Cdd:COG3638 82 IGMIFQ-QFNLVPRLSVLtNVLagrlgrtstW-----------RSLLG--LFPPEDReralealervgladkaYQRADQL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 449 SGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE 487
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDpKTARQVMD 187
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-200 |
1.24e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.87 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLAQNTG 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 77 letsltiwdeMltVFthlQQ-------------ME--TKLRRleqeMGKEENFSNAatyEKLLadyDQLQL-DYKDQggy 140
Cdd:COG1126 81 ----------M--VF---QQfnlfphltvlenvTLapIKVKK----MSKAEAEERA---MELL---ERVGLaDKADA--- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 141 qyeadirsilsglgFPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:COG1126 133 --------------YP--------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-503 |
1.32e-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: 73.10 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 354 TRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVsvgYYDQEQA-NLTSSKRVLNELWDEYPLQP--------- 423
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKiNLPPQQRKIGLVFQQYALFPhlnvrenla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 424 ---------EKEIRT--ILGnfLFTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL- 490
Cdd:cd03297 98 fglkrkrnrEDRISVdeLLD--LLGLDHLLNrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELk 175
|
170
....*....|....*.
gi 446524828 491 ---IDYPGTLLFVSHD 503
Cdd:cd03297 176 qikKNLNIPVIFVTHD 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-201 |
1.41e-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: 72.95 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGYLAQNTGLETSLTI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII------IDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVFTH---------LQQMETKLRRLeQEMGKEEnfsnA-ATYEKLLadyDQLQLDYKdqggyqyeADirsilsgl 153
Cdd:cd03262 75 RQKVGMVFQQfnlfphltvLENITLAPIKV-KGMSKAE----AeERALELL---EKVGLADK--------AD-------- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 154 GFPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03262 131 AYP--------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
331-515 |
1.42e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 76.94 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI------------VNKLQLLHGDVAF-------- 389
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlgfvdptegsiaVNGVPLADADADSwrdqiawv 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 390 --------GS---NVSVGYYDQEQANLT-SSKRV-LNELWDEYPLQPEKEIrtilgnflftGDDVlkpvSSLSGGQKARL 456
Cdd:TIGR02857 402 pqhpflfaGTiaeNIRLARPDASDAEIReALERAgLDEFVAALPQGLDTPI----------GEGG----AGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 457 ALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVV 515
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAALADRIVV 528
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-239 |
1.58e-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: 71.80 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLeTSLTiwdemltvfthlqq 96
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGT-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 97 metkLRrleqemgkeenfsnaatyeklladyDQLQLDYKDqggyqyeadirsilsglgfpvethqttisTLSGGQKTRLA 176
Cdd:cd03223 80 ----LR-------------------------EQLIYPWDD-----------------------------VLSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 177 LGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYpGAILI-VSHdRYFLDKLVTQVYEISNK 239
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL-GITVIsVGH-RPSLWKFHDRVLDLDGE 163
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-201 |
1.65e-14 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 73.55 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDV-----S 67
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtalRGRALrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 IGYLAQNTGLetsltIwdEMLTVFT-----HLQQMETkLRRLEQEMGKEEnfsnaatYEKLLADYDQLQLDYKdqggyqy 142
Cdd:COG3638 82 IGMIFQQFNL-----V--PRLSVLTnvlagRLGRTST-WRSLLGLFPPED-------RERALEALERVGLADK------- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 143 eADIRSilsglgfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG3638 140 -AYQRA----------------DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKT 181
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-200 |
1.66e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI---IKPKDVSIGYLAQ 73
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLE-TSLTIWDEmLTVFTHLqqMETKLRRLEqeMGKEENFSNAatyEKLLAdydQLQL-DYKDQggyqyeadirsils 151
Cdd:COG4161 83 KVGMVfQQYNLWPH-LTVMENL--IEAPCKVLG--LSKEQAREKA---MKLLA---RLRLtDKADR-------------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 152 glgFPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:COG4161 138 ---FPLH--------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
330-517 |
1.85e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDED-PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVS------------- 394
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvNGQDLSrlkrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYYDQEQanltsskRVLNEL--WD--EYPLQ----PEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARL 456
Cdd:COG2884 81 IGVVFQDF-------RLLPDRtvYEnvALPLRvtgkSRKEIRRRV-------REVLdlvglsdkakALPHELSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 457 ALAKLMMQKSNLLILDEPTNHLD-LNSKEILE-----NALidypG-TLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDpETSWEIMElleeiNRR----GtTVLIATHDLELVDRMPKRVLEL 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-221 |
2.26e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIA-------GELSHDGGEIIKPKDV-SIGYLAQNT 75
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAgllppaaGTIKLDGGDIDDPDVAeACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 76 GLETSLTIwdemltvfthlqqmetklrrleqemgkEENfsnaatyeklladydqLQL--DYKDQGgyqyEADIRSILSGL 153
Cdd:PRK13539 83 AMKPALTV---------------------------AEN----------------LEFwaAFLGGE----ELDIAAALEAV 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 154 GFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSH 221
Cdd:PRK13539 116 GLAPLAH-LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
2.38e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.23 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSI--GYL 71
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplaaWSPWELARrrAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIWDemlTVfthlqqmetklrrleqEMGKEENFSNAATYEKLLADYdqLQLdykdqggyqyeADirsiLS 151
Cdd:COG4559 81 PQHSSLAFPFTVEE---VV----------------ALGRAPHGSSAAQDRQIVREA--LAL-----------VG----LA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 GLGfpvethQTTISTLSGGQKTRLALGKLLL-------TKPDLLILDEPTNHLDI----ETLTWLEQYLQGyPGAILIVS 220
Cdd:COG4559 125 HLA------GRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQLARR-GGGVVAVL 197
|
..
gi 446524828 221 HD 222
Cdd:COG4559 198 HD 199
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
340-503 |
2.65e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 72.75 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 340 YDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSvgyYDQEQANLTSSKRVL---NELW 416
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVP---WKRRKKFLRRIGVVFgqkTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 417 -------------DEYPLQPEKEIRTI--LGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:cd03267 108 wdlpvidsfyllaAIYDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180
....*....|....*....|....*.
gi 446524828 482 SKEILENALIDY----PGTLLFVSHD 503
Cdd:cd03267 188 AQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-222 |
3.09e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.48 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANikLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-------------KPkdVSIgy 70
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltalppaeRP--VSM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETSLTIWDEM---------LTVFTHlQQMETKLRRleqeMGkeenfsnaatyeklLADYdqlqLDYKdqggyq 141
Cdd:COG3840 76 LFQENNLFPHLTVAQNIglglrpglkLTAEQR-AQVEQALER----VG--------------LAGL----LDRL------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 142 yeadirsilsglgfPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAIL 217
Cdd:COG3840 127 --------------P--------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVL 184
|
....*
gi 446524828 218 IVSHD 222
Cdd:COG3840 185 MVTHD 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-222 |
3.17e-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: 72.72 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 9 LSKLYGA-ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDV----------SIGYLAQNTG 76
Cdd:cd03295 6 VTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfIDGEDIreqdpvelrrKIGYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 77 LETSLTIWDEMLTVFTHLQQMETKLRRLEQEmgkeenfsnaatyekLLADYDQLQLDYKDQggYQYEadirsilsglgfp 156
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWPKEKIRERADE---------------LLALVGLDPAEFADR--YPHE------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 157 vethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ---YLQGYPG-AILIVSHD 222
Cdd:cd03295 136 ----------LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGkTIVFVTHD 195
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
3.50e-14 |
|
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: 72.21 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikPKDVSIGYLAQNtgletsltI 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLDGKD--------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVfthlqqmeTKLRRleqEMGKEenFSNAATYEKLLadYDQLQLDYKDQG---GYQYEADIRSILSGLGFPVETH 160
Cdd:cd03260 70 YDLDVDV--------LELRR---RVGMV--FQKPNPFPGSI--YDNVAYGLRLHGiklKEELDERVEEALRKAALWDEVK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 161 -QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD------IETLtwLEQYLQGYpgAILIVSHD 222
Cdd:cd03260 135 dRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpistakIEEL--IAELKKEY--TIVIVTHN 199
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-192 |
3.70e-14 |
|
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: 72.18 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSiGYLAQNTGLETSLTiwdemltvfthlqq 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-SLLGLGGGFNPELT-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 97 metklrrleqemGKEENFSNAATYEKLLADYDqlqldykdqggyQYEADIRSiLSGLGFPVETHqttISTLSGGQKTRLA 176
Cdd:cd03220 101 ------------GRENIYLNGRLLGLSRKEID------------EKIDEIIE-FSELGDFIDLP---VKTYSSGMKARLA 152
|
170
....*....|....*.
gi 446524828 177 LGKLLLTKPDLLILDE 192
Cdd:cd03220 153 FAIATALEPDILLIDE 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
4.38e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAetILAN--IKLEVQtKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------- 67
Cdd:COG3845 5 ALELRGITKRFGG--VVANddVSLTVR-PGEIhALLGENGAGKSTLMKILYGLYQPDSGEIlIDGKPVRirsprdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 IGYLAQNTGLETSLTIWDEMLtvfthlqqmetklrrleqeMGKEENFSnaatyeklladydqLQLDYKdqggyQYEADIR 147
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIV-------------------LGLEPTKG--------------GRLDRK-----AARARIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 148 SILSGLGFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD-------IETLTWLEQylQGYpgAILIVS 220
Cdd:COG3845 124 ELSERYGLDVDPD-AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRLAA--EGK--SIIFIT 198
|
.
gi 446524828 221 H 221
Cdd:COG3845 199 H 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
337-522 |
4.52e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 337 TIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVafgsnvsvgYYDQEQANLTSSKRV----- 411
Cdd:PRK10253 14 TLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDGEHIQHYASKEVarrig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 412 -------------LNEL--WDEYPLQP------EKEIRTILGNFLFTG--DDVLKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK10253 85 llaqnattpgditVQELvaRGRYPHQPlftrwrKEDEEAVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 469 LILDEPTNHLDLNSK----EILENALIDYPGTLLFVSHD-----RYFINRVTTTVVELSTEGA 522
Cdd:PRK10253 165 MLLDEPTTWLDISHQidllELLSELNREKGYTLAAVLHDlnqacRYASHLIALREGKIVAQGA 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
4.98e-14 |
|
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: 70.42 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYG--AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigYLaqntgletsl 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TL---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 tiwdemltvfthlqqmetklrrleqemgkeeNFSNAATYEKLLADYdqlqLDYKDQGGYQYEAdirSILSGLGFPvethq 161
Cdd:cd03247 62 -------------------------------DGVPVSDLEKALSSL----ISVLNQRPYLFDT---TLRNNLGRR----- 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 162 ttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET-LTWLEQYLQGYPG-AILIVSH 221
Cdd:cd03247 99 -----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITH 155
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-193 |
5.30e-14 |
|
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: 71.81 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----------IGYL 71
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlLDGQDITklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIWDEMLTVF-THLQQMETKLRRLEQemgkeenfsnaatyekLLADYdqlqldykdqggyqyeaDIRSIL 150
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLeIRGLSKKEREEKLEE----------------LLEEF-----------------HITHLR 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524828 151 SGLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEP 193
Cdd:cd03218 128 KSKA----------SSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
331-515 |
5.78e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 71.47 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPI--IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS----------VGY 397
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 398 YDQE--------QANLTSSKRVLNelwDEYPLqpekEIRTILGNFLFTGDD-------VLKPVSSLSGGQKARLALAKLM 462
Cdd:cd03245 83 VPQDvtlfygtlRDNITLGAPLAD---DERIL----RAAELAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 463 MQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVV 515
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVDRIIV 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
329-479 |
8.47e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 329 DVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNklQLLHGDVAFGSNVSVGYYDQEQAnltss 408
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCVDVPDNQFGREAS----- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 409 krVLNELWDEYPLQPEKEIRTILG---NFLFtgddvLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:COG2401 102 --LIDAIGRKGDFKDAVELLNAVGlsdAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4-222 |
9.31e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSklygAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSI----------GYLAQ 73
Cdd:PRK03695 1 MQLNDVA----VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAwsaaelarhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIWdEMLTVF----THLQQMETKLRRLEQemgkeenfsnaatyeklladydQLQLDYKdqggyqyeadirsi 149
Cdd:PRK03695 77 QQTPPFAMPVF-QYLTLHqpdkTRTEAVASALNEVAE----------------------ALGLDDK-------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 150 lsgLGFPvethqttISTLSGG--QKTRLAlGKLLLTKPD------LLILDEPTNHLDIETLTWLEQYL-----QGypGAI 216
Cdd:PRK03695 120 ---LGRS-------VNQLSGGewQRVRLA-AVVLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLselcqQG--IAV 186
|
....*.
gi 446524828 217 LIVSHD 222
Cdd:PRK03695 187 VMSSHD 192
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
9.35e-14 |
|
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: 69.55 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYG--AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGY 70
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrLDGADISqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNtgletsltiwdemltvfthlqqmetklrrleqemgkeenfsnaatyeklladyDQLqldykdqggyqyeadirsiL 150
Cdd:cd03246 81 LPQD-----------------------------------------------------DEL-------------------F 88
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 151 SGlgfpvethqtTIS--TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSH 221
Cdd:cd03246 89 SG----------SIAenILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAH 154
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-222 |
1.08e-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: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHdGGEII---KP-KDVSI-------GYLAQNTgleTSLTiwdeM 87
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILlngRPlSDWSAaelarhrAYLSQQQ---SPPF----A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 88 LTVFTHLQqmetklrrLEQEMGkeenfSNAATYEKLLADY-DQLQLDYKdqggyqyeadirsilsgLGFPVethqttiST 166
Cdd:COG4138 84 MPVFQYLA--------LHQPAG-----ASSEAVEQLLAQLaEALGLEDK-----------------LSRPL-------TQ 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 167 LSGG--QKTRLAlGKLLLTKPD------LLILDEPTNHLDIE----TLTWLEQY-LQGypGAILIVSHD 222
Cdd:COG4138 127 LSGGewQRVRLA-AVLLQVWPTinpegqLLLLDEPMNSLDVAqqaaLDRLLRELcQQG--ITVVMSSHD 192
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
331-475 |
1.24e-13 |
|
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: 70.63 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS-----------VGYY 398
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLdGEDITklppheraragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQ---ANLT--------------SSKRVLNELWDEYPLQpeKEIRTILGnflftGDdvlkpvssLSGGQKARLALAKL 461
Cdd:TIGR03410 81 PQGReifPRLTveenlltglaalprRSRKIPDEIYELFPVL--KEMLGRRG-----GD--------LSGGQQQQLAIARA 145
|
170
....*....|....
gi 446524828 462 MMQKSNLLILDEPT 475
Cdd:TIGR03410 146 LVTRPKLLLLDEPT 159
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-222 |
1.29e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTiwdemLTVfthlqqmeTKLRRLEQEMGKeenfsnaatyeklladydqlqldykdqggyqyeADIRSILSGLGfPVETH 160
Cdd:PRK09544 82 LP-----LTV--------NRFLRLRPGTKK---------------------------------EDILPALKRVQ-AGHLI 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWL----EQYLQGYPGAILIVSHD 222
Cdd:PRK09544 115 DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-198 |
1.41e-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: 69.50 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELS--HDGGEI------IKPKDV--SIGYLAQNTGLETSLTI 83
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVlingrpLDKRSFrkIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WdEMLtvfthlqqmetklrrleqemgkeenfsnaatyeklladydqlqldykdqggyQYEADIRSIlsglgfpvethqtt 163
Cdd:cd03213 100 R-ETL----------------------------------------------------MFAAKLRGL-------------- 112
|
170 180 190
....*....|....*....|....*....|....*
gi 446524828 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 |
1.42e-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: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SIGYLAQ 73
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrEPREVrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIWDEMLTvfthlqqmetklrrleqeMGKEENFSNAATYEKL--LADYDQLqLDYKDQggyqyeadirsils 151
Cdd:cd03265 81 DLSVDDELTGWENLYI------------------HARLYGVPGAERRERIdeLLDFVGL-LEAADR-------------- 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 152 glgfpvethqtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ 210
Cdd:cd03265 128 -----------LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
330-475 |
1.48e-13 |
|
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: 70.40 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS-----------VGY 397
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 398 YDQEQ---ANLT----------------SSKRVLNELWDEYP-LqpeKEIRTILGNflftgddvlkpvsSLSGGQKARLA 457
Cdd:COG0410 83 VPEGRrifPSLTveenlllgayarrdraEVRADLERVYELFPrL---KERRRQRAG-------------TLSGGEQQMLA 146
|
170
....*....|....*...
gi 446524828 458 LAKLMMQKSNLLILDEPT 475
Cdd:COG0410 147 IGRALMSRPKLLLLDEPS 164
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
344-502 |
1.56e-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: 73.54 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDV-------------AFGSnvSVGYYDQeQANLTSSKR 410
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkqwdreTFGK--HIGYLPQ-DVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQPEKEIRT---------ILGnfLFTG-DDVLKPV-SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:TIGR01842 409 AENIARFGENADPEKIIEAaklagvhelILR--LPDGyDTVIGPGgATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180
....*....|....*....|....*.
gi 446524828 480 LNSKEILENALIDYP---GTLLFVSH 502
Cdd:TIGR01842 487 EEGEQALANAIKALKargITVVVITH 512
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
330-503 |
1.93e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVA-FGSNVSvGYYDQEQA----- 403
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlNGRPLA-DWSPAELArrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 -----NLTSSKRVlnelwDE------YPL-QPEKEIRTILgnflftgDDVL----------KPVSSLSGGQKARLALAKL 461
Cdd:PRK13548 81 lpqhsSLSFPFTV-----EEvvamgrAPHgLSRAEDDALV-------AAALaqvdlahlagRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 462 MMQKSN------LLILDEPTNHLDL----NSKEILENALIDYPGTLLFVSHD 503
Cdd:PRK13548 149 LAQLWEpdgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-201 |
2.37e-13 |
|
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: 70.02 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYG-AETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDV-----S 67
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCInrlvepsSGSILLEGTDItkLRGKKLrklrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 IGYLAQNTGLETSLTIWDEMLTVFthLQQMETkLRRLEQEMGKEEnfsnaatYEKLLADYDQLQLDYKdqggyqyeADIR 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGR--LGYKPT-WRSLLGRFSEED-------KERALSALERVGLADK--------AYQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 148 SilsglgfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:TIGR02315 143 A----------------DQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
331-504 |
2.39e-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: 71.67 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKR 410
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD--------GRDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLN------ELWD--------EYPLQ----PEKEIRTI---------LGNFlftGDdvlKPVSSLSGGQKARLALAKLMM 463
Cdd:COG3842 78 NVGmvfqdyALFPhltvaenvAFGLRmrgvPKAEIRARvaellelvgLEGL---AD---RYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524828 464 QKSNLLILDEPTNHLDLNSKEILENALIDY----PGTLLFVSHDR 504
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQ 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-222 |
3.10e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNTGLetslt 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRDGQL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 iwdemltvfTHLQQM-ETKLRRL--------EQ--EMGKEENFSNAATY-EKLLAdydqlqldykdQGGYQYeADIRSIL 150
Cdd:PRK11701 73 ---------RDLYALsEAERRRLlrtewgfvHQhpRDGLRMQVSAGGNIgERLMA-----------VGARHY-GDIRATA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 SGLGFPVETHQTTI----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG----AILIVSHD 222
Cdd:PRK11701 132 GDWLERVEIDAARIddlpTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelglAVVIVTHD 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
331-490 |
3.96e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 69.18 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTL--------------------------LKSIVNKLQ- 381
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLvnliprfydvdsgrilidghdvrdytLASLRRQIGl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 382 ------LLHGDVAfgSNVSVGYYDQEQANLTSSKRVLN--ELWDEYPLQPEKEIrtilgnflftGDDVLKpvssLSGGQK 453
Cdd:cd03251 81 vsqdvfLFNDTVA--ENIAYGRPGATREEVEEAARAANahEFIMELPEGYDTVI----------GERGVK----LSGGQR 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-198 |
4.19e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----------IKPKDVSIGY 70
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETSLTIwDEMLTVFTHLQQMETklRRLEQEMGKeenfsnaatyeklLADYDQLQldykdqggyqYEADIRsil 150
Cdd:PRK13536 119 VPQFDNLDLEFTV-RENLLVFGRYFGMST--REIEAVIPS-------------LLEFARLE----------SKADAR--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 151 sglgfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13536 170 -------------VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
344-518 |
4.45e-13 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 69.46 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS----------VGYYDQE---QANLTSSK 409
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLaGVDLHglsrrararrVALVEQDsdtAVPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVL------NELWDEYPLQPEKEIRTILGNflfTGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:TIGR03873 95 VVAlgriphRSLWAGDSPHDAAVVDRALAR---TELSHLadRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 482 SKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:TIGR03873 172 AQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLD 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-229 |
4.83e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVS--IGYlaqNTGLETSLTiwdemltvfthl 94
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalLEL---GAGFHPELT------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 95 qqmetklrrleqemGkEEN-FSNAATYEKLLADYDQLqldykdqggyqyEADIRSiLSGLG-F---PVethqttiSTLSG 169
Cdd:COG1134 105 --------------G-RENiYLNGRLLGLSRKEIDEK------------FDEIVE-FAELGdFidqPV-------KTYSS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 170 GQKTRLALGKLLLTKPDLLILDEPTNHLDIE----TLTWLEQYLQGyPGAILIVSHDRYFLDKL 229
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRL 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
349-517 |
4.89e-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: 68.71 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVS------VGYydqeQANLTSSKRV-LNELWdeYPL 421
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllglgGGF----NPELTGRENIyLNGRL--LGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 422 QPeKEIRTILGNFL-FT--GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN----SKEILENaLIDYP 494
Cdd:cd03220 115 SR-KEIDEKIDEIIeFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRE-LLKQG 192
|
170 180
....*....|....*....|...
gi 446524828 495 GTLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03220 193 KTVILVSHDPSSIKRLCDRALVL 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-233 |
5.32e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.61 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKD--VSIGYLA 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTInlVRDKDgqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLETSLTIWDEMLTVFTHLQQMETKLRRLEQEMGkeenFSNAATYEKLLADYDQLQLDYKDQGGYqyeadirsilsg 152
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLG----LSKQEARERAVKYLAKVGIDERAQGKY------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 153 lgfPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHDRYFLDKL 229
Cdd:PRK10619 150 ---PVH--------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHV 218
|
....
gi 446524828 230 VTQV 233
Cdd:PRK10619 219 SSHV 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
331-487 |
5.42e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 69.13 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQLlhgdvafGSNVSVGYYDQEQANLtsSK 409
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NGLVE-------PTSGSVLIDGTDINKL--KG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNEL-------WDEYPLQPEKE---------------IRTILGnfLFTG----------------DDVLKPVSSLSGG 451
Cdd:cd03256 71 KALRQLrrqigmiFQQFNLIERLSvlenvlsgrlgrrstWRSLFG--LFPKeekqralaalervgllDKAYQRADQLSGG 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 452 QKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE 487
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDpASSRQVMD 185
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-221 |
6.42e-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: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAE--TILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII--------KPKDV--SI 68
Cdd:cd03266 1 MITADALTKRFRDVkkTVQAvdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAEArrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 69 GYLAQNTGLETSLTIWdEMLTVFTHLQQMEtklrrleqemgkeenfsnaatyeklladydqlqldykdqgGYQYEADIRS 148
Cdd:cd03266 81 GFVSDSTGLYDRLTAR-ENLEYFAGLYGLK----------------------------------------GDELTARLEE 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 149 ILSGLGFPvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG---AILIVSH 221
Cdd:cd03266 120 LADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
293-515 |
6.65e-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: 71.82 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 293 AQSRRKQLDrmELLTRPLGDSKSASFhFDIEKQSGNdvLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKS 370
Cdd:TIGR03375 431 AKTALQSLD--ELMQLPVERPEGTRF-LHRPRLQGE--IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKS 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 371 TLLKSIVNKLQLLHGDVAF-GSNVS----------VGYYDQEQA--------NLTSSKRVLNelwDEYPLQPEKeiRTIL 431
Cdd:TIGR03375 506 TLLKLLLGLYQPTEGSVLLdGVDIRqidpadlrrnIGYVPQDPRlfygtlrdNIALGAPYAD---DEEILRAAE--LAGV 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 432 GNFLFT---GDDvlKPVS----SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:TIGR03375 581 TEFVRRhpdGLD--MQIGergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTH 658
|
250
....*....|...
gi 446524828 503 DRYFINRVTTTVV 515
Cdd:TIGR03375 659 RTSLLDLVDRIIV 671
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
331-504 |
7.83e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 70.18 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ------LLHGDVAFgSNVS-----VGYYD 399
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLF-TNLPprerrVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 QEQA---NLTSSK------RVLNelwdeyplQPEKEIRTILgnflftgDDVLKPV----------SSLSGGQKARLALAK 460
Cdd:COG1118 82 QHYAlfpHMTVAEniafglRVRP--------PSKAEIRARV-------EELLELVqlegladrypSQLSGGQRQRVALAR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 461 LMMQKSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHDR 504
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQ 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-523 |
8.80e-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: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 341 DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLksivnklqllhgdvafgsnvsvgyydqeqanltsskRVLNELWdeyP 420
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF------------------------------------RALAGLW---P 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 421 LQPEKEIRTILGNFLF--------TG---DDVLKPVSS-LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK----E 484
Cdd:cd03223 53 WGSGRIGMPEGEDLLFlpqrpylpLGtlrEQLIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEdrlyQ 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524828 485 ILENALIdypgTLLFVSHdRYFINRVTTTVVELSTEGAQ 523
Cdd:cd03223 133 LLKELGI----TVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-522 |
9.79e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 324 KQSGNDVLQVKDATIG-YDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNklqlL----HGDVAFGSNVSVGYY 398
Cdd:COG4178 356 ETSEDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARPAGARVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQE----QANLtssKRVLNelwdeYPLQPEK----EIRTI-----LGNF---LFTGDD---VlkpvssLSGGQKARLALA 459
Cdd:COG4178 432 PQRpylpLGTL---REALL-----YPATAEAfsdaELREAleavgLGHLaerLDEEADwdqV------LSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 460 KLMMQKSNLLILDEPTNHLDLNSKEILENALID-YPG-TLLFVSHdRYFINRVTTTVVELSTEGA 522
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
328-514 |
1.12e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.76 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDAT----IGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLksivNKLQLL----HGDVAF-GSNVS---- 394
Cdd:COG1136 2 SPLLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL----NILGGLdrptSGEVLIdGQDISslse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 ----------VGYYDQeQANLtsskrvLNEL--WD--EYPL--------QPEKEIRTILGNF-LftGDDVLKPVSSLSGG 451
Cdd:COG1136 78 relarlrrrhIGFVFQ-FFNL------LPELtaLEnvALPLllagvsrkERRERARELLERVgL--GDRLDHRPSQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 452 QKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILE--NALIDYPG-TLLFVSHDRYFINRVTTTV 514
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSkTGEEVLEllRELNRELGtTIVMVTHDPELAARADRVI 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
330-492 |
1.93e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNklqLLHGDVAFGSNVSV-------------- 395
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAGSHIELlgrtvqregrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 396 --------GYYDQeQANLTSSKRVLNE----------LWDE-----YPLQPEKEIR--TILGNFLFTGddvlKPVSSLSG 450
Cdd:PRK09984 81 irksrantGYIFQ-QFNLVNRLSVLENvligalgstpFWRTcfswfTREQKQRALQalTRVGMVHFAH----QRVSTLSG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524828 451 GQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALID 492
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRD 197
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
330-503 |
1.94e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.81 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDED----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsIVNKLQ-------LLHGDVAFGSNVSVGYY 398
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLEkptsgevLVDGKPVTGPGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQE---------QANLtsskrvlnelwdEYPLQ----PEKEIRTILGNFLftgDDV-LKPV-----SSLSGGQKARLALA 459
Cdd:COG1116 86 FQEpallpwltvLDNV------------ALGLElrgvPKAERRERARELL---ELVgLAGFedaypHQLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 460 KLMMQKSNLLILDEPTNHLDLNSKEILENALID----YPGTLLFVSHD 503
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwqeTGKTVLFVTHD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-503 |
2.01e-12 |
|
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: 66.76 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 339 GYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvGYYDQEQANltSSKRVL------ 412
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-----GYSIRTDRK--AARQSLgycpqf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 413 NELWDEY-PLQ-----------PEKEIRTILGNFLFT---GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03263 84 DALFDELtVREhlrfyarlkglPKSEIKEEVELLLRVlglTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180
....*....|....*....|....*...
gi 446524828 478 LDLNSKEILENALIDYPG--TLLFVSHD 503
Cdd:cd03263 164 LDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-238 |
2.05e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.66 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 11 KLYGAETI-LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS------IGYLAQNTGL--ETS 80
Cdd:cd03292 8 KTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSdlrgraIPYLRRKIGVvfQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWDemLTVFTHLQ-QMEtklrrLEQEMGKEENfsnaatyEKLLADYDQLQLDYKdqggyqyeadirsilsglgfpvet 159
Cdd:cd03292 88 RLLPD--RNVYENVAfALE-----VTGVPPREIR-------KRVPAALELVGLSHK------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 160 HQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHDRYFLDKLVTQVYEI 236
Cdd:cd03292 130 HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIAL 209
|
..
gi 446524828 237 SN 238
Cdd:cd03292 210 ER 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-237 |
2.52e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 66.69 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSK-----LYGAETI--LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQN 74
Cdd:COG4778 3 TLLEVENLSKtftlhLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLE-TSLTIWdEMLtvfthlqqmetKLRRleQEMGKEENFSNA--------ATYEKLLAdydqlqldykdQGGYQYEAD 145
Cdd:COG4778 75 GWVDlAQASPR-EIL-----------ALRR--RTIGYVSQFLRViprvsaldVVAEPLLE-----------RGVDREEAR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 146 IR--SILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGypG-AILI 218
Cdd:COG4778 130 ARarELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GtAIIG 207
|
250
....*....|....*....
gi 446524828 219 VSHDRYFLDKLVTQVYEIS 237
Cdd:COG4778 208 IFHDEEVREAVADRVVDVT 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-223 |
3.01e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVSigylaqntglets 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDIS------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 lTIWDEmltvfTHLQQMetklrrleqemgkeenfSNAATYEKLLAD--YDQLQLDYKDQGGYQYEADIRSILSGLGFPVE 158
Cdd:PRK10247 73 -TLKPE-----IYRQQV-----------------SYCAQTPTLFGDtvYDNLIFPWQIRNQQPDPAIFLDDLERFALPDT 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 159 THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLT----WLEQYLQGYPGAILIVSHDR 223
Cdd:PRK10247 130 ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDK 198
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-542 |
3.10e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQAN 404
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 405 LTSSKRVLNELWDE--------------YPLQP-----EKEIRTIL-------GNFLFTGDDVLKPVSSLSGGQKARLAL 458
Cdd:PRK14246 85 AIKLRKEVGMVFQQpnpfphlsiydniaYPLKShgikeKREIKKIVeeclrkvGLWKEVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 459 AKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDYDYYVEKK 536
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
....*.
gi 446524828 537 NEMIER 542
Cdd:PRK14246 245 NELTEK 250
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
331-516 |
3.14e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 66.06 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSvALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS---------VGYYDQ 400
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 E---QANLTSSKRV-----LNELWDEyplQPEKEIRTILGNfLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:cd03264 80 EfgvYPNFTVREFLdyiawLKGIPSK---EVKARVDEVLEL-VNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 473 EPTNHLDLNSKEILENALIDypgtllfVSHDRYFInrVTTTVVE 516
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSE-------LGEDRIVI--LSTHIVE 190
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-194 |
4.59e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVsigylaqnTGLET 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfDGKDI--------TDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 80 SLTIWDEMLTVfthlqqmeTKLRRLEQEMGKEENFSNAATYekllADYDqlqldykdqggyQYEADIRSILSGLGFPVET 159
Cdd:PRK11614 75 AKIMREAVAIV--------PEGRRVFSRMTVEENLAMGGFF----AERD------------QFQERIKWVYELFPRLHER 130
|
170 180 190
....*....|....*....|....*....|....*
gi 446524828 160 HQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:PRK11614 131 RIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-224 |
4.95e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-------IGYLAQN 74
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTATrgdrsrfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWdEMLTVFTHLQQmetklRRLEQEMGkeenfsNAATYEKLlADYDQlqldykdqggyqyeadirsilsglg 154
Cdd:PRK13543 91 PGLKADLSTL-ENLHFLCGLHG-----RRAKQMPG------SALAIVGL-AGYED------------------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 155 fpvethqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRY 224
Cdd:PRK13543 133 -------TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-503 |
5.11e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSN-------------VSV 395
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 396 GYYDQEQANLTSSKRVLNEL-WDEYPLQ-PEKEIRTILGNFLF-TGDDVL--KPVSSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVsFGAVNLKlPEDEVRKRVDNALKrTGIEHLkdKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 471 LDEPTNHLD-LNSKEILENALIDYPG---TLLFVSHD 503
Cdd:PRK13636 165 LDEPTAGLDpMGVSEIMKLLVEMQKElglTIIIATHD 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-502 |
5.41e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 64.37 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgsnvsvgyyDQEQANLTSSKRVLNelwdeyplqpeKEIR 428
Cdd:cd03216 19 VSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV---------DGKEVSFASPRDARR-----------AGIA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 429 TilgnflftgddvlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILEN---ALIDYPGTLLFVSH 502
Cdd:cd03216 79 M---------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKvirRLRAQGVAVIFISH 140
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-502 |
5.60e-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: 65.96 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDP---IIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGY---YDQEQA 403
Cdd:cd03248 11 IVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 NLTSSKRVL--NELWDE--YPLQ--PEKEIRT----------ILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:cd03248 91 SLVGQEPVLfaRSLQDNiaYGLQscSFECVKEaaqkahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 468 LLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
331-502 |
5.61e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED-PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsivnklqLLhgdvafgsnvsVGYYDqeqanlTSSK 409
Cdd:COG1132 340 IEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVN-------LL-----------LRFYD------PTSG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLnelWDEYPLQ--PEKEIRTILG-----NFLFTG----------------------------DDVLK-------PV-- 445
Cdd:COG1132 396 RIL---IDGVDIRdlTLESLRRQIGvvpqdTFLFSGtirenirygrpdatdeeveeaakaaqahEFIEAlpdgydtVVge 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 446 --SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:COG1132 473 rgVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
330-504 |
6.01e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSnvsvgyydQEQANLTSSK 409
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--------VDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDEYPLQP----EKEIRTILGNFLFTGDDVLKPVS-----------------SLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK11607 91 RPINMMFQSYALFPhmtvEQNIAFGLKQDKLPKAEIASRVNemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 469 LILDEPTNHLDLNSKEILENALID----YPGTLLFVSHDR 504
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDilerVGVTCVMVTHDQ 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-233 |
7.54e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLS-----------KLYGAETILANIKLEVQTKDRIALVGRNGAGKST----LLKIIA--GELSHDGGEIikpkd 65
Cdd:PRK15134 275 LLDVEQLQvafpirkgilkRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPL----- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 66 vsigylaQNTGLETSLTIWDEMLTVFthlQQMETKLR-RLEQEMGKEENfsnaatyeklladydqLQLDYKDQGGYQYEA 144
Cdd:PRK15134 350 -------HNLNRRQLLPVRHRIQVVF---QDPNSSLNpRLNVLQIIEEG----------------LRVHQPTLSAAQREQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 DIRSILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVS 220
Cdd:PRK15134 404 QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFIS 483
|
250
....*....|...
gi 446524828 221 HDRYFLDKLVTQV 233
Cdd:PRK15134 484 HDLHVVRALCHQV 496
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
331-517 |
7.72e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 65.21 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIieHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ------LLHG-DVAFG--SNVSVGYYDQE 401
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETpqsgrvLINGvDVTAAppADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 Q---ANLTSSKRVLNELWDEYPLQPE--KEIRTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:cd03298 79 NnlfAHLTVEQNVGLGLSPGLKLTAEdrQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 477 HLDlnskEILENALIDY--------PGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03298 158 ALD----PALRAEMLDLvldlhaetKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-201 |
7.93e-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: 65.30 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQvnGLSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEI--IKPKDV- 66
Cdd:cd03258 1 MIELK--NVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLtlLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 67 ----SIGYLAQNTGLETSLTIWDEM---LTVfTHLQQMETKLRRLEqemgkeenfsnaatyekLLAdydqlqldykdqgg 139
Cdd:cd03258 79 karrRIGMIFQHFNLLSSRTVFENValpLEI-AGVPKAEIEERVLE-----------------LLE-------------- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 140 yqyeadirsiLSGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03258 127 ----------LVGLE---DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-221 |
8.10e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIG----YLA 72
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepIRRQRDEYHqdllYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLETSLTIWdemltvfthlqqmetklrrleqemgkeENfsnaatyeklLADYDQLQldykdqgGYQYEADIRSILS- 151
Cdd:PRK13538 81 HQPGIKTELTAL---------------------------EN----------LRFYQRLH-------GPGDDEALWEALAq 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 -GL-GF---PVethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-----QGypGAILIVSH 221
Cdd:PRK13538 117 vGLaGFedvPV-------RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhaeQG--GMVILTTH 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-198 |
8.14e-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: 65.37 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG---GEI------IKPKDV--SIGYLAQNTGLETSLTIwDE 86
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqpRKPDQFqkCVAYVRQDDILLPGLTV-RE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 87 MLTVFTHLqqmetKLRRLeqemgkeenfSNAATYEKLLADYDQLQLDYKDQGGYQYEAdirsilsglgfpvethqttist 166
Cdd:cd03234 101 TLTYTAIL-----RLPRK----------SSDAIRKKRVEDVLLRDLALTRIGGNLVKG---------------------- 143
|
170 180 190
....*....|....*....|....*....|..
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03234 144 ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
330-487 |
8.82e-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: 65.40 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQ-LLHGDVAF-GSNV------------- 393
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCI-NRLVePSSGSILLeGTDItklrgkklrklrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 394 SVGYYDQeQANLTSSKRVL-NELWDEypLQPEKEIRTILGnfLFTGDD----------------VLKPVSSLSGGQKARL 456
Cdd:TIGR02315 80 RIGMIFQ-HYNLIERLTVLeNVLHGR--LGYKPTWRSLLG--RFSEEDkeralsalervgladkAYQRADQLSGGQQQRV 154
|
170 180 190
....*....|....*....|....*....|..
gi 446524828 457 ALAKLMMQKSNLLILDEPTNHLD-LNSKEILE 487
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDpKTSKQVMD 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-222 |
1.08e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.86 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLY---------GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiIKPKDVSIGYL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN-VSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 --AQNTGL--ETSLTIWDEMLTV---FTHLQQMETKLRRLeqemgkeenfsnaatyeklladydqLQLDYKDQggyqyEA 144
Cdd:PRK10419 80 nrAQRKAFrrDIQMVFQDSISAVnprKTVREIIREPLRHL-------------------------LSLDKAER-----LA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 DIRSILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVS 220
Cdd:PRK10419 130 RASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFIT 209
|
..
gi 446524828 221 HD 222
Cdd:PRK10419 210 HD 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-221 |
1.60e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 24 LEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKD----------VSIgyLAQNTGLETSLTIWDEM----- 87
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDhtttppsrrpVSM--LFQENNLFSHLTVAQNIglgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 88 --LTVfTHLQQMetKLRRLEQEMGKEENFSNaatyeklladydqlqldykdqggyqyeadirsilsglgFPvethqttiS 165
Cdd:PRK10771 98 pgLKL-NAAQRE--KLHAIARQMGIEDLLAR--------------------------------------LP--------G 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSH 221
Cdd:PRK10771 129 QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-201 |
2.17e-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: 67.07 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYG-AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYL 71
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIlLNGFSLKdidrhtlrqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSlTIWDEMLtvfthlqqMETKlRRLEQEMGKEenfsnAATYEKLLADYDQLQLdykdqgGYQYEadirsiLS 151
Cdd:TIGR01193 554 PQEPYIFSG-SILENLL--------LGAK-ENVSQDEIWA-----ACEIAEIKDDIENMPL------GYQTE------LS 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 GLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:TIGR01193 607 EEG----------SSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-200 |
2.22e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIaGELSHDGGEIIKPKDVSIgylaqNTGlets 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAGTIRVGDITI-----DTA---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 ltiwdemltvfTHLQQMETKLRRLEQEMG-KEENFsNAATYEKLLADYDQLQLDYKDQGGYQYEADIRSILSGLGFPVEt 159
Cdd:PRK11264 71 -----------RSLSQQKGLIRQLRQHVGfVFQNF-NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 160 HQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK11264 138 ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-479 |
2.44e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIGYLAQNTGLETSL 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 TIWDEMLtvFTHLQQMETKLRRLEQemgkeenfsNAATYEKLLADYDQL--QLDYKDQGGYQYEAD--IRSILSGlgfpv 157
Cdd:PRK15439 91 VPQEPLL--FPNLSVKENILFGLPK---------RQASMQKMKQLLAALgcQLDLDSSAGSLEVADrqIVEILRG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 158 ethqttistlsggqktrlalgklLLTKPDLLILDEPTNHLD-IETLTwleqylqgypgailIVSHDRYFLDKLVTQVYeI 236
Cdd:PRK15439 155 -----------------------LMRDSRILILDEPTASLTpAETER--------------LFSRIRELLAQGVGIVF-I 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 237 SNK--ESRRFVGNYSKYLDLKSALYEqeikryekqqdeiaKLEDFVQKNIARASTTKraqSRRKQLDRMELLTRPLGDSK 314
Cdd:PRK15439 197 SHKlpEIRQLADRISVMRDGTIALSG--------------KTADLSTDDIIQAITPA---AREKSLSASQKLWLELPGNR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 315 SAsfhfdieKQSGNDVLQVKDAT-IGYdedpiiEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFG--- 390
Cdd:PRK15439 260 RQ-------QAAGAPVLTVEDLTgEGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgke 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 391 -SNVSVG--------YY--DQEQA----------NLTSSKRVLNELWdeypLQPEKEIRTILG-----NFLFTGDDvlKP 444
Cdd:PRK15439 327 iNALSTAqrlarglvYLpeDRQSSglyldaplawNVCALTHNRRGFW----IKPARENAVLERyrralNIKFNHAE--QA 400
|
490 500 510
....*....|....*....|....*....|....*
gi 446524828 445 VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-199 |
2.60e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.02 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS------IGYLAQ 73
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlVAGDDVEalsaraASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTiwdemltvfthlqqMETKLRRLeQEMGKEENFSNAATYEklladydqlqldykdqggyqyEADIRSILSGL 153
Cdd:PRK09536 81 SVPQDTSLS--------------FEFDVRQV-VEMGRTPHRSRFDTWT---------------------ETDRAAVERAM 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 154 GfPVETHQ---TTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK09536 125 E-RTGVAQfadRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-501 |
3.14e-11 |
|
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: 66.00 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG--GEIIkpkdvsigylaqntglets 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIY------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 ltiWDEMLTVFTHLQQMETK-LRRLEQEMGKEENFS--------NAATYEKLLADYDQLQLDYKDqggyqyeadirsILS 151
Cdd:TIGR02633 62 ---WSGSPLKASNIRDTERAgIVIIHQELTLVPELSvaeniflgNEITLPGGRMAYNAMYLRAKN------------LLR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 GLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSHdryfldK 228
Cdd:TIGR02633 127 ELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISH------K 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 229 LvTQVYEISnkesrrfvgnyskyldlksalyeqeikryekqqDEIAKLEDfvqkniARASTTKRAQSrrkqLDRMELLTR 308
Cdd:TIGR02633 201 L-NEVKAVC---------------------------------DTICVIRD------GQHVATKDMST----MSEDDIITM 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 309 PLGDSKSASFHFDiEKQSGNDVLQVKDATIGYDEDPIIEHVN---MRLTRGDSVALVGPNGIGKSTL------------- 372
Cdd:TIGR02633 237 MVGREITSLYPHE-PHEIGDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELvqalfgaypgkfe 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 373 ---------------LKSIVNKLQLL------HGDVafgSNVSVGYydqeqaNLTSSkrVLNELWDEYPLQPEKEIRTIL 431
Cdd:TIGR02633 316 gnvfingkpvdirnpAQAIRAGIAMVpedrkrHGIV---PILGVGK------NITLS--VLKSFCFKMRIDAAAELQIIG 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 432 GNF----LFTGDDVLkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI--LENALIDYPGTLLFVS 501
Cdd:TIGR02633 385 SAIqrlkVKTASPFL-PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyEIykLINQLAQEGVAIIVVS 460
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
3.16e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS-----------I 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiIDDEDISllplhararrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 69 GYLAQNTGLETSLTIWDEMLTVFthlqqmetklrRLEQEMGKEENFSNAatyEKLLADYdqlqldykdqggyqyeaDIRS 148
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVL-----------QIRDDLSAEQREDRA---NELMEEF-----------------HIEH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 149 ILSGLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDE------PTNHLDIETLTwleQYLQGYPGAILIVSHD 222
Cdd:PRK10895 130 LRDSMG----------QSLSGGERRRVEIARALAANPKFILLDEpfagvdPISVIDIKRII---EHLRDSGLGVLITDHN 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-83 |
3.23e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.95 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MIllQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKD----VS 67
Cdd:COG4604 1 MI--EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvatTPSRElakrLA 78
|
90
....*....|....*.
gi 446524828 68 IgyLAQNTGLETSLTI 83
Cdd:COG4604 79 I--LRQENHINSRLTV 92
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-502 |
3.60e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.02 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSI-----------VNKL---------------------QLLHGDVAfgSNVSVG 396
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyqgslkINGIelreldpeswrkhlswvgqnpQLPHGTLR--DNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 YYD--QEQANLTSSKRVLNELWDEYPLQPEKEIrtilgnflftGDDVlkpvSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:PRK11174 447 NPDasDEQLQQALENAWVSEFLPLLPQGLDTPI----------GDQA----AGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190
....*....|....*....|....*....|
gi 446524828 475 TNHLDLNSKEILENALIDYPG--TLLFVSH 502
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRrqTTLMVTH 542
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
331-503 |
3.84e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSnvsvgyydqeqANLTSSKR 410
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT-----------APLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQPEKEIRTILGNFLfTGD------DVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGL-KGQwrdaalQALAAVgladranewpAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 446524828 475 TNHLD----LNSKEILENALIDYPGTLLFVSHD 503
Cdd:PRK11247 161 LGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-222 |
4.40e-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: 64.74 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 21 NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQntglETSLtiwd 85
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqdsargifLPPHRRRIGYVFQ----EARL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 86 emltvFTHL---QQMETKLRRLEQEMGKeenfsnaatyekllADYDQLqldykdqggyqyeadIRsiLSGLGfpvetH-- 160
Cdd:COG4148 89 -----FPHLsvrGNLLYGRKRAPRAERR--------------ISFDEV---------------VE--LLGIG-----Hll 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQyLQ---GYPgaILIVSHD 222
Cdd:COG4148 128 DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLER-LRdelDIP--ILYVSHS 193
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-200 |
5.20e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.19 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 10 SKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIKPKdVSIGYLAQNTGLETslt 82
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVNDPK-VDERLIRQEAGMVF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 iwdEMLTVFTHLQQME------TKLRRleqeMGKEENfsnaatyeklladydqlqldykdqggyqyEADIRSILSGLGFP 156
Cdd:PRK09493 84 ---QQFYLFPHLTALEnvmfgpLRVRG----ASKEEA-----------------------------EKQARELLAKVGLA 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 157 VETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK09493 128 ERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
331-503 |
5.39e-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: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKR 410
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------GKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQP------------------EKEIR---------TILGNFLFtgddvlKPVSSLSGGQKARLALAKLMM 463
Cdd:cd03300 73 PVNTVFQNYALFPhltvfeniafglrlkklpKAEIKervaealdlVQLEGYAN------RKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 464 QKSNLLILDEPTNHLDLNSKEILE---NALIDYPG-TLLFVSHD 503
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-222 |
5.54e-11 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 63.29 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-----------KPKDVSIGYLA 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLETSLTIWDEMLtvfthlqqmetkLRRLeqemgkeenfsnaaTYEKLLAdydqlqLDYKDQGGYQYEADIRSILSG 152
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVA------------LGRI--------------PHRSLWA------GDSPHDAAVVDRALARTELSH 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 153 LGfpvethQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQyLQGYPGAILIVSHD 222
Cdd:TIGR03873 130 LA------DRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVraqlETLALVRE-LAATGVTVVAALHD 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-222 |
5.60e-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: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQN 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlLDGKDITnlpphkrpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDEMltvfthlqQMETKLRRLeqemgkeenfSNAATYEKLLADYDQLQLDykdqgGYQYEadirsilsglg 154
Cdd:cd03300 81 YALFPHLTVFENI--------AFGLRLKKL----------PKAEIKERVAEALDLVQLE-----GYANR----------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 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 |
6.03e-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: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 360 ALVGPNGIGKSTLLKSIvnkLQLLHGDVAFGSNVSVGYYD--QEQANLTSSKRVLNELWDEyPLQPEKEIRtILGNFLFT 437
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL---KYALTGELPPNSKGGAHDPKliREGEVRAQVKLAFENANGK-KYTITRSLA-ILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 438 -GDDVLKP----VSSLSGGQKA------RLALAKLMMQKSNLLILDEPTNHLDLNSK-----EILENALIDYPGTLLFVS 501
Cdd:cd03240 101 hQGESNWPlldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeeslaEIIEERKSQKNFQLIVIT 180
|
....*...
gi 446524828 502 HDRYFINR 509
Cdd:cd03240 181 HDEELVDA 188
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
331-503 |
6.32e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIieHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKR 410
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN--------GQDLTALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQP----------------------EKEIRTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNL 468
Cdd:COG3840 72 PVSMLFQENNLFPhltvaqniglglrpglkltaeqRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 469 LILDEPTNHLDLNSK-EILenALID-----YPGTLLFVSHD 503
Cdd:COG3840 151 LLLDEPFSALDPALRqEML--DLVDelcreRGLTVLMVTHD 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-233 |
6.91e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNtgl 77
Cdd:PRK11629 4 ILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI--------FNGQP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 78 etsltiwdemltvfthLQQMET----KLRrlEQEMGKEENFSNaatyekLLADYDQLQ-------LDYKDQGGYQYEAdi 146
Cdd:PRK11629 73 ----------------MSKLSSaakaELR--NQKLGFIYQFHH------LLPDFTALEnvampllIGKKKPAEINSRA-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 147 RSILSGLGFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL------QGypGAILIVS 220
Cdd:PRK11629 127 LEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgelnrlQG--TAFLVVT 203
|
250
....*....|...
gi 446524828 221 HDRYFLDKLVTQV 233
Cdd:PRK11629 204 HDLQLAKRMSRQL 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
330-509 |
7.35e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS------------VG 396
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlctyqkqlcfVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 YYDQEQANLTSSKrvlNELWDEYPLQPEKEIRTILGnfLFTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PRK13540 81 HRSGINPYLTLRE---NCLYDIHFSPGAVGITELCR--LFSLEHLIDyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 476 NHLDLNSKEILENALIDYP---GTLLFVSHDRYFINR 509
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-238 |
8.01e-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: 61.72 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 10 SKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKdvSIGYLAQNTGLEtSLTIWDEMLt 89
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQ-NGTIRENIL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 90 vfthlqqmetklrrleqeMGKEEnfsNAATYEKLLaDYDQLQLDYKdqggyqyeadirsILSGLgfpvetHQTTI----S 165
Cdd:cd03250 88 ------------------FGKPF---DEERYEKVI-KACALEPDLE-------------ILPDG------DLTEIgekgI 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWL-EQYLQGY---PGAILIVSHDRYFLDKlVTQVYEISN 238
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-503 |
8.71e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKS-TLLKII-----------AGELSHDGGEIIKPK 64
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 65 DVSigyLAQNTGLETSLtIWDEMLTVFTHLQQMETKLRR---LEQEMGKEenfsnAATYEklladydqlQLDYKDQGGyq 141
Cdd:PRK15134 83 EQT---LRGVRGNKIAM-IFQEPMVSLNPLHTLEKQLYEvlsLHRGMRRE-----AARGE---------ILNCLDRVG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 142 yeadIRSILSGLG-FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAI 216
Cdd:PRK15134 143 ----IRQAAKRLTdYP---HQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 217 LIVSHDRYFLDKLVTQVYEISNKESrrfvgnyskyldlksalyeqeikryekqqdeiakledfVQKNIARASTTKRAQSR 296
Cdd:PRK15134 211 LFITHNLSIVRKLADRVAVMQNGRC--------------------------------------VEQNRAATLFSAPTHPY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 297 RKQLdrmeLLTRPLGDSKSASfhfdiekQSGNDVLQVKDATIGY-----------DEDPIIEHVNMRLTRGDSVALVGPN 365
Cdd:PRK15134 253 TQKL----LNSEPSGDPVPLP-------EPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGES 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 366 GIGKST----LLKSI---------------VNKLQLLhgdvAFGSNVSVGYYDQEQA---NLTSSKRVLNELWDEYPL-- 421
Cdd:PRK15134 322 GSGKSTtglaLLRLInsqgeiwfdgqplhnLNRRQLL----PVRHRIQVVFQDPNSSlnpRLNVLQIIEEGLRVHQPTls 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 422 --QPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN-SKEILenALI-----DY 493
Cdd:PRK15134 398 aaQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTvQAQIL--ALLkslqqKH 475
|
570
....*....|
gi 446524828 494 PGTLLFVSHD 503
Cdd:PRK15134 476 QLAYLFISHD 485
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
353-515 |
8.94e-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: 62.43 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 353 LTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgSNVSVGYYDQE-QANLTSSKRVLnelwdeyplqpEKEIRTIL 431
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYiKADYEGTVRDL-----------LSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 432 GNFLFTGDDVLKP----------VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS--------KEILENAlidy 493
Cdd:cd03237 90 YTHPYFKTEIAKPlqieqildreVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmaskviRRFAENN---- 165
|
170 180
....*....|....*....|..
gi 446524828 494 PGTLLFVSHDRYFINRVTTTVV 515
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-237 |
9.03e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 62.35 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----IKPKDVSIGYLAQNT---GLETSLtIWDemltvf 91
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRRIGvvfGQKTQL-WWD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 92 thLQQMETklRRLEQEMGKEENFSNAATYEKLLadyDQLqldykdqggyqyeaDIRSILsglgfpvethQTTISTLSGGQ 171
Cdd:cd03267 110 --LPVIDS--FYLLAAIYDLPPARFKKRLDELS---ELL--------------DLEELL----------DTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 172 KTRLALGKLLLTKPDLLILDEPTNHLDI---ETL-TWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEIS 237
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIrNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
335-526 |
1.03e-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: 64.74 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 335 DATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVN-------------------KLQLLHGDVAF-GSNV- 393
Cdd:TIGR02203 337 TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRfyepdsgqilldghdladyTLASLRRQVALvSQDVv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 394 --------SVGYYDQEQANLTSSKRVL-----NELWDEYPLQPEKEIrtilgnflftGDDVlkpvSSLSGGQKARLALAK 460
Cdd:TIGR02203 417 lfndtianNIAYGRTEQADRAEIERALaaayaQDFVDKLPLGLDTPI----------GENG----VLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 461 LMMQKSNLLILDEPTNHLDLNSKEILENALidypgtllfvshDRYFINRvTTTVV--ELST-EGAQEYL 526
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAAL------------ERLMQGR-TTLVIahRLSTiEKADRIV 538
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-198 |
1.05e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----------IKPKDVSIGYLAQ 73
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpsrARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIwDEMLTVFthlqqmetklrrleqemGKEENFSNAATYEKLLADYDQLQLDYKdqggyqyeADIRsilsgl 153
Cdd:PRK13537 88 FDNLDPDFTV-RENLLVF-----------------GRYFGLSAAAARALVPPLLEFAKLENK--------ADAK------ 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524828 154 gfpvethqttISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13537 136 ----------VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
331-503 |
1.10e-10 |
|
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: 62.36 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKR 410
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG--------GEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPL----------------------QPEKEIRTILGNFL-FTGDDVLK---PvSSLSGGQKARLALAKLMMQ 464
Cdd:cd03296 75 NVGFVFQHYALfrhmtvfdnvafglrvkprserPPEAEIRAKVHELLkLVQLDWLAdryP-AQLSGGQRQRVALARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524828 465 KSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHD 503
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRrlhdELHVTTVFVTHD 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-229 |
1.17e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigyLAQntgleTS 80
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL---------LNG-----QP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWDE-----MLTVFT---HLqqMETKLRrleqemgkeENF---SNAATYEKLLADYDQLQLDYKDQGgyqyEADIRSI 149
Cdd:PRK11160 404 IADYSEaalrqAISVVSqrvHL--FSATLR---------DNLllaAPNASDEALIEVLQQVGLEKLLED----DKGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 150 LSGLGFPvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGypGAILIVSHDRYF 225
Cdd:PRK11160 469 LGEGGRQ----------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITHRLTG 536
|
....
gi 446524828 226 LDKL 229
Cdd:PRK11160 537 LEQF 540
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-222 |
1.30e-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: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG-ELSHDGGEIIKPKDVSIG-----YLAQNTGLETSLTIWDEM-LTVF 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQITEPgpdrmVVFQNYSLLPWLTVRENIaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 92 THLQQMetklRRLEQEMGKEENFsnaatyeklladydqlqldykDQGGYQYEADIRsilsglgfpvethqttISTLSGGQ 171
Cdd:TIGR01184 81 RVLPDL----SKSERRAIVEEHI---------------------ALVGLTEAADKR----------------PGQLSGGM 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 172 KTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:TIGR01184 120 KQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
331-479 |
1.65e-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: 61.01 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKL-QLLHGDVAFgsnvsvgyydqEQANLTSSK 409
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTIII-----------DGLKLTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDE-------YPLQPEKeirTILGNFLF---------------TGDDVLKPV----------SSLSGGQKARLA 457
Cdd:cd03262 69 KNINELRQKvgmvfqqFNLFPHL---TVLENITLapikvkgmskaeaeeRALELLEKVgladkadaypAQLSGGQQQRVA 145
|
170 180
....*....|....*....|..
gi 446524828 458 LAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALD 167
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
324-515 |
1.78e-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: 64.58 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 324 KQSGNDVLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSvgyYDQE 401
Cdd:TIGR00957 630 KPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA---YVPQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QANLTSSKRVLNELWDeYPLQPEKEIRTILG-------NFLFTGD--DVLKPVSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:TIGR00957 707 QAWIQNDSLRENILFG-KALNEKYYQQVLEAcallpdlEILPSGDrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 473 EPTNHLDLN-SKEILENaLIDYPGTL-----LFVSHDRYFINRVTTTVV 515
Cdd:TIGR00957 786 DPLSAVDAHvGKHIFEH-VIGPEGVLknktrILVTHGISYLPQVDVIIV 833
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-229 |
1.95e-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: 61.66 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 32 IALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvSIGYLAQNTGLETSLTIwDEMLtvfthlqqmetklrrleqeMGKE 111
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTV-RDLL-------------------SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 112 ENFSNAATYEKLLAdyDQLQLDykdqggyqyeadirSILsglgfpvethQTTISTLSGGQKTRLALGKLLLTKPDLLILD 191
Cdd:cd03237 87 KDFYTHPYFKTEIA--KPLQIE--------------QIL----------DREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524828 192 EPTNHLDIE----TLTWLEQYLQGYPGAILIVSHDRYFLDKL 229
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYL 182
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
331-518 |
1.97e-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: 61.03 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIieHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKR 410
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVN--------DQSHTGLAPYQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQPEKEIRTILGNFLFTG--------------------DDVLKPV-SSLSGGQKARLALAKLMMQKSNLL 469
Cdd:TIGR01277 71 PVSMLFQENNLFAHLTVRQNIGLGLHPGlklnaeqqekvvdaaqqvgiADYLDRLpEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 470 ILDEPTNHLD-LNSKEILenALI-----DYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:TIGR01277 151 LLDEPFSALDpLLREEML--ALVkqlcsERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-230 |
2.07e-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: 61.74 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY---------GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGelshdggeIIKPKDVSIGYLAQ 73
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG--------LEKPAQGTVSFRGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NtgletsltiwdemltvFTHLQQMETKLRRLEQEMGKEENFS--NA-ATYEKLLAD--YDQLQLDYKDQggyqyEADIRS 148
Cdd:TIGR02769 74 D----------------LYQLDRKQRRAFRRDVQLVFQDSPSavNPrMTVRQIIGEplRHLTSLDESEQ-----KARIAE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 149 ILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD-- 222
Cdd:TIGR02769 133 LLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDlr 212
|
250
....*....|
gi 446524828 223 --RYFLDKLV 230
Cdd:TIGR02769 213 lvQSFCQRVA 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-518 |
2.11e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS----------VGYY 398
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATrgdrsrfmayLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQANLTSSKRV--LNELWDEYPLQPEKEIRTILGnfLFTGDDVLkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:PRK13543 91 PGLKADLSTLENLhfLCGLHGRRAKQMPGSALAIVG--LAGYEDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524828 477 HLDLNSKEILENAL---IDYPGTLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK13543 167 NLDLEGITLVNRMIsahLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
331-517 |
2.25e-10 |
|
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: 60.76 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS------VGYYDQEQA 403
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDiaarnrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 nLTSSKRV------LNELWDEYPLQPEKEIRTILGNFLFtGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:cd03269 81 -LYPKMKVidqlvyLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524828 478 LDLNSKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
349-517 |
2.43e-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: 60.88 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSvGYYDQEQANLtssKRVLNELWDEYPLQPEkei 427
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVS-DLRGRAIPYL---RRKIGVVFQDFRLLPD--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 428 RTILGNFLFT-------GDDVLKPVSS-----------------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NS 482
Cdd:cd03292 93 RNVYENVAFAlevtgvpPREIRKRVPAalelvglshkhralpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPdTT 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 483 KEILE--NALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:cd03292 173 WEIMNllKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-221 |
2.44e-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: 63.58 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETI--LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETS 80
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWDEML---TVFTHLQqmetklrrleqeMGKEENFSNAATYEKLLADYDQlqlDYKDQggyqyeadirsILSGLGFPV 157
Cdd:TIGR02203 410 LVSQDVVLfndTIANNIA------------YGRTEQADRAEIERALAAAYAQ---DFVDK-----------LPLGLDTPI 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 158 ETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGaiLIVSH 221
Cdd:TIGR02203 464 GENG---VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTT--LVIAH 526
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
330-512 |
2.52e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.26 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQ-------LLHGDVAFGSNVSVGYYDQEq 402
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEeitsgdlIVDGLKVNDPKVDERLIRQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 ANLtsskrvlneLWDEYPLQPEkeiRTILGNFLF---------------TGDDVLKPV----------SSLSGGQKARLA 457
Cdd:PRK09493 79 AGM---------VFQQFYLFPH---LTALENVMFgplrvrgaskeeaekQARELLAKVglaerahhypSELSGGQQQRVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 458 LAKLMMQKSNLLILDEPTNHLDLNSK-EILE--NALIDYPGTLLFVSHDRYFINRVTT 512
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEKVAS 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-492 |
2.74e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSVG---YYDQ----- 400
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRQrdeYHQDllylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 EQA----------NLTSSKRVLNELWDEyplqpekEIRTILGNFLFTG-DDVlkPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK13538 81 HQPgikteltaleNLRFYQRLHGPGDDE-------ALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|...
gi 446524828 470 ILDEPTNHLDLNSKEILEnALID 492
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLE-ALLA 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-230 |
2.85e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAgelshdggEIIKPKDvsigylaqntgleTSLTI 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--------RLLTPQS-------------GTVFL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVFTHlQQMETKLRRLEQEMGKEENFsnaaTYEKLLA----DYDQL--QLDYKDQGGYQYEADIRSIlsglgfpV 157
Cdd:PRK11231 62 GDKPISMLSS-RQLARRLALLPQHHLTPEGI----TVRELVAygrsPWLSLwgRLSAEDNARVNQAMEQTRI-------N 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 158 ETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE---TLTWLEQYLQGYPGAILIVSHD-----RYfLDKL 229
Cdd:PRK11231 130 HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDlnqasRY-CDHL 208
|
.
gi 446524828 230 V 230
Cdd:PRK11231 209 V 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-221 |
2.96e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 21 NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------------IKPKDVSIGYLAQNTGLetsltiwd 85
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvlfdaekgicLPPEKRRIGYVFQDARL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 86 emltvFTHlqqmetklrrleqemgkeenfsnaatyeklladydqlqldYKDQGGYQY------EADIRSILSGLG----- 154
Cdd:PRK11144 88 -----FPH----------------------------------------YKVRGNLRYgmaksmVAQFDKIVALLGiepll 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 155 --FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSH 221
Cdd:PRK11144 123 drYP--------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-233 |
3.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.60 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGYLA 72
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvdITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLetsltiwdemltVFthlQQMETKLrrLEQEMGKEENF-------SNAATYEKLLADYDQLQLDY---KDQGgyqy 142
Cdd:PRK13637 83 KKVGL------------VF---QYPEYQL--FEETIEKDIAFgpinlglSEEEIENRVKRAMNIVGLDYedyKDKS---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 143 eadirsilsglgfPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILI 218
Cdd:PRK13637 142 -------------PFE--------LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIIL 200
|
250
....*....|....*
gi 446524828 219 VSHDRYFLDKLVTQV 233
Cdd:PRK13637 201 VSHSMEDVAKLADRI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
331-503 |
3.01e-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: 60.91 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGS------------------- 391
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 392 --------------NVSVGYYDQEQANLTSSKRVlnelwdeyplQPEKEIRTILGNFL-FTG-DDVL-KPVSSLSGGQKA 454
Cdd:cd03219 81 fqiprlfpeltvleNVMVAAQARTGSGLLLARAR----------REEREARERAEELLeRVGlADLAdRPAGELSYGQQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 455 RLALAKLMMQKSNLLILDEPTNhlDLNSKEIleNALIDY------PG-TLLFVSHD 503
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAA--GLNPEET--EELAELirelreRGiTVLLVEHD 202
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-201 |
3.20e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 60.53 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigYLAQntgle 78
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV---------RLAG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 79 TSLTIWDE----------MLTVFTHLQQMETkLRRLEQEM------GKEENFSNAAtyeKLLADYdqlqldykdqggyqy 142
Cdd:COG4181 74 QDLFALDEdararlrarhVGFVFQSFQLLPT-LTALENVMlplelaGRRDARARAR---ALLERV--------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 143 eadirsilsGLG-----FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG4181 135 ---------GLGhrldhYP--------AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
331-479 |
3.41e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.19 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLqllhgDVAFGSNVSVGYYDQEQANLTSSKR 410
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTL-----SPAFSASGEVLLNGRRLTALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQPEkeiRTILGNFLF-------------TGDDVL----------KPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:COG4136 77 RIGILFQDDLLFPH---LSVGENLAFalpptigraqrraRVEQALeeaglagfadRDPATLSGGQRARVALLRALLAEPR 153
|
170
....*....|..
gi 446524828 468 LLILDEPTNHLD 479
Cdd:COG4136 154 ALLLDEPFSKLD 165
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
328-523 |
3.70e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.50 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDatIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS---------- 394
Cdd:PRK10247 5 SPLLQLQN--VGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIStlkpeiyrqq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYYDQEQANLTSSkrVLNEL---WDEYPLQPE-KEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:PRK10247 83 VSYCAQTPTLFGDT--VYDNLifpWQIRNQQPDpAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 471 LDEPTNHLDLNSK----EILENALIDYPGTLLFVSHDRYFINRvTTTVVELSTEGAQ 523
Cdd:PRK10247 161 LDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQPHAGE 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-210 |
3.79e-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: 60.32 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVS-------IGYLAQNTGLETSlti 83
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGHDV---RDYTlaslrrqIGLVSQDVFLFND--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 wdemlTVFthlqqmetklrrleqemgkeENFsnaaTYEKLLADYDQLQLDYKDQGGYQYeadIRSILSGLgfpvethQTT 163
Cdd:cd03251 91 -----TVA--------------------ENI----AYGRPGATREEVEEAARAANAHEF---IMELPEGY-------DTV 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 164 I----STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQ 210
Cdd:cd03251 132 IgergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES----ERLVQ 178
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
330-515 |
3.89e-10 |
|
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: 60.82 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ------LLHG-DVA-------------- 388
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGrDITglpphriarlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 389 -------FGS-----NVSVGYYDQEQANLTSSKRVLNELWDEYPlQPEKEIRTILGnflFTG-DDVL-KPVSSLSGGQKA 454
Cdd:COG0411 84 tfqnprlFPEltvleNVLVAAHARLGRGLLAALLRLPRARREER-EARERAEELLE---RVGlADRAdEPAGNLSYGQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 455 RLALAKLMMQKSNLLILDEPTNhlDLNSKEILE-NALI----DYPG-TLLFVSHDRYFINRVTTTVV 515
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAA--GLNPEETEElAELIrrlrDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-233 |
3.95e-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: 59.85 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGelsHDGGEIIKPKdvsIGYlaqntgletslti 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKYEVTEGE---ILF------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 wdemltvfthlqqmetklrrleqemgKEENFSNAATYEKLLAdydqlqldykdqG---GYQYEADI---------RSIls 151
Cdd:cd03217 62 --------------------------KGEDITDLPPEERARL------------GiflAFQYPPEIpgvknadflRYV-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 152 GLGFpvethqttistlSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ---YLQGYPGAILIVSHDRYFLDK 228
Cdd:cd03217 102 NEGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDY 169
|
....*
gi 446524828 229 LVTQV 233
Cdd:cd03217 170 IKPDR 174
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-198 |
4.09e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.97 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSIGYL 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLTIWDEMltvfthlqQMETKLRRLEQ-EMGKEENfsNAAtyeklladyDQLQLDY------KDqggyqyea 144
Cdd:PRK11000 81 FQSYALYPHLSVAENM--------SFGLKLAGAKKeEINQRVN--QVA---------EVLQLAHlldrkpKA-------- 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 145 dirsilsglgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11000 134 ----------------------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
331-514 |
4.24e-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: 60.32 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYD-EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsivnkLQLLHGDVAFGSnVSVGYYDQEQANLTSSK 409
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-----LLFRFYDVSSGS-ILIDGQDIREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVL------NELWDEyplqpekeirTILGNFLF-----TGDDVLKPVSS------------------------LSGGQKA 454
Cdd:cd03253 75 RAIgvvpqdTVLFND----------TIGYNIRYgrpdaTDEEVIEAAKAaqihdkimrfpdgydtivgerglkLSGGEKQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHdryfinRVTTTV 514
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH------RLSTIV 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-490 |
4.63e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD--GGEIikpkdvsigylaqntglets 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEI-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 ltIWDEMLTVFTHLQQMETK--------LrRLEQEMGKEEN--FSNAATYEKLLaDYDQLQLDYKdqggyqyeadirSIL 150
Cdd:PRK13549 65 --IFEGEELQASNIRDTERAgiaiihqeL-ALVKELSVLENifLGNEITPGGIM-DYDAMYLRAQ------------KLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 SGLGFPVETHqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL-DIETLTWLEqylqgypgailIVshdRYFLDKL 229
Cdd:PRK13549 129 AQLKLDINPA-TPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLD-----------II---RDLKAHG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 230 VTQVYeISNKesrrfvgnyskyLDlksalyeqEIKRYekqQDEIAKLEDfvQKNIArastTKRAQsrrkQLDRMELLTRP 309
Cdd:PRK13549 194 IACIY-ISHK------------LN--------EVKAI---SDTICVIRD--GRHIG----TRPAA----GMTEDDIITMM 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 310 LGDSKSASFHfDIEKQSGNDVLQVKDATIGYDEDP---IIEHVNMRLTRGDSVALVGPNGIGKSTLLKS----------- 375
Cdd:PRK13549 240 VGRELTALYP-REPHTIGEVILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQClfgaypgrweg 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 376 ----------IVNKLQLL-------------HG---DVAFGSNVSVGYYDQeqanlTSSKRVLNElwdeyplqpEKEIRT 429
Cdd:PRK13549 319 eifidgkpvkIRNPQQAIaqgiamvpedrkrDGivpVMGVGKNITLAALDR-----FTGGSRIDD---------AAELKT 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 430 ILgnflfTGDDVLK--------PVSSLSGG--QKArlALAKLMMQKSNLLILDEPTNHLDLNSK-EI--LENAL 490
Cdd:PRK13549 385 IL-----ESIQRLKvktaspelAIARLSGGnqQKA--VLAKCLLLNPKILILDEPTRGIDVGAKyEIykLINQL 451
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
340-474 |
4.81e-10 |
|
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: 60.25 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 340 YDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSN------------VSVGYYDQEQA---N 404
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLPQEASifrK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 405 LTSSKRVLNELwdEYPLQPEKEIRTILGNFL--FTGDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:cd03218 90 LTVEENILAVL--EIRGLSKKEREEKLEELLeeFHITHLRKsKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-222 |
5.21e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.80 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD---GGEI---------IKPKDVSIGYL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVllngrrltaLPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQntgletsltiwDEMLtvFTHLQQMETKLRRLEQEMGKEENfsnAATYEKLLADYDqlqldykdqggyqyeadirsiLS 151
Cdd:COG4136 82 FQ-----------DDLL--FPHLSVGENLAFALPPTIGRAQR---RARVEQALEEAG---------------------LA 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 152 GLGFpvethqTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:COG4136 125 GFAD------RDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
339-517 |
5.42e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 339 GYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ------LLHGDVAFGSNVSVGYydqeQANLT------ 406
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsgrvEVNGRVSALLELGAGF----HPELTgreniy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 407 SSKRVLNelwdeyplQPEKEIRTI---------LGNFLFTgddvlkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNH 477
Cdd:COG1134 111 LNGRLLG--------LSRKEIDEKfdeivefaeLGDFIDQ------PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 478 LDLN----SKEILENaLIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG1134 177 GDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
330-502 |
5.50e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQLLHGDVAFgsnvsVGYYDQEQANLTSSK 409
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTI-----TGSIVYNGHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDEYPL---QPEKEIRTILGNFLF-----------TGDDV----LKPVS--------------SLSGGQKARLA 457
Cdd:PRK14239 79 TDTVDLRKEIGMvfqQPNPFPMSIYENVVYglrlkgikdkqVLDEAveksLKGASiwdevkdrlhdsalGLSGGQQQRVC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524828 458 LAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYpgTLLFVSH 502
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLglkdDY--TMLLVTR 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
320-542 |
6.46e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.96 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 320 FDIEKQSGNdvLQVKDATIGYD--EDPIIEHVNMRLTRGDSVALVGPNGIGKSTllksIVNKLQLLHgDVAFGS----NV 393
Cdd:PRK11176 333 RVIERAKGD--IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFY-DIDEGEilldGH 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 394 SVGYYD----QEQANLTSSK------RVLNELW----DEYPL-QPEKEIRTILG-NFLFTGDDVLKPV-----SSLSGGQ 452
Cdd:PRK11176 406 DLRDYTlaslRNQVALVSQNvhlfndTIANNIAyartEQYSReQIEEAARMAYAmDFINKMDNGLDTVigengVLLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 453 KARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL--IDYPGTLLFVSHdryfinrvtttvvELST-EGAQEYLgdy 529
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH-------------RLSTiEKADEIL--- 549
|
250
....*....|...
gi 446524828 530 dyyVEKKNEMIER 542
Cdd:PRK11176 550 ---VVEDGEIVER 559
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
344-490 |
6.78e-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: 59.86 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTllksIVNKLQLLH----GDVAF-GSNVS----------VGYYDQEQANLTSS 408
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERFYdptsGEILLdGVDIRdlnlrwlrsqIGLVSQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 KRVlNELWDEYPLQPEKEIRTI----LGNFLFT----GDDVLKPV-SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03249 93 IAE-NIRYGKPDATDEEVEEAAkkanIHDFIMSlpdgYDTLVGERgSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170
....*....|.
gi 446524828 480 LNSKEILENAL 490
Cdd:cd03249 172 AESEKLVQEAL 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
344-502 |
7.42e-10 |
|
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: 59.27 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNV---------------SVGYYDQE------- 401
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnrySVAYAAQKpwllnat 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 -QANLTS----SKRVLNELWDEYPLQPEKEIrtilgnfLFTGD--DVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:cd03290 95 vEENITFgspfNKQRYKAVTDACSLQPDIDL-------LPFGDqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|...
gi 446524828 475 TNHLDLN-SKEILENALI----DYPGTLLFVSH 502
Cdd:cd03290 168 FSALDIHlSDHLMQEGILkflqDDKRTLVLVTH 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
344-490 |
7.64e-10 |
|
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: 62.24 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSvgYYDQEQANLTSSKR---VLNELWDEY- 419
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--FSPQTSWIMPGTIKdniIFGLSYDEYr 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 420 --------------PLQPEKEiRTILGNFLFTgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKE 484
Cdd:TIGR01271 518 ytsvikacqleediALFPEKD-KTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTEKE 586
|
....*.
gi 446524828 485 ILENAL 490
Cdd:TIGR01271 587 IFESCL 592
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-200 |
7.97e-10 |
|
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: 61.59 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIK--PKDV--SIGYLAQNTGLETSlt 82
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIvgiwpptSGSVRLDGADLKQwdRETFgkHIGYLPQDVELFPG-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 iwdemlTVFTHLQQMEtklrrleqemgkeENFSNAATYEKL-LADYDQLQLDYKDQggyqYEADIrsilsGLGFpvethq 161
Cdd:TIGR01842 407 ------TVAENIARFG-------------ENADPEKIIEAAkLAGVHELILRLPDG----YDTVI-----GPGG------ 452
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524828 162 ttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:TIGR01842 453 ---ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
331-479 |
8.62e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.86 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKR 410
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG--------GRDVTDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 vlN--------ELWD--------EYPLQ----PEKEIR-------TILGnfLftgDDVL--KPvSSLSGGQKARLALAKL 461
Cdd:COG3839 76 --NiamvfqsyALYPhmtvyeniAFPLKlrkvPKAEIDrrvreaaELLG--L---EDLLdrKP-KQLSGGQRQRVALGRA 147
|
170
....*....|....*...
gi 446524828 462 MMQKSNLLILDEPTNHLD 479
Cdd:COG3839 148 LVREPKVFLLDEPLSNLD 165
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
345-510 |
8.74e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgSNVSVGYYDQEQANltSSKRVLNELWDEYP--LQ 422
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRAQRK--AFRRDIQMVFQDSIsaVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 423 PEKEIRTILGNFL--FTG----------DDVLKPV-----------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK10419 104 PRKTVREIIREPLrhLLSldkaerlaraSEMLRAVdlddsvldkrpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524828 480 LnskeILENALIDYPGTL--------LFVSHD----RYFINRV 510
Cdd:PRK10419 184 L----VLQAGVIRLLKKLqqqfgtacLFITHDlrlvERFCQRV 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
325-474 |
8.92e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSV----GYYD 399
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAmsrsRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 --QEQANLTSSKRVLNEL--WDE--YPLQ-----PEKEIRTILGNFL----FTGDDVLKPvSSLSGGQKARLALAKLMMQ 464
Cdd:PRK11831 82 vrKRMSMLFQSGALFTDMnvFDNvaYPLRehtqlPAPLLHSTVMMKLeavgLRGAAKLMP-SELSGGMARRAALARAIAL 160
|
170
....*....|
gi 446524828 465 KSNLLILDEP 474
Cdd:PRK11831 161 EPDLIMFDEP 170
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-201 |
8.99e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELShdggeiiKPKDVSIGYLAQNTglets 80
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------GTPVAGCVDVPDNQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 ltiWDEMLTVFTHLqqmetklrrleqemGKEENFSNAAtyeKLLADydqlqldykdqggyqyeadirsilSGLGFPVeTH 160
Cdd:COG2401 96 ---FGREASLIDAI--------------GRKGDFKDAV---ELLNA------------------------VGLSDAV-LW 130
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG2401 131 LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-222 |
9.29e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.62 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiIKPKDVSIGYLA---------- 72
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQHIEGLPghqiarmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 ---QNTGLETSLTIWdEMLTVFTHlQQMETKL----------RRLEQEMgkeenFSNAATYeklLADYDQLQLDYKDQGg 139
Cdd:PRK11300 84 rtfQHVRLFREMTVI-ENLLVAQH-QQLKTGLfsgllktpafRRAESEA-----LDRAATW---LERVGLLEHANRQAG- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 140 yqyeadirsilsglgfpvethqttisTLSGGQKTRLALGKLLLTKPDLLILDEPT---NHLDIETLTWLEQYLQGYPG-A 215
Cdd:PRK11300 153 --------------------------NLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvT 206
|
....*..
gi 446524828 216 ILIVSHD 222
Cdd:PRK11300 207 VLLIEHD 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
9.83e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.88 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYG----AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDVSIGY 70
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETsltiWdemLTVfthLQQMETKLRRleQEMGKEENFSNAatyEKLLAdydqlqldykdqggyqyeadirsiL 150
Cdd:COG4525 81 VFQKDALLP----W---LNV---LDNVAFGLRL--RGVPKAERRARA---EELLA------------------------L 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 151 SGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG4525 122 VGLA---DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-223 |
1.01e-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: 61.85 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGgeiikpkDVSIGYLAQNTgleTSL 81
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-------EIQIDGVSWNS---VTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 TIWDEMLTVFthlqqmetklrrleqemgKEENFSNAATYEKLLADYDQlqldYKDQGGYQY--EADIRSILSglGFPVET 159
Cdd:TIGR01271 1288 QTWRKAFGVI------------------PQKVFIFSGTFRKNLDPYEQ----WSDEEIWKVaeEVGLKSVIE--QFPDKL 1343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 160 HQTTIS---TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-QGYPGAILIVSHDR 223
Cdd:TIGR01271 1344 DFVLVDggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-227 |
1.09e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGaetilaNIKLEVQ-----TKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpkDVSIGYLAQNTg 76
Cdd:PRK13409 339 TLVEYPDLTKKLG------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYI- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 77 letsltiwdemltvfthlqqmetklrRLEQEMGKEENFSNAAtyEKLLADYdqlqldykdqggYQYEadirsILSGLGFP 156
Cdd:PRK13409 410 --------------------------KPDYDGTVEDLLRSIT--DDLGSSY------------YKSE-----IIKPLQLE 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 157 vETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE----TLTWLEQYLQGYPGAILIVSHDRYFLD 227
Cdd:PRK13409 445 -RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMID 518
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
331-503 |
1.14e-09 |
|
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: 58.92 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGD-VAFGSNV---------SVGYYDQ 400
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 EQA---------NLTSSKRVLNELWDEYplqpEKEIRTILgNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03265 81 DLSvddeltgweNLYIHARLYGVPGAER----RERIDELL-DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 446524828 472 DEPTNHLDLNSK----EILENALIDYPGTLLFVSHD 503
Cdd:cd03265 156 DEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHY 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-502 |
1.14e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.23 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI-------VNKLQLLHGDV---AFGSNVSVGY--- 397
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdAGKITVLGVPVparARLARARIGVvpq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 398 YDQEQANLTSSKRVLneLWDEYPLQPEKEIRTILGNFL-FT--GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:PRK13536 122 FDNLDLEFTVRENLL--VFGRYFGMSTREIEAVIPSLLeFArlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190
....*....|....*....|....*....|.
gi 446524828 475 TNHLDLNSKE-ILE--NALIDYPGTLLFVSH 502
Cdd:PRK13536 200 TTGLDPHARHlIWErlRSLLARGKTILLTTH 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-229 |
1.20e-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: 59.30 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 34 LVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvsigylaqntgletsltiWDEMLTVF--THLQQMETKLRrlEQEMGKE 111
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPD------------------WDEILDEFrgSELQNYFTKLL--EGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 112 ENFSNAATYEKLLADYDQLQLDYKDQGGYQYEADIRSILSGLgfpVETHqttISTLSGGQKTRLALGKLLLTKPDLLILD 191
Cdd:cd03236 91 VKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHV---LDRN---IDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 192 EPTNHLDIE---TLTWLEQYLQGYPGAILIVSHDRYFLDKL 229
Cdd:cd03236 165 EPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYL 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-517 |
1.41e-09 |
|
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: 60.13 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQL------LHGDVAFGSNV---------SVGYYDQEqANL---TSSKR 410
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPdegeivLNGRTLFDSRKgiflppekrRIGYVFQE-ARLfphLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNE-LWD---EYPLQPEKEIRTILGnflfTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI 485
Cdd:TIGR02142 95 NLRYgMKRarpSERRISFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKyEI 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 486 ---LEN--ALIDYPgtLLFVSHDRYFINRVTTTVVEL 517
Cdd:TIGR02142 171 lpyLERlhAEFGIP--ILYVSHSLQEVLRLADRVVVL 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
329-517 |
1.44e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 329 DVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQE---QANL 405
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 T-SSKRVLNelwdeypLQPEKEIRTILGNF--LFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS 482
Cdd:PRK09544 83 PlTVNRFLR-------LRPGTKKEDILPALkrVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 483 KEILENaLIDYPGT-----LLFVSHDRYFINRVTTTVVEL 517
Cdd:PRK09544 156 QVALYD-LIDQLRReldcaVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-201 |
1.57e-09 |
|
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: 58.39 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI----IKPKDVS-------IGYLAQNTGLeTSLTIWDE 86
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgIDIRDISrkslrsmIGVVLQDTFL-FSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 87 MLtvfthlqqmetklrrleqeMGKEEnfsnaATYEKLLADYDQLQLDY---KDQGGYQYEADIRSilsglgfpvethqtt 163
Cdd:cd03254 97 IR-------------------LGRPN-----ATDEEVIEAAKEAGAHDfimKLPNGYDTVLGENG--------------- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524828 164 iSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03254 138 -GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
346-503 |
1.80e-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: 59.00 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLksivnklQLL-------HGDVAFGSNVSVgyydqeqanlTSSKRVLNELWDE 418
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLI-------QHLngllkptSGTVTIDGRDIT----------AKKKKKLKDLRKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 419 YPL---QPEKEI--RTIL-------GNFLFTGDDVLKPVS------------------SLSGGQKARLALAKLMMQKSNL 468
Cdd:TIGR04521 84 VGLvfqFPEHQLfeETVYkdiafgpKNLGLSEEEAEERVKealelvgldeeylerspfELSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 469 LILDEPTNHLDLNS-KEILEnaLID-----YPGTLLFVSHD 503
Cdd:TIGR04521 164 LILDEPTAGLDPKGrKEILD--LFKrlhkeKGLTVILVTHS 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-502 |
1.90e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNDVLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgSNVSVGYYDQEQ 402
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 -------------------------ANLTSS----KRVLNELWDEYPLQPEKEIRTILGnflftgdDVLKPvssLSGGQK 453
Cdd:PRK11160 412 lrqaisvvsqrvhlfsatlrdnlllAAPNASdealIEVLQQVGLEKLLEDDKGLNAWLG-------EGGRQ---LSGGEQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 454 ARLALAKLMMQKSNLLILDEPTNHLDLNS-KEILENALIDYPG-TLLFVSH 502
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITH 532
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
344-502 |
2.44e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ-------------------LLHGDVA------------FGSN 392
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQptggqvlldgvplvqydhhYLHRQVAlvgqepvlfsgsVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 393 VSVGYYDQEQANLTSSKRVLNElwDEYPLQPEKEIRTILGNflfTGddvlkpvSSLSGGQKARLALAKLMMQKSNLLILD 472
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANA--HDFIMEFPNGYDTEVGE---KG-------SQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|
gi 446524828 473 EPTNHLDLNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR00958 643 EATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
322-504 |
2.72e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.58 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 322 IEKQSGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQE 401
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD--------GQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QANLTSSKRVLNELWDEYPL------------------QPEKEIRTILgnflftgDDVLKPV----------SSLSGGQK 453
Cdd:PRK09452 78 ITHVPAENRHVNTVFQSYALfphmtvfenvafglrmqkTPAAEITPRV-------MEALRMVqleefaqrkpHQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL--------IdypgTLLFVSHDR 504
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELkalqrklgI----TFVFVTHDQ 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-485 |
2.90e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKD---VSIGY 70
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevtfnGPKSsqeAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETSLTIWDEMLtvfthlqqmetklrrleqeMGKEenFSNAATyeklladydqlQLDYKDQggYQyEADirSIL 150
Cdd:PRK10762 84 IHQELNLIPQLTIAENIF-------------------LGRE--FVNRFG-----------RIDWKKM--YA-EAD--KLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 SGLGFPVETHQtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL-DIETLTWL----EQYLQGYpgAILIVSHDryf 225
Cdd:PRK10762 127 ARLNLRFSSDK-LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFrvirELKSQGR--GIVYISHR--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 226 ldklVTQVYEISNK----ESRRFVGNySKYLDLKS-ALYEQEIKRyekqqdeiaKLEDfvqkniarasttkraqsrrkQL 300
Cdd:PRK10762 201 ----LKEIFEICDDvtvfRDGQFIAE-REVADLTEdSLIEMMVGR---------KLED--------------------QY 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 301 DRmelltrplgdsksasfhfdIEKQSGNDVLQVKDATigydeDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKL 380
Cdd:PRK10762 247 PR-------------------LDKAPGEVRLKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAL 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 381 QLLHGDVA-FGSNVS-------------------------VGYYDQEQANLTSskrvLNELWDEYPLQPEKEIRTILGNF 434
Cdd:PRK10762 303 PRTSGYVTlDGHEVVtrspqdglangivyisedrkrdglvLGMSVKENMSLTA----LRYFSRAGGSLKHADEQQAVSDF 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 435 --LF-----TGDdvlKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS-KEI 485
Cdd:PRK10762 379 irLFniktpSME---QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkKEI 434
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-222 |
3.20e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkdVSIgylaqntgLE 78
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGE------VSL--------VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 79 TSLTIWDEmltvfthlqQMETKLRrlEQEMG-KEENFSNAATYEKLlaDYDQLQLDYKDQGGYQYEADIRSILSGLGFPV 157
Cdd:PRK10584 72 QPLHQMDE---------EARAKLR--AKHVGfVFQSFMLIPTLNAL--ENVELPALLRGESSRQSRNGAKALLEQLGLGK 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 158 ETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL----QGYPGAILIVSHD 222
Cdd:PRK10584 139 RLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
344-518 |
3.31e-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: 57.44 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI-----VNKLQLL--HG----DVAFGSNVSV--------GY------- 397
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylPDSGSILvrHDggwvDLAQASPREIlalrrrtiGYvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 398 ------------------YDQEQAnLTSSKRVLN------ELWDEYPlqpekeirtilGNFlftgddvlkpvsslSGGQK 453
Cdd:COG4778 105 iprvsaldvvaepllergVDREEA-RARARELLArlnlpeRLWDLPP-----------ATF--------------SGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 454 ARLALAKLMMQKSNLLILDEPTNHLDLNSK----EILENALIDypGT-LLFVSHDRYFINRVTTTVVELS 518
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR--GTaIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-221 |
3.35e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 57.48 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KPKDvsigyLAQNTGLETSLTIWDEMLTVFTHL 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPIS-----QYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 95 QQ--METKLRRLEQEMGKE-ENFSNAATYEKLLADydqlqldykdqgGYQYEADIRSilsglgfpvethqttiSTLSGGQ 171
Cdd:cd03248 104 LQdnIAYGLQSCSFECVKEaAQKAHAHSFISELAS------------GYDTEVGEKG----------------SQLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 172 KTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSH 221
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-222 |
3.38e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPkdvsiGYLAQNTGLETSLT 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWDEMLTVFTHLQqmetklrrleqemgkeenfSNAAtyeklladydqLQLDYKDQGGYQYEADIRSILSGLGFpVETHQT 162
Cdd:PRK11248 76 FQNEGLLPWRNVQ-------------------DNVA-----------FGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK11248 125 YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTreqmQTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
331-503 |
3.47e-09 |
|
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: 57.26 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSvgyydqeqANLTSSKR 410
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--------TDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPLQPEKeirTILGNFLF-------TGDDVLKPVSS-----------------LSGGQKARLALAKLMMQKS 466
Cdd:cd03301 73 DIAMVFQNYALYPHM---TVYDNIAFglklrkvPKDEIDERVREvaellqiehlldrkpkqLSGGQRQRVALGRAIVREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 467 NLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHD 503
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKrlqqRLGTTTIYVTHD 190
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
347-502 |
3.52e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.67 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 347 EHVNMRLT----RGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKRVLNELWDEYPLQ 422
Cdd:PRK10771 12 HHLPMRFDltveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN--------GQDHTTTPPSRRPVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 423 PEKEIRTILGNFLFTG-----------DDVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-- 479
Cdd:PRK10771 84 SHLTVAQNIGLGLNPGlklnaaqreklHAIARQMgiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*
gi 446524828 480 LNSK--EILENALIDYPGTLLFVSH 502
Cdd:PRK10771 164 LRQEmlTLVSQVCQERQLTLLMVSH 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
355-509 |
3.52e-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: 55.84 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 355 RGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgsnvsvgyydqeqANLTSSKRVLNELWDEYPLQPEKEirtilgnf 434
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------------IDGEDILEEVLDQLLLIIVGGKKA-------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 435 lftgddvlkpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD---------LNSKEILENALIDYPGTLLFVSHDRY 505
Cdd:smart00382 60 ------------SGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEK 127
|
....
gi 446524828 506 FINR 509
Cdd:smart00382 128 DLGP 131
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
359-479 |
3.64e-09 |
|
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: 56.79 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 359 VALVGPNGIGKSTLLKSIVNKLQLLH--GDVAF-GSNVS-------VGYYDQEQAnltsskrVLNELwdeyplqpekeir 428
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLInGRPLDkrsfrkiIGYVPQDDI-------LHPTL------------- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 429 TILGNFLFTGddVLKpvsSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03213 98 TVRETLMFAA--KLR---GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
3.91e-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: 58.23 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGelshdggeIIKPkdvsigylaqNTGle 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNG--------LLKP----------TSG-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 79 tSLTIWDEMLTvfthlQQMETKLRRLEQEMGkeenfsnaatyekLLADYDQLQL----DYKD-------QGGYQYEAD-- 145
Cdd:TIGR04521 61 -TVTIDGRDIT-----AKKKKKLKDLRKKVG-------------LVFQFPEHQLfeetVYKDiafgpknLGLSEEEAEer 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 146 IRSILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSH 221
Cdd:TIGR04521 122 VKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgrKEILDLFKRLHKEKGLTVILVTH 201
|
.
gi 446524828 222 D 222
Cdd:TIGR04521 202 S 202
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-238 |
4.06e-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: 57.18 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 24 LEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIiKPKDVSIGYLAQNtglETSLTIWDEMLTVFTHLQqmetklrr 103
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-KVNDQSHTGLAPY---QRPVSMLFQENNLFAHLT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 104 LEQEMGKEENFS---NAATYEKLLADYDQLQLDykdqggyqyeaDIRSILSGlgfpvethqttisTLSGGQKTRLALGKL 180
Cdd:TIGR01277 87 VRQNIGLGLHPGlklNAEQQEKVVDAAQQVGIA-----------DYLDRLPE-------------QLSGGQRQRVALARC 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 181 LLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVYEISN 238
Cdd:TIGR01277 143 LVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQ 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-223 |
5.13e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVSIGYLAQNTGletsltiwdemlTVF 91
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDI---RTVTRASLRRNIA------------VVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 92 thlQQ-------METKLRrleqeMGKEEnfsnaATYEKLLADYDQLQ-LDY--KDQGGYQYEADIRSilsglgfpvethq 161
Cdd:PRK13657 416 ---QDaglfnrsIEDNIR-----VGRPD-----ATDEEMRAAAERAQaHDFieRKPDGYDTVVGERG------------- 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 162 ttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQgypGAILIVSHDR 223
Cdd:PRK13657 470 ---RQLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVK---AALDELMKGR 521
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
5.57e-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: 59.05 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY-----GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-----------IKPKDV 66
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 67 S-------IGYLAQNTGLETSLTIWDEmLTVFTHLQqmetklrrLEQEMGKEEnfsnaATYEKLLADYDqlqldykdqgg 139
Cdd:TIGR03269 359 GrgrakryIGILHQEYDLYPHRTVLDN-LTEAIGLE--------LPDELARMK-----AVITLKMVGFD----------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 140 yqyEADIRSILSGLGfpvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET--------LTWLEQYLQG 211
Cdd:TIGR03269 414 ---EEKAEEILDKYP----------DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITkvdvthsiLKAREEMEQT 480
|
250
....*....|....*
gi 446524828 212 YpgaiLIVSHDRYFL 226
Cdd:TIGR03269 481 F----IIVSHDMDFV 491
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-503 |
5.57e-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: 56.96 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS--------VGYYDQEQA---NLTSSKRVlnelw 416
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITnlppekrdISYVPQNYAlfpHMTVYKNI----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 417 dEYPL--------QPEKEIRTILGnflFTGDDVL---KPvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEI 485
Cdd:cd03299 93 -AYGLkkrkvdkkEIERKVLEIAE---MLGIDHLlnrKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|..
gi 446524828 486 LENALID----YPGTLLFVSHD 503
Cdd:cd03299 168 LREELKKirkeFGVTVLHVTHD 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-222 |
5.73e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTL-------LKIIAGELSHDGGEII-KPKDVSIGYLAQNTGletsltiwdeMLTV 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLiqninalLKPTTGTVTVDDITIThKTKDKYIRPVRKRIG----------MVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 91 FTHLQQMETKLRRlEQEMGKEeNFsnaatyeklladydqlQLDYKDQGGYQYEadirsILSGLGFPVETHQTTISTLSGG 170
Cdd:PRK13646 93 FPESQLFEDTVER-EIIFGPK-NF----------------KMNLDEVKNYAHR-----LLMDLGFSRDVMSQSPFQMSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 171 QKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-479 |
5.77e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDE--DPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVnklqllhgdvafgsnvsvGYYDQEQANL 405
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLN------------------GLLLPEAGTI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 TSSKRVLNE--LWDeyplqpekeIRTILGNFL------FTG----DDV---------------------LKPV------- 445
Cdd:PRK13635 65 TVGGMVLSEetVWD---------VRRQVGMVFqnpdnqFVGatvqDDVafglenigvpreemvervdqaLRQVgmedfln 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524828 446 ---SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13635 136 repHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
6.69e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KPKDVS---IGYLAQNTGLetsltiwdemltVFt 92
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILfdgKPIDYSrkgLMKLRESVGM------------VF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 93 hlQQMETKLrrleqemgkeenFSnAATYEKLLADYDQLQLDYKdqggyQYEADIRSILSGLGFPVETHQTTiSTLSGGQK 172
Cdd:PRK13636 89 --QDPDNQL------------FS-ASVYQDVSFGAVNLKLPED-----EVRKRVDNALKRTGIEHLKDKPT-HCLSFGQK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 173 TRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-480 |
6.82e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 57.05 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsivnklqLLHGDVAfGSNVSVGYYDQEQANLT---- 406
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLK-------LLTGELT-PSSGEVRLNGRPLAAWSpwel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 407 SSKR-VL---NEL----------------WDEYPLQPEKEIRTILGNflfTGDDVL--KPVSSLSGGQKARLALAKLMMQ 464
Cdd:COG4559 74 ARRRaVLpqhSSLafpftveevvalgrapHGSSAAQDRQIVREALAL---VGLAHLagRSYQTLSGGEQQRVQLARVLAQ 150
|
170 180
....*....|....*....|...
gi 446524828 465 -------KSNLLILDEPTNHLDL 480
Cdd:COG4559 151 lwepvdgGPRWLFLDEPTSALDL 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-222 |
7.54e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIikpkdvsigylaqntgletslTIWDEMLTvfthLQQME 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---------------------TIAGYHIT----PETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 99 TKLRRLEQEMGKEENFSNAATYEK-LLADydqLQLDYKDQGGYQYEADIRSI--LSGLGFPVETHQTTISTLSGGQKTRL 175
Cdd:PRK13641 78 KNLKKLRKKVSLVFQFPEAQLFENtVLKD---VEFGPKNFGFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 176 ALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHD 222
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-211 |
9.05e-09 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDV-------SIGYLAQNTGLETSlTI 83
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDGQDI---REVtldslrrAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMltvfthlqqmetklrRLEQEMGKEENFSNAAtyekLLADYDQLQLDYKDqgGYQYEADIRsilsGLgfpvethqtt 163
Cdd:cd03253 92 GYNI---------------RYGRPDATDEEVIEAA----KAAQIHDKIMRFPD--GYDTIVGER----GL---------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 164 isTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQG 211
Cdd:cd03253 137 --KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT----EREIQA 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-242 |
9.09e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIaGELSHDGGEIIKPKDVSigYLAQNtgletsltI 83
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVE--FFNQN--------I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMLTVfthlqqmeTKLRRLEQEMGKEEN------FSNAATYEKLLADYDQLQLDYKDQGGYQyEADIRSILSGlgfpv 157
Cdd:PRK14258 77 YERRVNL--------NRLRRQVSMVHPKPNlfpmsvYDNVAYGVKIVGWRPKLEIDDIVESALK-DADLWDEIKH----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 158 ETHQTTIStLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP----GAILIVSHDRYFLDKLVTQV 233
Cdd:PRK14258 143 KIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLSDFT 221
|
....*....
gi 446524828 234 YEISNKESR 242
Cdd:PRK14258 222 AFFKGNENR 230
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-475 |
9.29e-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: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANL-- 405
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLgi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 -----TSSkrVLNEL--WD--EYPLQPEKEIRTILGNFLfTG------DDVL----------KPVSSLSGGQKARLALAK 460
Cdd:COG4674 88 grkfqKPT--VFEELtvFEnlELALKGDRGVFASLFARL-TAeerdriEEVLetigltdkadRLAGLLSHGQKQWLEIGM 164
|
170
....*....|....*
gi 446524828 461 LMMQKSNLLILDEPT 475
Cdd:COG4674 165 LLAQDPKLLLLDEPV 179
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-221 |
9.85e-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: 55.96 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 24 LEVQTKDRIALVGRNGAGKSTLLKIIAG-ELSHDGGEIIKPKDVSIGYLAQNTgleTSLTIWDEmlTVFTHLQqmetklr 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPPADRP---VSMLFQEN--NLFAHLT------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 103 rLEQEMGkeenfsnaatyeklLADYDQLQLDYKDQGGyqyeadIRSILSGLGFPvETHQTTISTLSGGQKTRLALGKLLL 182
Cdd:cd03298 87 -VEQNVG--------------LGLSPGLKLTAEDRQA------IEVALARVGLA-GLEKRLPGELSGGERQRVALARVLV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524828 183 TKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSH 221
Cdd:cd03298 145 RDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-306 |
1.10e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpKDVSIGYLAQNTGLETSLT 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWDEMLTVFthlqqmetklrrleQEMGKEENFsnaatYEKLLADYDQLQLDYKDQGGYQYEADIrsILSGLGFPVEThQT 162
Cdd:PRK09700 84 IIYQELSVI--------------DELTVLENL-----YIGRHLTKKVCGVNIIDWREMRVRAAM--MLLRVGLKVDL-DE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 163 TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSH---------DRYFLDKLV 230
Cdd:PRK09700 142 KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHklaeirricDRYTVMKDG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 231 TQVY-----EISNKesrrfvgnyskylDLKSALYEQEIK-RYEKQQDEIAKLED---FVQKNIARAStTKRAQSRRKQLD 301
Cdd:PRK09700 222 SSVCsgmvsDVSND-------------DIVRLMVGRELQnRFNAMKENVSNLAHetvFEVRNVTSRD-RKKVRDISFSVC 287
|
....*
gi 446524828 302 RMELL 306
Cdd:PRK09700 288 RGEIL 292
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
345-479 |
1.12e-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: 56.13 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ---LLHGDVAF-GSNVS-------VGYYDQEQANL-------- 405
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFnGQPRKpdqfqkcVAYVRQDDILLpgltvret 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 -----------TSSKRVLNELWDEYPLqpeKEIR-TILGNFLFTGddvlkpvssLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:cd03234 102 ltytailrlprKSSDAIRKKRVEDVLL---RDLAlTRIGGNLVKG---------ISGGERRRVSIAVQLLWDPKVLILDE 169
|
....*.
gi 446524828 474 PTNHLD 479
Cdd:cd03234 170 PTSGLD 175
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-502 |
1.13e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.58 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 326 SGNDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI--VNKLQ---------LLHGDVAFGSNVS 394
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgarvegeiLLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 -------VGY------------YDqeqaNLT--------SSKRVLNE----------LWDEYplqpekeirtilgnflft 437
Cdd:COG1117 87 vvelrrrVGMvfqkpnpfpksiYD----NVAyglrlhgiKSKSELDEiveeslrkaaLWDEV------------------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 438 gDDVLK-PVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENaLI-----DYpgTLLFVSH 502
Cdd:COG1117 145 -KDRLKkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEE-LIlelkkDY--TIVIVTH 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-514 |
1.14e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 21 NIKLEVQTKDRIALVGRNGAGKS----TLLKII---AGELSHDG-------GEIIKPKDVSIGYLAQNTGLETSLtIWDE 86
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKmllrrrsRQVIELSEQSAAQMRHVRGADMAM-IFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 87 MLT----VFTHLQQMETKLRrLEQEMGKEENFSNAatyEKLLadyDQLQLdykdqggyqyeADIRSILSGlgFPvetHQt 162
Cdd:PRK10261 113 PMTslnpVFTVGEQIAESIR-LHQGASREEAMVEA---KRML---DQVRI-----------PEAQTILSR--YP---HQ- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 163 tistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHDryfldklVTQVYEISN 238
Cdd:PRK10261 169 ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHD-------MGVVAEIAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 239 kesRRFVGNYSKYLDLKSAlyeQEIKRYEKQQDEIAKLEDFVQKNIARASTTKRaqsrrkqldRMELLTRPLGDSKSAsf 318
Cdd:PRK10261 238 ---RVLVMYQGEAVETGSV---EQIFHAPQHPYTRALLAAVPQLGAMKGLDYPR---------RFPLISLEHPAKQEP-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 319 hfDIEKQS---GNDVLQVKDATIGYD-----------EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLH 384
Cdd:PRK10261 301 --PIEQDTvvdGEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 385 GDVAFGSnvsvgyydQEQANLTSSK-----RVLNELW-DEY-PLQPEKEI-----RTILGNFLFTGDDVLKPVSSL---- 448
Cdd:PRK10261 379 GEIIFNG--------QRIDTLSPGKlqalrRDIQFIFqDPYaSLDPRQTVgdsimEPLRVHGLLPGKAAAARVAWLlerv 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 449 --------------SGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTL----LFVSHDRYFINRV 510
Cdd:PRK10261 451 gllpehawryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAVVERI 530
|
....
gi 446524828 511 TTTV 514
Cdd:PRK10261 531 SHRV 534
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
344-510 |
1.36e-08 |
|
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: 56.35 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgSNVSVGYYDQEQANltSSKRVLNELWDEYP--L 421
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-RGQDLYQLDRKQRR--AFRRDVQLVFQDSPsaV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 422 QPEKEIRTILGNFL-----------------------FTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:TIGR02769 102 NPRMTVRQIIGEPLrhltsldeseqkariaelldmvgLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 479 DL-NSKEILE--NALIDYPGT-LLFVSHD----RYFINRV 510
Cdd:TIGR02769 182 DMvLQAVILEllRKLQQAFGTaYLFITHDlrlvQSFCQRV 221
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
164-238 |
1.49e-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: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 164 ISTLSGGQKT------RLALGKLLLTKPDLLILDEPTNHLDIETLTW-----LEQYLQGYPGAILIVSHDRYFLDKLvTQ 232
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA-DH 191
|
....*.
gi 446524828 233 VYEISN 238
Cdd:cd03240 192 IYRVEK 197
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
344-490 |
1.57e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.40 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ-----LLH-GDVAFGSNVSVGYYDQEQANLtsskrVLNELWD 417
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEpsegkIKHsGRISFSSQFSWIMPGTIKENI-----IFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 418 EYPLQ---------------PEKEiRTILGNFLFTgddvlkpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-N 481
Cdd:cd03291 126 EYRYKsvvkacqleeditkfPEKD-NTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVfT 194
|
....*....
gi 446524828 482 SKEILENAL 490
Cdd:cd03291 195 EKEIFESCV 203
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
361-504 |
1.78e-08 |
|
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: 56.73 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 361 LVGPNGIGKSTLLKSIVNKLQLLHGDVAFG----SNV-----SVGYYDQEQA---NLTSSKRVlnelwdEYPLQPEKE-- 426
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDgedvTNVpphlrHINMVFQSYAlfpHMTVEENV------AFGLKMRKVpr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 427 ------IRTILGNFLFTGDDVLKPvSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG----T 496
Cdd:TIGR01187 75 aeikprVLEALRLVQLEEFADRKP-HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlgiT 153
|
....*...
gi 446524828 497 LLFVSHDR 504
Cdd:TIGR01187 154 FVFVTHDQ 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-479 |
1.85e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDV---------------AFGSNVS 394
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYYDQEQ--------ANLTSSKRVLNelwdeyplQPEKEI-RTIlgnflftgDDVL----------KPVSSLSGGQKAR 455
Cdd:PRK13638 81 TVFQDPEQqifytdidSDIAFSLRNLG--------VPEAEItRRV--------DEALtlvdaqhfrhQPIQCLSHGQKKR 144
|
170 180
....*....|....*....|....
gi 446524828 456 LALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLD 168
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
1.93e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.69 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKI------------IAGELSHDGGEIIKpKDVS- 67
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFK-MDVIe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 ----IGYLAQNTGLETSLTIWDEMltvfthlqQMETKLRRLEQemgkeenfSNAATYEKLLADYDQLQL--DYKDQggyq 141
Cdd:PRK14247 80 lrrrVQMVFQIPNPIPNLSIFENV--------ALGLKLNRLVK--------SKKELQERVRWALEKAQLwdEVKDR---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 142 yeadirsilsgLGFPVethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIV 219
Cdd:PRK14247 140 -----------LDAPA-------GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLV 201
|
..
gi 446524828 220 SH 221
Cdd:PRK14247 202 TH 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-201 |
2.00e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD----------------GGEI---IKP 63
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqrEGRLardIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 64 KDVSIGYLAQNTGLETSLTIWDEMLtvfthlqqmetklrrleqeMGKeenFSNAATYEKLLADYDQLQldykDQGGYQye 143
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVL-------------------IGA---LGSTPFWRTCFSWFTREQ----KQRALQ-- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 144 adirsILSGLGFPVETHQTtISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:PRK09984 136 -----ALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
340-479 |
2.10e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.58 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 340 YDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsnvsvgyyDQEQANLTSSKRVLNELWDEY 419
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--------EKRMNDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 420 PLQP------------------EKEIRTILGNflftGDDVL--------KPvSSLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:PRK11000 85 ALYPhlsvaenmsfglklagakKEEINQRVNQ----VAEVLqlahlldrKP-KALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
....*.
gi 446524828 474 PTNHLD 479
Cdd:PRK11000 160 PLSNLD 165
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
346-503 |
2.30e-08 |
|
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: 55.16 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVafgsnvsvgYYDQEQANLTSSKRVLneLWDEYPLQPEK 425
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV---------ILEGKQITEPGPDRMV--VFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 426 EIRTilgNFLFTGDDVL--------------------------KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:TIGR01184 70 TVRE---NIALAVDRVLpdlskserraiveehialvglteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*...
gi 446524828 480 LNSKEILENALI----DYPGTLLFVSHD 503
Cdd:TIGR01184 147 ALTRGNLQEELMqiweEHRVTVLMVTHD 174
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-234 |
2.66e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNtgLETSLT 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL--------FERQS--IKKDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWDEMLTVFTHLQQMETKLrRLEQEMGKEENFSNAATyekllaDYDQLqldykdqggyqyeADIRSILSGLGFPVethqt 162
Cdd:PRK13540 71 TYQKQLCFVGHRSGINPYL-TLRENCLYDIHFSPGAV------GITEL-------------CRLFSLEHLIDYPC----- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 163 tiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD---IETLTWLEQYLQGYPGAILIVSHDRYFLDKLVTQVY 234
Cdd:PRK13540 126 --GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEY 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-201 |
2.92e-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: 54.34 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAE--TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIGYLaqnTGLETS 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPL---EDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIWDEMLTVFthlqqMETkLRrleqemgkeenfSNAATYEKlladYDQLQLdykdqggyqYEAdIRSILSGLgfpveth 160
Cdd:cd03369 84 LTIIPQDPTLF-----SGT-IR------------SNLDPFDE----YSDEEI---------YGA-LRVSEGGL------- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 161 qttisTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03369 125 -----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-514 |
3.35e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQL-----LHGDVA-FGSNV-------- 393
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRlFGRNIyspdvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 394 ----SVGY-------------YDQ-----EQANLTSSKRVLNE----------LWDEyplqpekeIRTILGNFlftgddv 441
Cdd:PRK14267 82 evrrEVGMvfqypnpfphltiYDNvaigvKLNGLVKSKKELDErvewalkkaaLWDE--------VKDRLNDY------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 442 lkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYpgTLLFVSHDRYFINRVTTTV 514
Cdd:PRK14267 147 ---PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFelkkEY--TIVLVTHSPAQAARVSDYV 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-198 |
3.55e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSH---------DGGEIIKPKDVSIGYLAQNTGLETSLTIWDEM 87
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnftgtilaNNRKPTKQILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 88 LTVfthlqqmetKLRRLEQEMGKEENFSNAatyeklladydqlqldykdqggyqyeadiRSILSGLGFP----VETHQTT 163
Cdd:PLN03211 162 VFC---------SLLRLPKSLTKQEKILVA-----------------------------ESVISELGLTkcenTIIGNSF 203
|
170 180 190
....*....|....*....|....*....|....*
gi 446524828 164 ISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
331-479 |
3.90e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.85 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNmrltRGDSVALVGPNGIGKSTLLkSIVNKLQLLHGDVAFG----SNVSV-------GYYD 399
Cdd:COG4138 1 LQLNDVAVAGRLGPISAQVN----AGELIHLIGPNGAGKSTLL-ARMAGLLPGQGEILLNgrplSDWSAaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 QEQ-------------------ANLTSSKRVLNELWDEYPLqpekeirtilgnflftgDDVL-KPVSSLSGGQKARLALA 459
Cdd:COG4138 76 QQQsppfampvfqylalhqpagASSEAVEQLLAQLAEALGL-----------------EDKLsRPLTQLSGGEWQRVRLA 138
|
170 180
....*....|....*....|....*..
gi 446524828 460 KLMMQ-------KSNLLILDEPTNHLD 479
Cdd:COG4138 139 AVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-490 |
4.20e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.15 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDED-PIIEHVNMRLTRGDSVALVGPNGIGKSTLLksivnklqllhgdvafgsNVSVGYYDQEQANLTSSKR 410
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLI------------------NLLMRFYDPQKGQILIDGI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELwdeyplqPEKEIRTILG-----NFLFTG---------------DDVLKPV------------------------S 446
Cdd:cd03254 66 DIRDI-------SRKSLRSMIGvvlqdTFLFSGtimenirlgrpnatdEEVIEAAkeagahdfimklpngydtvlgengG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEAL 182
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
331-503 |
4.36e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATigydEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLlHGDVAF-GSNVSV----------GYYD 399
Cdd:PRK03695 1 MQLNDVA----VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEAwsaaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 QEQ-------------------ANLTSSKRVLNELwdeyplqpekeirtilGNFLFTGDDVLKPVSSLSGGQKARLALAK 460
Cdd:PRK03695 76 QQQtppfampvfqyltlhqpdkTRTEAVASALNEV----------------AEALGLDDKLGRSVNQLSGGEWQRVRLAA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 461 LMMQ-------KSNLLILDEPTNHLDLNSKEILE---NALIDYPGTLLFVSHD 503
Cdd:PRK03695 140 VVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
331-515 |
4.63e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 54.57 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLQLLHGDVAF-GSN--------------- 392
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFkGQDllelepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 393 -----------VSVGYYDQEQANLTSSKRVLNELWDeypLQPEKEIRTIL------GNFLFTGDDVlkpvsSLSGGQKAR 455
Cdd:TIGR01978 81 lafqypeeipgVSNLEFLRSALNARRSARGEEPLDL---LDFEKLLKEKLalldmdEEFLNRSVNE-----GFSGGEKKR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 456 LALAKLMMQKSNLLILDEPTNHLDLNS-KEILE--NALIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDAlKIVAEgiNRLREPDRSFLIITHYQRLLNYIKPDYV 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-198 |
4.69e-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: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD---------GGEIIKPKDVSI--GYLAQNTGLETSLTIwD 85
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgsgsvllNGMPIDAKEMRAisAYVQQDDLFIPTLTV-R 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 86 EMLTVFTHLqqmetklrRLEQEMGKEEnfsnaatyeKLLADYDQLQldykdQGGYQYEADIRsilsgLGFPvethqTTIS 165
Cdd:TIGR00955 118 EHLMFQAHL--------RMPRRVTKKE---------KRERVDEVLQ-----ALGLRKCANTR-----IGVP-----GRVK 165
|
170 180 190
....*....|....*....|....*....|...
gi 446524828 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:TIGR00955 166 GLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
326-503 |
4.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.81 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 326 SGNDVLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsIVNKLQLLHGDVAFGSNVS--------- 394
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISK-LINGLLLPDDNPNSKITVDgitltaktv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 ------VGYYDQEQANLTSSKRVLNELwdEYPLQ----PEKEIRTILgnflftgDDVLKPV----------SSLSGGQKA 454
Cdd:PRK13640 80 wdirekVGIVFQNPDNQFVGATVGDDV--AFGLEnravPRPEMIKIV-------RDVLADVgmldyidsepANLSGGQKQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKE----ILENALIDYPGTLLFVSHD 503
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEqilkLIRKLKKKNNLTVISITHD 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-479 |
5.81e-08 |
|
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: 53.42 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 339 GYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQL---LHGDVAFGsnvsvGYYDQEQANLTSSKRVLNEL 415
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYN-----GIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 416 WDEYPlqPEKEIR-TILGNFLFTGDDVlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:cd03233 91 EDVHF--PTLTVReTLDFALRCKGNEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-267 |
7.24e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.01 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII------------AGELSHDGGEIIKPKDVS--- 67
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 ---IGYLAQNTGlETSLTIWDemlTVFTHLQQMETKLRRLEQEmGKEENFSNAATYEKLladydqlqldyKDQggyqyea 144
Cdd:PRK14239 85 rkeIGMVFQQPN-PFPMSIYE---NVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEV-----------KDR------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 145 dirsilsglgfpveTHQTTIStLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:PRK14239 142 --------------LHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446524828 223 ryfldklVTQVYEISNKESRRFVGNYSKYLDLKSALYEQEIKRYE 267
Cdd:PRK14239 207 -------MQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETE 244
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-201 |
7.56e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 53.70 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpKDVSIGYLAQNTGLetsltiwdemltv 90
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVDI---RDLNLRWLRSQIGL------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 91 fthLQQmETKLrrleqemgkeenFSNAATYEKLLADYDQLQLDYKDQGGyqyEADIRSILSGLgfPvETHQTTI----ST 166
Cdd:cd03249 82 ---VSQ-EPVL------------FDGTIAENIRYGKPDATDEEVEEAAK---KANIHDFIMSL--P-DGYDTLVgergSQ 139
|
170 180 190
....*....|....*....|....*....|....*
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-199 |
8.39e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIA-------GELSHDGGEIIK--PKDVS--IGYLAQNTGLETSL 81
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIQHyaSKEVArrIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 TIwDEMLT--VFTHlQQMETKLRrleqemgKEEnfsnaatyeklladydqlqldykdqggyqyEADIRSILSGLGFPVET 159
Cdd:PRK10253 97 TV-QELVArgRYPH-QPLFTRWR-------KED------------------------------EEAVTKAMQATGITHLA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 160 HQtTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK10253 138 DQ-SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-486 |
9.26e-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: 53.26 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 341 DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIV------NKLQLLHG-DVAFGSNVS----VGYYDQEQANLTSSK 409
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQrfyvpeNGRVLVDGhDLALADPAWlrrqVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 RVLNELWDE-YPLQPEKEIRTILGNFLFT-------GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:cd03252 93 RDNIALADPgMSMERVIEAAKLAGAHDFIselpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
....*
gi 446524828 482 SKEIL 486
Cdd:cd03252 173 SEHAI 177
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-198 |
9.63e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQ 73
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlshvPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLetsltiwdemltvFTHlqqmetklrrleqeMGKEENFSNAATYEKLLADYDQLQLdykdqggyqyeADIRSILSGL 153
Cdd:PRK11607 99 SYAL-------------FPH--------------MTVEQNIAFGLKQDKLPKAEIASRV-----------NEMLGLVHMQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524828 154 GFPV-ETHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11607 141 EFAKrKPHQ-----LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
330-479 |
9.71e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvnkLQLLHGDV-------------AFGSNVSVG 396
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRML---LGLTHPDAgsislcgepvpsrARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 Y---YDQEQANLTSSKRVLneLWDEYPLQPEKEIRTI---LGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:PRK13537 84 VvpqFDNLDPDFTVRENLL--VFGRYFGLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
....*....
gi 446524828 471 LDEPTNHLD 479
Cdd:PRK13537 162 LDEPTTGLD 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-221 |
1.02e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVSIgylaQNT--GLETS 80
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlIDGQEMRF----ASTtaALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 81 LTIwdemltVFTHLQqmetklrrLEQEMGKEENFsnaatyekLLAdydqlQLDYK----DQGGYQYEAdiRSILSGLGFP 156
Cdd:PRK11288 81 VAI------IYQELH--------LVPEMTVAENL--------YLG-----QLPHKggivNRRLLNYEA--REQLEHLGVD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 157 VEThQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSH 221
Cdd:PRK11288 132 IDP-DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
447-515 |
1.11e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG----TLLFVSHDRYFINRVTTTVV 515
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAHRIASIKRSDKIVV 1430
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-201 |
1.12e-07 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 53.26 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 13 YGAET--ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------IGYLAQNTGLeT 79
Cdd:cd03252 10 YKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlVDGHDLAladpawlrrqVGVVLQENVL-F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 80 SLTIWDEMltvftHLQQMETKLRRLEqemgkeENFSNAATYEKLLadydQLQLDYKDQGGYQyeadirsilsGLGfpvet 159
Cdd:cd03252 89 NRSIRDNI-----ALADPGMSMERVI------EAAKLAGAHDFIS----ELPEGYDTIVGEQ----------GAG----- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524828 160 hqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03252 139 -------LSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
346-502 |
1.20e-07 |
|
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: 52.76 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQllhgdvAFGSNVSVGYYDQEQANLtSSKRVLNELWDEYPLQPEK 425
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE------PDAGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 426 EIRTILGNF---------------------LFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKE 484
Cdd:cd03266 94 TARENLEYFaglyglkgdeltarleeladrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180
....*....|....*....|.
gi 446524828 485 ILENALIDYPG---TLLFVSH 502
Cdd:cd03266 174 ALREFIRQLRAlgkCILFSTH 194
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-222 |
1.30e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 52.32 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 32 IALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWDEMLTV------FTHLQQMETKLRR-- 103
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYRIerrqgeFAEFLEAKPSERKea 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 104 LEQEMGKEenfsnaaTYEKLLADYDQLQLDYKDQ-----GGYQYEADIRSILSGLGfpvethqtTISTLSGGQKTRLALG 178
Cdd:COG0419 106 LKRLLGLE-------IYEELKERLKELEEALESAleelaELQKLKQEILAQLSGLD--------PIETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 179 KLLltkpdLLILDepTNHLDIETLTWLEQYLQgypgAILIVSHD 222
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-502 |
1.31e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.51 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSvgyydQEQANLTS-SKRV-LNELWDEYPLQ 422
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdGVDIT-----DKKVKLSDiRKKVgLVFQYPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 423 PE---KEIRTILGNFLFTGDDVLKPVSS-------------------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK13637 98 EEtieKDIAFGPINLGLSEEEIENRVKRamnivgldyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180
....*....|....*....|....*...
gi 446524828 481 NSK-EILEnaLI-----DYPGTLLFVSH 502
Cdd:PRK13637 178 KGRdEILN--KIkelhkEYNMTIILVSH 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-503 |
1.49e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.94 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF------GSNVSVGYYDQ 400
Cdd:COG4525 4 LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 EQAnLTSSKRVLNELwdEYPLQ----PEKEIRTILGNFL-------FTGddvlKPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:COG4525 84 KDA-LLPWLNVLDNV--AFGLRlrgvPKAERRARAEELLalvgladFAR----RRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524828 470 ILDEPTNHLDLNSKEILENALIDYPG----TLLFVSHD 503
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQrtgkGVFLITHS 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-479 |
1.51e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 341 DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGS----------------------------- 391
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykrakyigrvfqdpmmgtaps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 392 -----NVSVGYYDQEQANLtsSKRVLNELWDEYplqpeKEIRTILGNFLftgDDVLK-PVSSLSGGQkaRLALAKLM--M 463
Cdd:COG1101 97 mtieeNLALAYRRGKRRGL--RRGLTKKRRELF-----RELLATLGLGL---ENRLDtKVGLLSGGQ--RQALSLLMatL 164
|
170
....*....|....*.
gi 446524828 464 QKSNLLILDEPTNHLD 479
Cdd:COG1101 165 TKPKLLLLDEHTAALD 180
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
325-514 |
1.61e-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: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNdvLQVKDATIGYDED-PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDV---------------- 387
Cdd:PRK10790 337 QSGR--IDIDNVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsvlr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 388 ---------------AFGSNVSVGYYDQEQANLTSSKRV-LNELWDEYPlqpeKEIRTILGnflftgddvlKPVSSLSGG 451
Cdd:PRK10790 415 qgvamvqqdpvvladTFLANVTLGRDISEEQVWQALETVqLAELARSLP----DGLYTPLG----------EQGNNLSVG 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 452 QKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL--IDYPGTLLFVSHdryfinRVTTTV 514
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALaaVREHTTLVVIAH------RLSTIV 539
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-198 |
1.65e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI---------IKPKDVSIGY 70
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrvvneLEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLetsltiWDEMlTVFthlQQME--TKLRRleqeMGKEE---NFSNAATYEKLladyDQLqLDYKdqggyqyead 145
Cdd:PRK11650 81 VFQNYAL------YPHM-SVR---ENMAygLKIRG----MPKAEieeRVAEAARILEL----EPL-LDRK---------- 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 146 irsilsglgfPVEthqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11650 132 ----------PRE--------LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
332-519 |
1.75e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYD-EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLlksiVNKLQLLHgDVAFGSnVSVGYYDQEQANLTSSKR 410
Cdd:PRK13657 336 EFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRVF-DPQSGR-ILIDGTDIRTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNELWDEYPL------------QP---EKEIRTILG-----NFLFTGDDVLKPV-----SSLSGGQKARLALAKLMMQK 465
Cdd:PRK13657 410 NIAVVFQDAGLfnrsiednirvgRPdatDEEMRAAAEraqahDFIERKPDGYDTVvgergRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 466 SNLLILDEPTNHLDLNSKEILENALIDypgtllfVSHDRyfinrvTTTVV--ELST 519
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDE-------LMKGR------TTFIIahRLST 532
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-210 |
1.78e-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: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET-ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII---KP-KDVSIGYLAQNTGL- 77
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgRPlSSLSHSVLRQGVAMv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 78 -ETSLTIWDEMLTVFThlqqmetkLRRleqemgkeeNFSNAATYEKLladyDQLQLdykdqggyqyeAD-IRSILSGLGF 155
Cdd:PRK10790 421 qQDPVVLADTFLANVT--------LGR---------DISEEQVWQAL----ETVQL-----------AElARSLPDGLYT 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 156 PVETHQttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQ 210
Cdd:PRK10790 469 PLGEQG---NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT----EQAIQ 516
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
1.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.17 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigYLAQNtglE 78
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE--------WIFKD---E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 79 TSLTIWDEMLTVFTHLQQMETKLRRLEQ------EMGKEENFSN----AATYEKLLAdYDQLQLDYKDQGGYQYEADIRS 148
Cdd:PRK13651 72 KNKKKTKEKEKVLEKLVIQKTRFKKIKKikeirrRVGVVFQFAEyqlfEQTIEKDII-FGPVSMGVSKEEAKKRAAKYIE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 149 ILsglGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQ-YLQGypGAILIVSHD 222
Cdd:PRK13651 151 LV---GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNlNKQG--KTIILVTHD 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
353-503 |
1.92e-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: 51.21 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 353 LTRGDSVALVGPNGIGKSTLLKSIvnklqllhGDVAFGSNVSVGYYDQEQANLTSSkrvlnelwdeyplQPEKEIRTIlg 432
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGVKAGCIVA-------------AVSAELIFT-- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 433 nflftgddvlkpVSSLSGGQKARLALAKLM----MQKSNLLILDEPTNHLDLNSKEILENALIDY---PGTLLFVSHD 503
Cdd:cd03227 75 ------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHL 140
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-503 |
1.93e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.17 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNklqLLHGDvafGSNVSV-GY--YDQEQANLtssKR---VL---NELW 416
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---ILVPT---SGEVRVlGYvpFKRRKEFA---RRigvVFgqrSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 417 DEYPLQ------------PEKEIRTILGNF--LFTGDDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:COG4586 109 WDLPAIdsfrllkaiyriPDAEYKKRLDELveLLDLGELLdTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180
....*....|....*....|....*.
gi 446524828 482 SKEILENALIDY----PGTLLFVSHD 503
Cdd:COG4586 189 SKEAIREFLKEYnrerGTTILLTSHD 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
155-510 |
2.07e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.92 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 155 FPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQyLQGYPG-AILIVSHDryfLDkL 229
Cdd:COG4172 153 YP---HQ-----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaQILDLLKD-LQRELGmALLLITHD---LG-V 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 230 VtqvyeisnkesRRFVgnyskyldlksalyeqeikryekqqDEIAkledfVQKN--IARASTTKR--AQSR----RKQLD 301
Cdd:COG4172 220 V-----------RRFA-------------------------DRVA-----VMRQgeIVEQGPTAElfAAPQhpytRKLLA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 302 -RMELLTRPLGDSKSAsfhfdiekqsgndVLQVKDATIGYdedPI--------------IEHVNMRLTRGDSVALVGPNG 366
Cdd:COG4172 259 aEPRGDPRPVPPDAPP-------------LLEARDLKVWF---PIkrglfrrtvghvkaVDGVSLTLRRGETLGLVGESG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 367 IGKSTLLKSIvnkLQLLH--GDVAFGsnvsvgyyDQEQANLTSS------KRV----------LN------ELWDEyPL- 421
Cdd:COG4172 323 SGKSTLGLAL---LRLIPseGEIRFD--------GQDLDGLSRRalrplrRRMqvvfqdpfgsLSprmtvgQIIAE-GLr 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 422 ---------QPEKEIRTILgnflftgDDV-LKPVS------SLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLnS--K 483
Cdd:COG4172 391 vhgpglsaaERRARVAEAL-------EEVgLDPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SvqA 462
|
410 420 430
....*....|....*....|....*....|....*
gi 446524828 484 EILEnALID----YPGTLLFVSHD----RYFINRV 510
Cdd:COG4172 463 QILD-LLRDlqreHGLAYLFISHDlavvRALAHRV 496
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-542 |
2.21e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 329 DVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsIVNKLQLLH------GDV--------------- 387
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYpearvsGEVyldgqdifkmdviel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 388 -----------------AFGSNVSVGYydqEQANLTSSKRVLNE----------LWDEyplqpekeirtilgnflfTGDD 440
Cdd:PRK14247 81 rrrvqmvfqipnpipnlSIFENVALGL---KLNRLVKSKKELQErvrwalekaqLWDE------------------VKDR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 441 VLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLY 219
|
250 260
....*....|....*....|....
gi 446524828 519 TEGAQEYLGDYDYYVEKKNEMIER 542
Cdd:PRK14247 220 KGQIVEWGPTREVFTNPRHELTEK 243
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
331-517 |
2.58e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSivnkLQLLhgDVAFGSNVSVG--YYDQEQANLTSS 408
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRV----LNLL--ETPDSGQLNIAghQFDFSQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 KRVLNE----LWDEYPLQPEkeiRTILGNFLFTGDDVLKPVSS-------------------------LSGGQKARLALA 459
Cdd:COG4161 77 IRLLRQkvgmVFQQYNLWPH---LTVMENLIEAPCKVLGLSKEqarekamkllarlrltdkadrfplhLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 460 KLMMQKSNLLILDEPTNHLDLN-SKEILE--NALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEiTAQVVEiiRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
330-479 |
2.68e-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: 51.92 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQ-------LLHGDVAFGSNVSVGYYDQE- 401
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLEepdsgtiTVDGEDLTDSKKDINKLRRKv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 -----QANLTSSKRVLNELWdEYPLQ----PEKEIRTIlgnflftGDDVLKPV----------SSLSGGQKARLALAK-L 461
Cdd:COG1126 80 gmvfqQFNLFPHLTVLENVT-LAPIKvkkmSKAEAEER-------AMELLERVgladkadaypAQLSGGQQQRVAIARaL 151
|
170
....*....|....*...
gi 446524828 462 MMqKSNLLILDEPTNHLD 479
Cdd:COG1126 152 AM-EPKVMLFDEPTSALD 168
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-200 |
2.89e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 52.11 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHdGGEIIKPKDVSIGYL----- 71
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRV-GGEEIRLKPDRDGELvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 72 AQNTGLETSLT-------IWDEMlTVfthLQQ-METKLRRLEqeMGKEENFSNAatyEKLLADYdqlqldykdqggyqye 143
Cdd:COG4598 88 RQLQRIRTRLGmvfqsfnLWSHM-TV---LENvIEAPVHVLG--RPKAEAIERA---EALLAKV---------------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 144 adirsilsGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:COG4598 143 --------GLA---DKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
328-503 |
3.20e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.43 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGY-DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLksivnklqlLHGDvafgsnvsvGYYDQEQANLT 406
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLL---------LHLN---------GIYLPQRGRVK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 407 SSKRVLNElwdeyplQPEKEIRTILG------------------------NFLFTGDDVL-----------------KPV 445
Cdd:PRK13647 64 VMGREVNA-------ENEKWVRSKVGlvfqdpddqvfsstvwddvafgpvNMGLDKDEVErrveealkavrmwdfrdKPP 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 446 SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILE---NALIDYPGTLLFVSHD 503
Cdd:PRK13647 137 YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMeilDRLHNQGKTVIVATHD 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-198 |
3.66e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.31 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDG-----GEIIKPKDVS-----IGYLAQNTGLETSlTIWDE 86
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGslkinGIELRELDPEswrkhLSWVGQNPQLPHG-TLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 87 MLtvfthlqqmetklrrleqeMGKEEnfsnaATYEKLLADYDQlqldykdqggyqyeADIRSILS----GLGFPVETHQt 162
Cdd:PRK11174 443 VL-------------------LGNPD-----ASDEQLQQALEN--------------AWVSEFLPllpqGLDTPIGDQA- 483
|
170 180 190
....*....|....*....|....*....|....*.
gi 446524828 163 tiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11174 484 --AGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-504 |
4.03e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.39 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 340 YDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS--------VGYYDQEQA------- 403
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVSrlhardrkVGFVFQHYAlfrhmtv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 --NLTSSKRVLnelwdeyplqPEKE------IRTILGNFLftgdDVLK--------PvSSLSGGQKARLALAKLMMQKSN 467
Cdd:PRK10851 92 fdNIAFGLTVL----------PRRErpnaaaIKAKVTQLL----EMVQlahladryP-AQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 468 LLILDEPTNHLDLN-SKEI---LENALIDYPGTLLFVSHDR 504
Cdd:PRK10851 157 ILLLDEPFGALDAQvRKELrrwLRQLHEELKFTSVFVTHDQ 197
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-227 |
4.09e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.61 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 17 TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSH--DGGEII-KPKDVsigylaqnTGLETsltiwDE--MLTVF 91
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILlDGEDI--------LELSP-----DEraRAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 92 THLQQ--------METKLRRLEQEMGKEEnfSNAATYEKLLADY-DQLQLD--YKDqggyqyeadiRSILSGLgfpveth 160
Cdd:COG0396 81 LAFQYpveipgvsVSNFLRTALNARRGEE--LSAREFLKLLKEKmKELGLDedFLD----------RYVNEGF------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 161 qttistlSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGY--PG-AILIVSHDRYFLD 227
Cdd:COG0396 142 -------SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDrGILIITHYQRILD 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
325-479 |
4.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNDVLQVKDATIGYD---EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ-------LLHGDVAFGSNVS 394
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaetssvVIRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYYDQEQAN-LTSSKRVLNELW---DEYPLQPEKEirtilgnfLFTGDDVLKPVS---SLSGGQKARLALAKLMMQKSN 467
Cdd:PLN03232 689 WIFNATVRENiLFGSDFESERYWraiDVTALQHDLD--------LLPGRDLTEIGErgvNISGGQKQRVSMARAVYSNSD 760
|
170
....*....|..
gi 446524828 468 LLILDEPTNHLD 479
Cdd:PLN03232 761 IYIFDDPLSALD 772
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-201 |
4.19e-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: 53.38 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSigYLAQNTGLETSlTIWDEMLTVFTHlqqM 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--FSPQTSWIMPG-TIKDNIIFGLSY---D 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 98 ETKLRRLEQEMGKEENFSnaatyekLLADYDQLQLDykdQGGYqyeadirsilsglgfpvethqttisTLSGGQKTRLAL 177
Cdd:TIGR01271 515 EYRYTSVIKACQLEEDIA-------LFPEKDKTVLG---EGGI-------------------------TLSGGQRARISL 559
|
170 180
....*....|....*....|....
gi 446524828 178 GKLLLTKPDLLILDEPTNHLDIET 201
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
344-514 |
5.07e-07 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 51.04 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKsIVNKLQL-LHGDVA-FGSNVS-------------VGYYDQeQANLTSS 408
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLvDGTDLTllsgkelrkarrrIGMIFQ-HFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 409 KRVLNELwdEYPLQ----PEKEIR---TILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:cd03258 97 RTVFENV--ALPLEiagvPKAEIEervLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524828 482 S-KEILE-----NALIDYpgTLLFVSHDRYFINRVTTTV 514
Cdd:cd03258 175 TtQSILAllrdiNRELGL--TIVLITHEMEVVKRICDRV 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-479 |
5.83e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.62 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDP-IIEHVNMRLTRGDSVALVGPNGIGKSTLL-------------------------KSIVNKLQ-- 381
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgevlikgepikydkKSLLEVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 382 --------------LLHGDVAFGS-NVSVGYYDQEQANLTSSKRVLNELWDEyplqpekeirtilgnflftgddvlKPVS 446
Cdd:PRK13639 81 givfqnpddqlfapTVEEDVAFGPlNLGLSKEEVEKRVKEALKAVGMEGFEN------------------------KPPH 136
|
170 180 190
....*....|....*....|....*....|...
gi 446524828 447 SLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13639 137 HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
330-490 |
6.02e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLQLLHGDVAFgSNVSVGYYDQEQ-ANL- 405
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILF-KGESILDLEPEErAHLg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 -----------------------TSSKRVLNELWDEYPLQPEKEIRTILG----NFLFTGDDVLKpvsSLSGGQKARLAL 458
Cdd:CHL00131 86 iflafqypieipgvsnadflrlaYNSKRKFQGLPELDPLEFLEIINEKLKlvgmDPSFLSRNVNE---GFSGGEKKRNEI 162
|
170 180 190
....*....|....*....|....*....|..
gi 446524828 459 AKLMMQKSNLLILDEPTNHLDLNSKEILENAL 490
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGI 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
328-504 |
6.64e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLK-----------------------SIVNK----- 379
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRlvaglekptegqifidgedvthrSIQQRdicmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 380 LQ--LLHGDVAFGSNVSVGYYDQEQANLTSSKRVLN--ELWDeyplqpekeirtiLGNFlftGDdvlKPVSSLSGGQKAR 455
Cdd:PRK11432 84 FQsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEalELVD-------------LAGF---ED---RYVDQISGGQQQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524828 456 LALAKLMMQKSNLLILDEPTNHLDLNSKEILENALID----YPGTLLFVSHDR 504
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-503 |
6.67e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 337 TIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQ------LLHGDVAFGSNVSVGYYDQeqanLTSSKR 410
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNdkvsgyRYSGDVLLGGRSIFNYRDV----LEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 V--LNELWDEYPLQ---------------PEKEIR-------TILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKS 466
Cdd:PRK14271 103 VgmLFQRPNPFPMSimdnvlagvrahklvPRKEFRgvaqarlTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524828 467 NLLILDEPTNHLDLNSKEILENALIDYPG--TLLFVSHD 503
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
159-199 |
6.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 6.86e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446524828 159 THQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK10982 384 GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-198 |
6.90e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS--------IGYLAQ 73
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImLDGQDIThvpaenrhVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 74 NTGLETSLTIWD------EMLTVfthlQQMETKLRRLEQ-EMGKEENFSNaatyeklladydqlqldykdqggyqyeadi 146
Cdd:PRK09452 94 SYALFPHMTVFEnvafglRMQKT----PAAEITPRVMEAlRMVQLEEFAQ------------------------------ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 147 RSIlsglgfpvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK09452 140 RKP----------HQ-----LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
331-515 |
7.21e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.90 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKL------QLLHGDVAFGSNVSVGyydQEQA- 403
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLeqpeagTIRVGDITIDTARSLS---QQKGl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 ---------------NLTSSKRVLNELWdEYPLQPEKEI--------RTILGNFLFTGDDVLKPvSSLSGGQKARLALAK 460
Cdd:PRK11264 80 irqlrqhvgfvfqnfNLFPHRTVLENII-EGPVIVKGEPkeeataraRELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 461 LMMQKSNLLILDEPTNHLDLN-SKEILEN--ALIDYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPElVGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-198 |
7.60e-07 |
|
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: 51.59 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG---ELSHDGGEII-KPKDVS------- 67
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILfDGEDLLklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 -------IGYLAQNTGleTSL----TIWD---EMLTVFTHL--QQMETKLRRLEQEMGkeenFSNAatyEKLLADYdqlq 131
Cdd:COG0444 81 rkirgreIQMIFQDPM--TSLnpvmTVGDqiaEPLRIHGGLskAEARERAIELLERVG----LPDP---ERRLDRY---- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 132 ldykdqggyqyeadirsilsglgfPvetHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:COG0444 148 ------------------------P---HE-----LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-223 |
7.69e-07 |
|
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: 51.01 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLY--GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGgeiikpkDVSIGYLAQNTgleTSL 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-------DIQIDGVSWNS---VPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 82 TIWDEMLTVFThlqqmetklrrleqemgkEENFSNAATYEKLLADYDQlqldYKDQGGYQY--EADIRSILSglGFPVET 159
Cdd:cd03289 73 QKWRKAFGVIP------------------QKVFIFSGTFRKNLDPYGK----WSDEEIWKVaeEVGLKSVIE--QFPGQL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 160 HQTTIS---TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-QGYPGAILIVSHDR 223
Cdd:cd03289 129 DFVLVDggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
332-480 |
8.28e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.85 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 332 QVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLkSIVNKLQ-------LLHG-DVA--------------- 388
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLppdsgevLVDGlDVAttpsrelakrlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 389 ----FGSNVSV------GYYDQEQANLTSSKRV----------LNELWDEYplqpekeirtilgnflftgddvlkpVSSL 448
Cdd:COG4604 82 qenhINSRLTVrelvafGRFPYSKGRLTAEDREiideaiayldLEDLADRY-------------------------LDEL 136
|
170 180 190
....*....|....*....|....*....|..
gi 446524828 449 SGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
348-510 |
9.56e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.27 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 348 HVNMRLTRGDSVALVGPNGIGKSTLLKSIvnkLQLLH---GDVAF-GSNVSVGyydqeqanltsSKRVLNELW------- 416
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLL---LRLEEptsGEILFdGQDITGL-----------SGRELRPLRrrmqmvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 417 -DEY-PLQPEKEIRTILG-----NFLFTGDDVLKPVSSL------------------SGGQKARLALAKLMMQKSNLLIL 471
Cdd:COG4608 102 qDPYaSLNPRMTVGDIIAeplriHGLASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 472 DEPTNHLD-------LNSKEILENALidypG-TLLFVSHD----RYFINRV 510
Cdd:COG4608 182 DEPVSALDvsiqaqvLNLLEDLQDEL----GlTYLFISHDlsvvRHISDRV 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-198 |
9.57e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.78 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY-GAETI-LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI------IKPKDV-----SIG 69
Cdd:PRK13635 5 IIRVEHISFRYpDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvLSEETVwdvrrQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 70 YLAQNT---------------GLETSLTIWDEMLtvfthlQQMETKLRRLEQEmgkeenfsnaatyeklladydqlqlDY 134
Cdd:PRK13635 85 MVFQNPdnqfvgatvqddvafGLENIGVPREEMV------ERVDQALRQVGME-------------------------DF 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 135 KDQggyqyeadirsilsglgfpvETHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13635 134 LNR--------------------EPHR-----LSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-222 |
1.03e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 6 VNGLSKLY---GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIagelshdgGEIIKPKDvsigylaqntgleTSLT 82
Cdd:PRK14246 10 VFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--------NRLIEIYD-------------SKIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWDEMLTVFTHLQQMETKlrRLEQEMGKEENFSNAATYeklLADYDQLQLDYKDQGgYQYEADIRSI----LSGLGFPVE 158
Cdd:PRK14246 69 VDGKVLYFGKDIFQIDAI--KLRKEVGMVFQQPNPFPH---LSIYDNIAYPLKSHG-IKEKREIKKIveecLRKVGLWKE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 159 TH---QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHD 222
Cdd:PRK14246 143 VYdrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
345-503 |
1.05e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.16 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSVgyYDQEQANLTSSKRV------------ 411
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQ--MDEEARAKLRAKHVgfvfqsfmlipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 412 LNELWD---------EYPLQPEKEIRTILGNfLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS 482
Cdd:PRK10584 103 LNALENvelpallrgESSRQSRNGAKALLEQ-LGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*
gi 446524828 483 KEILENALI----DYPGTLLFVSHD 503
Cdd:PRK10584 182 GDKIADLLFslnrEHGTTLILVTHD 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-198 |
1.29e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.87 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDV---SIgylaQNTglet 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGEDVthrSI----QQR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 80 SLTIWDEMLTVFTHLQQMETKLRRLE-QEMGKEEnfSNAATYEKL-LADYDQLQLDYKDQggyqyeadirsilsglgfpv 157
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKmLGVPKEE--RKQRVKEALeLVDLAGFEDRYVDQ-------------------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 158 ethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK11432 137 ---------ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
327-479 |
1.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.47 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 327 GNDVLQVKDATIGYDED------PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQllhgdVAFGSNVSVGYYDQ 400
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHM-NALL-----IPSEGKVYVDGLDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 401 EQANLTSSKR--------------VLNELWDEYPLQPE------KEIRTILgnflftgDDVLKPVSS----------LSG 450
Cdd:PRK13633 75 SDEENLWDIRnkagmvfqnpdnqiVATIVEEDVAFGPEnlgippEEIRERV-------DESLKKVGMyeyrrhaphlLSG 147
|
170 180
....*....|....*....|....*....
gi 446524828 451 GQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-218 |
1.42e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 15 AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkdVSIGylaqntgletsltiwdEMLTVFTHL 94
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK------VTVG----------------DIVVSSTSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 95 QQmetKLRRLEQEMGKEENFSNAATYEK-LLADydqLQLDYKDQGGYQYEAD--IRSILSGLGFPVETHQTTISTLSGGQ 171
Cdd:PRK13643 76 QK---EIKPVRKKVGVVFQFPESQLFEEtVLKD---VAFGPQNFGIPKEKAEkiAAEKLEMVGLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 172 KTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILI 218
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQTVVLV 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-240 |
1.62e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 33 ALVGRNGAGKSTLLKIIAGELSHDGGEII-----KPKDVS-------IGYLAQNTgLETSLTIWDEMLTVFTHLQQMETK 100
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDIIindshNLKDINlkwwrskIGVVSQDP-LLFSNSIKNNIKYSLYSLKDLEAL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 101 LRRLEQEMGKEENFSNA--ATYEKLLADYDQLQLDYKDQG------GYQYEAD-----------IRSILSGLGFPVETH- 160
Cdd:PTZ00265 494 SNYYNEDGNDSQENKNKrnSCRAKCAGDLNDMSNTTDSNEliemrkNYQTIKDsevvdvskkvlIHDFVSALPDKYETLv 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 161 QTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQY---LQGYPGAILIVSHDRYFLDKLVTQVYEIS 237
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRITIIIAHRLSTIRYANTIFVLS 653
|
...
gi 446524828 238 NKE 240
Cdd:PTZ00265 654 NRE 656
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
346-503 |
1.68e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.21 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgsnvsVGYydqeQANLTSSKRVLNELWDEYPLQ--- 422
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI-----AGY----HITPETGNKNLKKLRKKVSLVfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 423 PEKEI--RTILG-------NFLFTGDDV-------LKPVS-----------SLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:PRK13641 94 PEAQLfeNTVLKdvefgpkNFGFSEDEAkekalkwLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190
....*....|....*....|....*....|.
gi 446524828 476 NHLDLNSKEILENALIDYPG---TLLFVSHD 503
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-194 |
1.79e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 49.73 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII-KPKDVS-----------IGY 70
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLfGGTDLTgldeheiarlgIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 71 LAQNTGLETSLTIWDEML-------TVFTHLqqmetkLRRLeqemgkeenfsNAATYEKLLADYDQLQLdykdqggyqye 143
Cdd:COG4674 90 KFQKPTVFEELTVFENLElalkgdrGVFASL------FARL-----------TAEERDRIEEVLETIGL----------- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 144 ADIRSILSGLgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:COG4674 142 TDKADRLAGL-------------LSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-229 |
1.80e-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: 50.39 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 24 LEVQTKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLETSLTIWDEMLTVFTHL------QQ 96
Cdd:COG3593 17 LSIELSDDLtVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSRLLRLLlkeedkEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 97 METKLRRLEQEMGKE-ENFSNA-ATYEKLLADYDQLQLDYKdqggyqyEADIRSILSGLGFPVET-HQTTISTLSGGQKT 173
Cdd:COG3593 97 LEEALEELNEELKEAlKALNELlSEYLKELLDGLDLELELS-------LDELEDLLKSLSLRIEDgKELPLDRLGSGFQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 174 R--LALGKLLL-----TKPDLLILDEPTNHLDIETLTWLEQYLQGYPGA---ILIVSHDRYFLDKL 229
Cdd:COG3593 170 LilLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
331-479 |
2.02e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSivnkLQLLHGDVAFGSNVSVGYYDQEQANLTSSKR 410
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLEMPRSGTLNIAGNHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 411 VLNE----LWDEYPLQP---------EKEIRtILG----NFLFTGDDVLK-----------PVSsLSGGQKARLALAKLM 462
Cdd:PRK11124 79 ELRRnvgmVFQQYNLWPhltvqqnliEAPCR-VLGlskdQALARAEKLLErlrlkpyadrfPLH-LSGGQQQRVAIARAL 156
|
170
....*....|....*..
gi 446524828 463 MQKSNLLILDEPTNHLD 479
Cdd:PRK11124 157 MMEPQVLLFDEPTAALD 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
331-503 |
2.44e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF------GSNVSVGYYDQEQAN 404
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 405 LTSSKRVLN-----ELWDEYPLQPEKEIRTILGNFLFTGDDVlKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK11248 82 LPWRNVQDNvafglQLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 446524828 480 LNSKEILENALI----DYPGTLLFVSHD 503
Cdd:PRK11248 161 AFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-60 |
2.54e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 2.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI 60
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-222 |
2.55e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGYLAQNTGLETSltiwdemltvfthlqqme 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI------VGDYAIPANLKKI------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 99 TKLRRLEQEMGKEENFSN----AATYEKLLAdYDQLQLDYKDQGGYQyeaDIRSILSGLGFPVETHQTTISTLSGGQKTR 174
Cdd:PRK13645 83 KEVKRLRKEIGLVFQFPEyqlfQETIEKDIA-FGPVNLGENKQEAYK---KVPELLKLVQLPEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 175 LALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHN 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-198 |
2.63e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.41 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 16 ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEiikpkDVSIGYLAQNTGLETSLTIWDEMLTVFTHlq 95
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP-----NSKITVDGITLTAKTVWDIREKVGIVFQN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 96 qmetklrrleqemgkEENFSNAATYEKLLAdydqLQLDYKDQGGYQYEADIRSILSGLGFpVETHQTTISTLSGGQKTRL 175
Cdd:PRK13640 93 ---------------PDNQFVGATVGDDVA----FGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRV 152
|
170 180
....*....|....*....|...
gi 446524828 176 ALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLD 175
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
153-201 |
2.67e-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: 2.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446524828 153 LGFPVETHQTTISTLSGG--QKtrLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03215 91 LDLSVAENIALSSLLSGGnqQK--VVLARWLARDPRVLILDEPTRGVDVGA 139
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
344-503 |
2.87e-06 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 48.84 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNV----------SVGYYDQE---------QA 403
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYVIQQiglfphmtvEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 NLTSSKRVLNelWdeyplqPEKEIRTilgnflfTGDDVLKPV------------SSLSGGQKARLALAKLMMQKSNLLIL 471
Cdd:cd03295 95 NIALVPKLLK--W------PKEKIRE-------RADELLALVgldpaefadrypHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 446524828 472 DEPTNHLDLNSKEILENALIDYP----GTLLFVSHD 503
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-199 |
2.98e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 15 AETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGgeiiKPKDVSIgylaqnTGletSLTIWDEMLTVFTHL 94
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGG----APRGARV------TG---DVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 95 QQmeTKLRRLEQEMGkEENFSNAATYEKLLADYDQLQ----LDYKDqGGYQYEADIRSILSGLGfpvethQTTISTLSGG 170
Cdd:PRK13547 80 RL--ARLRAVLPQAA-QPAFAFSAREIVLLGRYPHARragaLTHRD-GEIAWQALALAGATALV------GRDVTTLSGG 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524828 171 QKTRLALGKLL---------LTKPDLLILDEPTNHLDI 199
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-82 |
3.11e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 3.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIgyLAQNTGLETSLT 82
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV--IAISAGLSGQLT 101
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-197 |
3.48e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.23 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRI-ALVGRNGAGKSTLLKIIAGELSHDGGEI--IKPKDVSIGYLAQNTGLETSL------TIWDEMLT 89
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLddVKFRKLLIRNGEFGDSAKLILyygtsrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 90 VFTHL-QQMETKLRRLEQEMGKEENFSNAATYekLLADYDQLQLDYKDQGGYQYEAdIRSILSGLgFP------------ 156
Cdd:COG3950 94 KLERLkEEYFSRLDGYDSLLDEDSNLREFLEW--LREYLEDLENKLSDELDEKLEA-VREALNKL-LPdfkdiridrdpg 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 157 ----VETHQTTIS--TLSGGQKTRLAL--------------GKLLLTKPDLLILDEPTNHL 197
Cdd:COG3950 170 rlviLDKNGEELPlnQLSDGERSLLALvgdlarrlaelnpaLENPLEGEGIVLIDEIDLHL 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
328-517 |
3.68e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS--------VGYY 398
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINlvrdkdgqLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQANLTSSKRVLN----ELWD---------EYPLQ------PEKEIRTI--LGNFLFTGDDVLKPVSSLSGGQKARLA 457
Cdd:PRK10619 83 DKNQLRLLRTRLTMVfqhfNLWShmtvlenvmEAPIQvlglskQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 458 LAKLMMQKSNLLILDEPTNHLDLN-SKEILE--NALIDYPGTLLFVSHDRYFINRVTTTVVEL 517
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPElVGEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-221 |
3.84e-06 |
|
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: 50.13 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 16 ETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIGYLAQNTGLeTSLTIWDEMLTVFTHLQ 95
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYM-TLGTLRDQIIYPDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 96 QMETKLRrlEQEMgkeenfsnaatyEKLLadyDQLQLDY--KDQGGYQYEADIRSILSGlgfpvethqttistlsgGQKT 173
Cdd:TIGR00954 544 MKRRGLS--DKDL------------EQIL---DNVQLTHilEREGGWSAVQDWMDVLSG-----------------GEKQ 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 174 RLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPGAILIVSH 221
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
330-530 |
4.02e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.62 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvNKLQLL------HGDVAF-GSNVsvgyYDQEQ 402
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCF-NRLNDLipgfrvEGKVTFhGKNL----YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 ANLTSSKRVLNELWDEYPLQpekeiRTILGNFLF-------TGD-------------------DVLKPV-SSLSGGQKAR 455
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPFP-----KSIYDNIAYgaringyKGDmdelverslrqaalwdevkDKLKQSgLSLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 456 LALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYpgTLLFVSHDRYFINRVTTTV----VELSTEGAQE-YL 526
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDpistLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTaffnVELTEGGGRYgYL 237
|
....
gi 446524828 527 GDYD 530
Cdd:PRK14243 238 VEFD 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-201 |
4.35e-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: 48.26 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 14 GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGylaqntGLETSlTIwdemltvftH 93
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL------ID------GVDIS-KI---------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 94 LQQMETKLRRLEQEmgkEENFS----------NAATYEKLLADYDQLQLDykdqggyqyeADIRSILSGLGFPVETHQtt 163
Cdd:cd03244 73 LHDLRSRISIIPQD---PVLFSgtirsnldpfGEYSDEELWQALERVGLK----------EFVESLPGGLDTVVEEGG-- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524828 164 iSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03244 138 -ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-201 |
4.38e-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: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 33 ALVGRNGAGKSTLLKIIAG--ELSHDGGEII---KPKDVS----IGYLAQNTGLETSLTIwdemltvfthlqqmetklrr 103
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAGrkTAGVITGEILingRPLDKNfqrsTGYVEQQDVHSPNLTV-------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 104 leqemgkeenfsnaatYEKLLadydqlqldykdqggyqYEADIRSilsglgfpvethqttistLSGGQKTRLALGKLLLT 183
Cdd:cd03232 97 ----------------REALR-----------------FSALLRG------------------LSVEQRKRLTIGVELAA 125
|
170
....*....|....*...
gi 446524828 184 KPDLLILDEPTNHLDIET 201
Cdd:cd03232 126 KPSILFLDEPTSGLDSQA 143
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
327-502 |
4.52e-06 |
|
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: 49.75 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 327 GNDVLQVKDATIGYDEDPI--------IEHVNMRLTRGDSVALVGPNGIGKSTLLKsIVNKLQLLHGDVAfgsnvsvgYY 398
Cdd:TIGR00954 441 GRGIVEYQDNGIKFENIPLvtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRL--------TK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 399 DQEQANLTSSKR---VLNELWDE--YPLQPE---------KEIRTILGNFLFtgDDVLKPVSS----------LSGGQKA 454
Cdd:TIGR00954 512 PAKGKLFYVPQRpymTLGTLRDQiiYPDSSEdmkrrglsdKDLEQILDNVQL--THILEREGGwsavqdwmdvLSGGEKQ 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 455 RLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALIDYPGTLLFVSH 502
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-503 |
5.38e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.81 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 349 VNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVsVGYYDQEQANLtsSKRVLNELWDEY-PLQPEKE 426
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDL-LKADPEAQKLL--RQKIQIVFQNPYgSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 427 IRTILGNFLFTGDDV-----------------LKPVSS------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK 483
Cdd:PRK11308 111 VGQILEEPLLINTSLsaaerrekalammakvgLRPEHYdryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180
....*....|....*....|....
gi 446524828 484 EILENALIDYPGTL----LFVSHD 503
Cdd:PRK11308 191 AQVLNLMMDLQQELglsyVFISHD 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-201 |
5.89e-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: 48.31 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 12 LYGAeTILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDVSIgylaqntgleTSLTIWDEMLTVf 91
Cdd:cd03291 47 LVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISF----------SSQFSWIMPGTI- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 92 thlqqmetklrrleqemgkEENFSNAATYEklladydqlQLDYKDQ-GGYQYEADIrsilsgLGFPvETHQTTIS----T 166
Cdd:cd03291 115 -------------------KENIIFGVSYD---------EYRYKSVvKACQLEEDI------TKFP-EKDNTVLGeggiT 159
|
170 180 190
....*....|....*....|....*....|....*
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
348-487 |
5.95e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.48 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 348 HVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANlTSSKRV-------LNELWDEyp 420
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLK-PLRKKVgivfqfpEHQLFEE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 421 lQPEKEIRTILGNFLFTGDDVLKPVS------------------SLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LN 481
Cdd:PRK13634 102 -TVEKDICFGPMNFGVSEEDAKQKARemielvglpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpKG 180
|
....*.
gi 446524828 482 SKEILE 487
Cdd:PRK13634 181 RKEMME 186
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
335-479 |
6.35e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 335 DATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ-------LLHGDVAFGSNV--SVGYYDQEQ--- 402
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnftgtILANNRKPTKQIlkRTGFVTQDDily 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 ANLT--------SSKRVLNELW-DEYPLQPEKEI---------RTILGNFLFTGddvlkpvssLSGGQKARLALAKLMMQ 464
Cdd:PLN03211 153 PHLTvretlvfcSLLRLPKSLTkQEKILVAESVIselgltkceNTIIGNSFIRG---------ISGGERKRVSIAHEMLI 223
|
170
....*....|....*
gi 446524828 465 KSNLLILDEPTNHLD 479
Cdd:PLN03211 224 NPSLLILDEPTSGLD 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
331-490 |
6.68e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDED--PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvnkLQLLHGD-------VAFGS------NVSV 395
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEgeiqidgVSWNSvtlqtwRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 396 GYYDQE--------QANLTSSKRVLN-ELWDeypLQPEKEIRTILGNFLFTGDDVLKPVSS-LSGGQKARLALAKLMMQK 465
Cdd:TIGR01271 1295 GVIPQKvfifsgtfRKNLDPYEQWSDeEIWK---VAEEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSK 1371
|
170 180
....*....|....*....|....*
gi 446524828 466 SNLLILDEPTNHLDLNSKEILENAL 490
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-490 |
6.90e-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: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVS-VGYYD------- 399
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISkIGLHDlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 --QEQANLTSSKRV----LNELWDEYPLQPEKE--IRTILGNFLFTGDDVLKPV-SSLSGGQKARLALAKLMMQKSNLLI 470
Cdd:cd03244 83 ipQDPVLFSGTIRSnldpFGEYSDEELWQALERvgLKEFVESLPGGLDTVVEEGgENLSVGQRQLLCLARALLRKSKILV 162
|
170 180
....*....|....*....|
gi 446524828 471 LDEPTNHLDLNSKEILENAL 490
Cdd:cd03244 163 LDEATASVDPETDALIQKTI 182
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
443-509 |
7.08e-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: 7.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 443 KPVSSLSGGQKARLALAKLMMQKS--NLLILDEPTNHLDLNSKEILENA---LIDYPGTLLFVSHDRYFINR 509
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLDVLSS 154
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-221 |
7.61e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.95 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTllkiIAGELSHdggeiikpkdvsigyLAQNTGleTSLTIWDEMLTVFTHlQQM 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST----VAALLQN---------------LYQPTG--GQVLLDGVPLVQYDH-HYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 98 ETKLRRLEQE---MGKeeNFSNAATYEKLLADYDQLQLDYKDQGGYQYEAdirsilsglGFPvETHQTTI----STLSGG 170
Cdd:TIGR00958 554 HRQVALVGQEpvlFSG--SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM---------EFP-NGYDTEVgekgSQLSGG 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 171 QKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQGYPGA----ILIVSH 221
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSRasrtVLLIAH 672
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-503 |
8.31e-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: 47.75 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 356 GDSVALVGPNGIGKSTLLKSIVNKL------------------------------QLLHGDVAfgSNVSVGYYDQEQANL 405
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddppdwdeildefrgselqnyftKLLEGDVK--VIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 TSSKRVLNELWDEYPLQPE----KEIRTILGNflftgddvlkPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-- 479
Cdd:cd03236 104 KGKVGELLKKKDERGKLDElvdqLELRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDik 173
|
170 180
....*....|....*....|....*.
gi 446524828 480 --LNSKEILENaLIDYPGTLLFVSHD 503
Cdd:cd03236 174 qrLNAARLIRE-LAEDDNYVLVVEHD 198
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-198 |
8.90e-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: 48.26 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 34 LVGRNGAGKSTLLKIIAGELSHDGGEII---------KPKDVSIGYLAQNTGLetsltiwdemltvFTHlqqmetklrrl 104
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMldgedvtnvPPHLRHINMVFQSYAL-------------FPH----------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 105 eqeMGKEENFSNAATYEKLladydqlqldykdqGGYQYEADIRSILSGLGFPvETHQTTISTLSGGQKTRLALGKLLLTK 184
Cdd:TIGR01187 57 ---MTVEENVAFGLKMRKV--------------PRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFK 118
|
170
....*....|....
gi 446524828 185 PDLLILDEPTNHLD 198
Cdd:TIGR01187 119 PKILLLDEPLSALD 132
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
346-518 |
9.07e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.18 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANLtssKRVLNELWDEYPLQPEk 425
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL---RRQIGMIFQDHHLLMD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 426 eiRTILGNFLF-------TGDDVLKPVSS-----------------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN 481
Cdd:PRK10908 94 --RTVYDNVAIpliiagaSGDDIRRRVSAaldkvglldkaknfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 482 SKEILENALIDYPG---TLLFVSHDRYFINRVTTTVVELS 518
Cdd:PRK10908 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
356-480 |
9.45e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 356 GDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgsnvsvgyyDQEQANLTSSKRVLNELwdEY-PLQ-PEKEIRTI--- 430
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL---------DAQPLESWSSKAFARKV--AYlPQQlPAAEGMTVrel 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 431 --LGNFLFTG-------------DDV-----LKP-----VSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK10575 106 vaIGRYPWHGalgrfgaadrekvEEAislvgLKPlahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-221 |
1.01e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 47.34 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 4 LQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKI------------IAGELSHDGGEIIKPK-DVS--- 67
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlipgarVEGEILLDGEDIYDPDvDVVelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 68 --IGYLAQN-TGLETSltIWDEMltVF----------THLQQM-ETKLRRleqemgkeenfsnAATYEKLladYDQLQLd 133
Cdd:COG1117 92 rrVGMVFQKpNPFPKS--IYDNV--AYglrlhgikskSELDEIvEESLRK-------------AALWDEV---KDRLKK- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 134 ykdqggyqyeadirsilSGLGfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD------IETLTW-L- 205
Cdd:COG1117 151 -----------------SALG------------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakIEELILeLk 201
|
250
....*....|....*.
gi 446524828 206 EQYlqgypgAILIVSH 221
Cdd:COG1117 202 KDY------TIVIVTH 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-304 |
1.02e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSH--DGGEIIKPkdvSIGYLAQNTgletsltiWdemltVFthlqq 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG---SVAYVPQVS--------W-----IF----- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 97 metklrrleqemgkeenfsNAATYEKLL--ADYDQLQldykdqggYQYEADIRSILSGLGFPVETHQTTIS----TLSGG 170
Cdd:PLN03232 692 -------------------NATVRENILfgSDFESER--------YWRAIDVTALQHDLDLLPGRDLTEIGergvNISGG 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 171 QKTRLALGKLLLTKPDLLILDEPTNHLDIETL-----TWLEQYLQGypGAILIVSHDRYFL---DKLVTqVYEISNKESR 242
Cdd:PLN03232 745 QKQRVSMARAVYSNSDIYIFDDPLSALDAHVAhqvfdSCMKDELKG--KTRVLVTNQLHFLplmDRIIL-VSEGMIKEEG 821
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 243 RFVgNYSKYLDLKSALYEQEIKRYEKQQ-----DEIAKLEDFVQKNIA--RASTTKRAQSRRKQLDRME 304
Cdd:PLN03232 822 TFA-ELSKSGSLFKKLMENAGKMDATQEvntndENILKLGPTVTIDVSerNLGSTKQGKRGRSVLVKQE 889
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
326-488 |
1.60e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 326 SGNDVLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSVGYYDQEQ 402
Cdd:PRK10789 309 EGRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhDIPLTKLQLDSWR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 ANLTS--------SKRVLNELWDEYPLQPEKEIRTI--LGNflfTGDDVLK-------PVSS----LSGGQKARLALAKL 461
Cdd:PRK10789 389 SRLAVvsqtpflfSDTVANNIALGRPDATQQEIEHVarLAS---VHDDILRlpqgydtEVGErgvmLSGGQKQRISIARA 465
|
170 180
....*....|....*....|....*...
gi 446524828 462 MMQKSNLLILDEPTNHLDLNSK-EILEN 488
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEhQILHN 493
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
325-594 |
1.88e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 325 QSGNDVLQVKDATIGYD---EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ-------LLHGDVAFGSNVS 394
Cdd:PLN03130 609 EPGLPAISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprsdasvVIRGTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYydqeqaNLTSSKRVLNELwdeyPLQPEKEIRTILGNFLFTGDDVLkPVSSL----------SGGQKARLALAKLMMQ 464
Cdd:PLN03130 689 WIF------NATVRDNILFGS----PFDPERYERAIDVTALQHDLDLL-PGGDLteigergvniSGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 465 KSNLLILDEPTNHLDLN-SKEILENALIDYPG--TLLFVSHDRYFINRVTTTVV-------------ELSTEGA-----Q 523
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHvGRQVFDKCIKDELRgkTRVLVTNQLHFLSQVDRIILvhegmikeegtyeELSNNGPlfqklM 837
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 524 EYLGDYDYYVEKKNEMIERAAFEQQEQQENQAPVQKTVAQEKlnylEEKERKQLerqrTRKIEELEQNIVS 594
Cdd:PLN03130 838 ENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKK----KSKEGKSV----LIKQEERETGVVS 900
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
2.07e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.72 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLY-GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsigylaqntglet 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 80 sltIWDEMLTvfthlqqmETKLRRLEQEMG------KEENFSnaATYEKLLA-DYDQLQLDYKdqggyQYEADIRSILSG 152
Cdd:PRK13652 63 ---IRGEPIT--------KENIREVRKFVGlvfqnpDDQIFS--PTVEQDIAfGPINLGLDEE-----TVAHRVSSALHM 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 153 LGFPvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYP 213
Cdd:PRK13652 125 LGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
448-503 |
2.12e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 2.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEILE--NALIDYPGTLLFVSHD 503
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
328-503 |
2.14e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.62 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDEDPIIEHVN---MRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF------GSNV----- 393
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdgelltAENVwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 394 SVGYYDQEQANLTSSKRVLNEL---WDEYPLQPEKEIRTILGNFLFTG--DDVLKPVSSLSGGQKARLALAKLMMQKSNL 468
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVafgMENQGIPREEMIKRVDEALLAVNmlDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524828 469 LILDEPTNHLDLNSK----EILENALIDYPGTLLFVSHD 503
Cdd:PRK13642 162 IILDESTSMLDPTGRqeimRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
167-246 |
2.26e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQGYPG--AILIVSHDryfldklVTQVYEISNKESRRF 244
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN-------LAQAARISDRAALFF 236
|
..
gi 446524828 245 VG 246
Cdd:PRK14271 237 DG 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-503 |
2.40e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.04 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 340 YDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFG-SNVS-----------VGYYDQEQA---- 403
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdEDISllplhararrgIGYLPQEASifrr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 404 ---------------NLTSSKRV--LNELWDEYPLQpekEIRTILGNflftgddvlkpvsSLSGGQKARLALAKLMMQKS 466
Cdd:PRK10895 93 lsvydnlmavlqirdDLSAEQREdrANELMEEFHIE---HLRDSMGQ-------------SLSGGERRRVEIARALAANP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524828 467 NLLILDEPTNHLD----LNSKEILENaLIDYPGTLLFVSHD 503
Cdd:PRK10895 157 KFILLDEPFAGVDpisvIDIKRIIEH-LRDSGLGVLITDHN 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-198 |
2.51e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 46.52 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGAETILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEI-IKPKDVS----------I 68
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITISkenlkeirkkI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 69 GYLAQNT---------------GLETSLTIWDEMLTVFTHLQQ---METKLRRLEQEmgkeenfsnaatyeklladydql 130
Cdd:PRK13632 86 GIIFQNPdnqfigatveddiafGLENKKVPPKKMKDIIDDLAKkvgMEDYLDKEPQN----------------------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 131 qldykdqggyqyeadirsilsglgfpvethqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13632 143 ------------------------------------LSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
329-491 |
3.12e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 329 DVLQVKDATIGYD--EDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFG-----SNVS-----VG 396
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgksilTNISdvhqnMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 YYDQEQA--NLTSSKRVLnELWDEYPLQPEKEIRTI-------LGNFLFTgdDVLkpVSSLSGGQKARLALAKLMMQKSN 467
Cdd:TIGR01257 2016 YCPQFDAidDLLTGREHL-YLYARLRGVPAEEIEKVanwsiqsLGLSLYA--DRL--AGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180
....*....|....*....|....
gi 446524828 468 LLILDEPTNHLDLNSKEILENALI 491
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
300-519 |
3.33e-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: 47.12 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 300 LDRM-ELLTRPLgdsksasfhfDIEKQSGNDVLQVKDATI-------GYDED-PIIEHVNMRLTRGDSVALVGPNGIGKS 370
Cdd:COG5265 329 MERMfDLLDQPP----------EVADAPDAPPLVVGGGEVrfenvsfGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 371 TLLKsivnklqLLHG--DVAFGSnVSVGyyDQEQANLT-SSKR----------VL-NElwdeyplqpekeirTILGNFLF 436
Cdd:COG5265 399 TLAR-------LLFRfyDVTSGR-ILID--GQDIRDVTqASLRaaigivpqdtVLfND--------------TIAYNIAY 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 437 -----TGDDV----------------------------LKpvssLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNS- 482
Cdd:COG5265 455 grpdaSEEEVeaaaraaqihdfieslpdgydtrvgergLK----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTe 530
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446524828 483 KEILEnalidypgTLLFVSHDRyfinrvtTTVV---ELST 519
Cdd:COG5265 531 RAIQA--------ALREVARGR-------TTLViahRLST 555
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-201 |
3.97e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.33 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQvnGLSKLYGAE----TILANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIikpkdvsig 69
Cdd:PRK11153 1 MIELK--NISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVLVDGQDL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 70 ylaqntgleTSLTiwdemltvfthlqqmETKLRRLEQEMG---KEEN-------FSNAAtyeklLAdydqLQLDYKDqgg 139
Cdd:PRK11153 70 ---------TALS---------------EKELRKARRQIGmifQHFNllssrtvFDNVA-----LP----LELAGTP--- 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 140 yqyEADIRSI------LSGLGfpvETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:PRK11153 114 ---KAEIKARvtelleLVGLS---DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
314-518 |
4.00e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 314 KSASFHFDIEKqsgnDVLQVKDatigydedpiiehVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDV------ 387
Cdd:PTZ00265 386 KNVRFHYDTRK----DVEIYKD-------------LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsh 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 388 --------------------------AFGSNVSVGYYD------------------QEQANLTSSKRV------------ 411
Cdd:PTZ00265 449 nlkdinlkwwrskigvvsqdpllfsnSIKNNIKYSLYSlkdlealsnyynedgndsQENKNKRNSCRAkcagdlndmsnt 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 412 -----LNELWDEYPLQPEKEI-----RTILGNFLFTGDD-----VLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTN 476
Cdd:PTZ00265 529 tdsneLIEMRKNYQTIKDSEVvdvskKVLIHDFVSALPDkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446524828 477 HLDLNSKEILENALIDYPGT----LLFVSHdRYFINRVTTTVVELS 518
Cdd:PTZ00265 609 SLDNKSEYLVQKTINNLKGNenriTIIIAH-RLSTIRYANTIFVLS 653
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
167-240 |
4.29e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 4.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYL-----QGYpgAILIVSHDRYFLDKLVTQVYEISNKE 240
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLydlnkEGI--TIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-198 |
4.29e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.78 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELshdggeiiKPKdvsigylaqntglETSLTIWDEMLTVfthlQQME 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL--------QPT-------------SGTVTIGERVITA----GKKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 99 TKLRRLEQEMGKEENFSNA----ATYEKLLAdYDQLQLDYKDQggyQYEADIRSILSGLGFPVETHQTTISTLSGGQKTR 174
Cdd:PRK13634 78 KKLKPLRKKVGIVFQFPEHqlfeETVEKDIC-FGPMNFGVSEE---DAKQKAREMIELVGLPEELLARSPFELSGGQMRR 153
|
170 180
....*....|....*....|....
gi 446524828 175 LALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
328-486 |
4.32e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.51 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGY--DEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgSNVSVgyydqEQANL 405
Cdd:PRK13648 5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY-NNQAI-----TDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 TSSKRVLNELWDeyplQPEKE-IRTI--------LGNFLFTGDDVLKPVS-----------------SLSGGQKARLALA 459
Cdd:PRK13648 79 EKLRKHIGIVFQ----NPDNQfVGSIvkydvafgLENHAVPYDEMHRRVSealkqvdmleradyepnALSGGQKQRVAIA 154
|
170 180
....*....|....*....|....*..
gi 446524828 460 KLMMQKSNLLILDEPTNHLDLNSKEIL 486
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNL 181
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-200 |
4.96e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.00 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 2 ILLQVNGLSKLYGAET-----ILANIKLEVQTKDRIALVGRNGAGKSTLLkiiagelSHDGGeIIKPK--DVSIG--YLA 72
Cdd:PRK13631 20 IILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLV-------THFNG-LIKSKygTIQVGdiYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QNTGLETSltiwdemltVFTHLQQMETKLRRLEQEMGkeenfsnaatyekLLADYDQLQLdYKDQ------------GGY 140
Cdd:PRK13631 92 DKKNNHEL---------ITNPYSKKIKNFKELRRRVS-------------MVFQFPEYQL-FKDTiekdimfgpvalGVK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 141 QYEADIRS--ILSGLGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIE 200
Cdd:PRK13631 149 KSEAKKLAkfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-510 |
4.98e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 45.81 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDED----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvnkLQLLhgdvafgsnvsvgyydqeQANL 405
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI---LGLL------------------PPPG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 TSSKRVLnelWDEYPLQ--PEKEIRTILGN-----F---------LFT-GD---DVLK---PVSS--------------- 447
Cdd:COG0444 60 ITSGEIL---FDGEDLLklSEKELRKIRGReiqmiFqdpmtslnpVMTvGDqiaEPLRihgGLSKaeareraiellervg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 448 --------------LSGGQKARLALAKLMMQKSNLLILDEPTNHLDL-NSKEILEnaLI-----DYPGTLLFVSHD---- 503
Cdd:COG0444 137 lpdperrldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVtIQAQILN--LLkdlqrELGLAILFITHDlgvv 214
|
....*..
gi 446524828 504 RYFINRV 510
Cdd:COG0444 215 AEIADRV 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
348-475 |
5.27e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 348 HVNMRLTRGDSVALVGPNGIGKSTLLK-----------SIvnklqLLHG-DVAFGS------------------------ 391
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKilyglyqpdsgEI-----LIDGkPVRIRSprdaialgigmvhqhfmlvpnltv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 392 --NVSVGYYDQEQA--NLTSSKRVLNELWDEYPLqpekEIrtilgnflftgdDVLKPVSSLSGGQKARLALAKLMMQKSN 467
Cdd:COG3845 98 aeNIVLGLEPTKGGrlDRKAARARIRELSERYGL----DV------------DPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
....*...
gi 446524828 468 LLILDEPT 475
Cdd:COG3845 162 ILILDEPT 169
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-198 |
5.31e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 13 YGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKI------------IAGELSHDGGEIIKPKDVSI------GYLAQN 74
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVRLFGRNIYSPDVDPIevrrevGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 75 TGLETSLTIWDEMltvfthlqQMETKLRRLEQemGKEENFSNAATYEKLLADYDQLQLDYKDqggyqyeadirsilsglg 154
Cdd:PRK14267 94 PNPFPHLTIYDNV--------AIGVKLNGLVK--SKKELDERVEWALKKAALWDEVKDRLND------------------ 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 155 FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK14267 146 YP--------SNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
168-222 |
5.69e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 5.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDI----ETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-222 |
5.79e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKDvsigylaqntgLETSLTIWDemltvfthlqqm 97
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-----------LLTEENVWD------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 98 etKLRRLEQEMGKEENFSNAATYEKLLA-DYDQLQLDYKDQGGYQYEAdirsiLSGLGFpVETHQTTISTLSGGQKTRLA 176
Cdd:PRK13650 79 --IRHKIGMVFQNPDNQFVGATVEDDVAfGLENKGIPHEEMKERVNEA-----LELVGM-QDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 177 LGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQG----YPGAILIVSHD 222
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
345-503 |
6.07e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.26 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLksivNKLQLLHG------DVAfGSNVS--------------VGYYDQEQ-- 402
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLM----NILGCLDKptsgtyRVA-GQDVAtldadalaqlrrehFGFIFQRYhl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 403 -ANLTSSKRVlnelwdEYPL---QPEKEIRTILGNFLFT----GDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEP 474
Cdd:PRK10535 98 lSHLTAAQNV------EVPAvyaGLERKQRLLRAQELLQrlglEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|...
gi 446524828 475 TNHLDLNSKE----ILENaLIDYPGTLLFVSHD 503
Cdd:PRK10535 172 TGALDSHSGEevmaILHQ-LRDRGHTVIIVTHD 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
330-535 |
6.23e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDED-PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAF-GSNVSvgyydqeQANLTS 407
Cdd:PRK13652 3 LIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPIT-------KENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 408 SKRVLNELW---DEYPLQPEKEIRTILG--NFLFTGDDVLKPVSS-----------------LSGGQKARLALAKLMMQK 465
Cdd:PRK13652 76 VRKFVGLVFqnpDDQIFSPTVEQDIAFGpiNLGLDEETVAHRVSSalhmlgleelrdrvphhLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 466 SNLLILDEPTNHLD-LNSKEILE--NALID-YPGTLLFVSHDryfinrvtttvVELSTEgaqeyLGDYDYYVEK 535
Cdd:PRK13652 156 PQVLVLDEPTAGLDpQGVKELIDflNDLPEtYGMTVIFSTHQ-----------LDLVPE-----MADYIYVMDK 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-222 |
6.73e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLY--GAETI--LANIKLEVQTKDRIALVGRNGAGKSTLLKIIagelshdgGEIIKPKDVSIGYLAQNTGle 78
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPTSGTYRVAGQDVA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 79 tslTIWDEMLTvfthlqqmetKLRRleqemgkeENFSNAATYEKLLADYDQLQ-----LDYKDQGGYQYEADIRSILSGL 153
Cdd:PRK10535 74 ---TLDADALA----------QLRR--------EHFGFIFQRYHLLSHLTAAQnvevpAVYAGLERKQRLLRAQELLQRL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 154 GFPVETHQTTiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQyLQGYPGAILIVSHD 222
Cdd:PRK10535 133 GLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
331-503 |
6.94e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANLTSSK- 409
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 410 ----RVLNELwdeyplqpekeirTILGNFL-----------FTG----------------------------DDVLKPVS 446
Cdd:PRK11300 86 fqhvRLFREM-------------TVIENLLvaqhqqlktglFSGllktpafrraesealdraatwlervgllEHANRQAG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 447 SLSGGQKARLALAKLMMQKSNLLILDEPTnhLDLNSKEILE-NALID-----YPGTLLFVSHD 503
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPA--AGLNPKETKElDELIAelrneHNVTVLLIEHD 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
345-503 |
7.69e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 44.73 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLkSIVNKLQLL-HGDVA-FGSNVS--------------VGYYDQ-EQ--ANL 405
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAGLDRPtSGTVRlAGQDLFaldedararlrarhVGFVFQsFQllPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 406 TSS-----------------------KRV-LNELWDEYPLQpekeirtilgnflftgddvlkpvssLSGGQKARLALAKL 461
Cdd:COG4181 106 TALenvmlplelagrrdarararallERVgLGHRLDHYPAQ-------------------------LSGGEQQRVALARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524828 462 MMQKSNLLILDEPTNHLDL-NSKEILE-----NAliDYPGTLLFVSHD 503
Cdd:COG4181 161 FATEPAILFADEPTGNLDAaTGEQIIDllfelNR--ERGTTLVLVTHD 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
7.83e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 44.73 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLL--------------KIIAGELSHDGGEIIKPKdvsIGYLAQNTGLET-SLTI 83
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvKVMGREVNAENEKWVRSK---VGLVFQDPDDQVfSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 WDEMltvfthlqqmetKLRRLEQEMGKEENFSNAATYEKLLADYDqlqldYKDQGGYQyeadirsilsglgfpvethqtt 163
Cdd:PRK13647 98 WDDV------------AFGPVNMGLDKDEVERRVEEALKAVRMWD-----FRDKPPYH---------------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 164 istLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD---IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13647 139 ---LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-60 |
7.94e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 7.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 2 ILLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHD--GGEI 60
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDI 66
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-503 |
7.95e-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: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIvnkLQLLH---GDVAF-GSNVS------VGYYD 399
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII---LGILApdsGEVLWdGEPLDpedrrrIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 400 QEQAnLTSSKRVLNELwdEYPLQ----PEKEIRTILgnflftgDDVL----------KPVSSLSGG--QKARLALAklMM 463
Cdd:COG4152 78 EERG-LYPKMKVGEQL--VYLARlkglSKAEAKRRA-------DEWLerlglgdranKKVEELSKGnqQKVQLIAA--LL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524828 464 QKSNLLILDEPTNHLD-LNSkEILENALIDY--PG-TLLFVSHD 503
Cdd:COG4152 146 HDPELLILDEPFSGLDpVNV-ELLKDVIRELaaKGtTVIFSSHQ 188
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
346-515 |
8.65e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.00 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKsIVNKL------QLLHGDVAFGSNVSvgyydqeqaNLTSSKRVLNEL---- 415
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQ-LTNGLiisetgQTIVGDYAIPANLK---------KIKEVKRLRKEIglvf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 416 -WDEYPLQPEKEIRTILGNFLFTGDD----------VLKPVS-----------SLSGGQKARLALAKLMMQKSNLLILDE 473
Cdd:PRK13645 97 qFPEYQLFQETIEKDIAFGPVNLGENkqeaykkvpeLLKLVQlpedyvkrspfELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524828 474 PTNHLDLNSKEILENALI----DYPGTLLFVSHDRYFINRVTTTVV 515
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
363-502 |
8.86e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 363 GPNGIGKSTLLKSIVNKLQLLHGDVAFGS----NVSVGY--YDQEQANLTSSKRVLNEL--WDEYPLQPEKEIRTIlgnF 434
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNcninNIAKPYctYIGHNLGLKLEMTVFENLkfWSEIYNSAETLYAAI---H 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 435 LFTGDDVL-KPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI---DYPGTLLFVSH 502
Cdd:PRK13541 110 YFKLHDLLdEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmkaNSGGIVLLSSH 181
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-201 |
9.57e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.07 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MIllQVNGLSKLY----GAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIkpkdvsIGylaqntG 76
Cdd:COG1135 1 MI--ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL------VD------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 77 LE-TSLTiwdemltvfthlqqmETKLRRLEQEMG----------------------KEENFSNAATYEK---LLAdydql 130
Cdd:COG1135 67 VDlTALS---------------ERELRAARRKIGmifqhfnllssrtvaenvalplEIAGVPKAEIRKRvaeLLE----- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 131 qldykdqggyqyeadirsiLSGLG-----FPvethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:COG1135 127 -------------------LVGLSdkadaYP--------SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
353-479 |
1.18e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 353 LTRGDSVALVGPNGIGKSTLLKsivnklqLLHGDVA--FGSnvsvgyYDQEqanlTSSKRVL-----NELWDEYPLQPEK 425
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------ILSGELIpnLGD------YEEE----PSWDEVLkrfrgTELQNYFKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 426 EIRTIL--------------------------GNFlftgDDVLK----------PVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK13409 159 EIKVVHkpqyvdlipkvfkgkvrellkkvderGKL----DEVVErlglenildrDISELSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 446524828 470 ILDEPTNHLD 479
Cdd:PRK13409 235 FFDEPTSYLD 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
448-541 |
1.28e-04 |
|
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: 45.18 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENALI----DYPGTLLFVSHDRYFINRVTTTVVELStEGAQ 523
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeavkASGISMVLTSHWPEVIEDLSDKAIWLE-NGEI 247
|
90
....*....|....*...
gi 446524828 524 EYLGDYDYYVEKKNEMIE 541
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGVS 265
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-60 |
1.32e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.31 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MIllQVNGLSKLY----------GA---------ETILA--NIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGE 59
Cdd:COG4586 1 II--EVENLSKTYrvyekepglkGAlkglfrreyREVEAvdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE 78
|
.
gi 446524828 60 I 60
Cdd:COG4586 79 V 79
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
330-492 |
1.33e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLK--SIVNKLQLLHGDVAF------GSNVSvgyyDQE 401
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFegeelqASNIR----DTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 QA-------------NLTSSKRVL--NEL-------WDEYPLQPEKEIRTilgnfLFTGDDVLKPVSSLSGGQKARLALA 459
Cdd:PRK13549 81 RAgiaiihqelalvkELSVLENIFlgNEItpggimdYDAMYLRAQKLLAQ-----LKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190
....*....|....*....|....*....|...
gi 446524828 460 KLMMQKSNLLILDEPTNHLDLNSKEILENALID 492
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRD 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-194 |
1.34e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 5 QVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIA-------GELSHDGGEIIKPK---DVS--IGYLA 72
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarkiqqGRVEVLGGDMADARhrrAVCprIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 73 QntGLETSL--TiwdemLTVFTHLQQMEtklrRLeqemgkeenFSnaatyeklladydqlqldykdQGGYQYEADIRSIL 150
Cdd:NF033858 83 Q--GLGKNLypT-----LSVFENLDFFG----RL---------FG---------------------QDAAERRRRIDELL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524828 151 --SGLG-F---PVethqttiSTLSGGQKTRLALGKLLLTKPDLLILDEPT 194
Cdd:NF033858 122 raTGLApFadrPA-------GKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-207 |
1.42e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG--ELSHD---------GGEIIKPKDVSiGYLAQNTGL----ETSLT 82
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDhhivfknehTNDMTNEQDYQ-GDEEQNVGMknvnEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 83 IWD---EMLTVFTHLQQME-----------TKLRRLEQEMGKEENFSNAATYEKL-LADYDQLQLDYKDQGGYqyeADIR 147
Cdd:PTZ00265 1262 KEGgsgEDSTVFKNSGKILldgvdicdynlKDLRNLFSIVSQEPMLFNMSIYENIkFGKEDATREDVKRACKF---AAID 1338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 148 SILSGLGFPVETHQTTI-STLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQ 207
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
331-480 |
1.55e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.90 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 331 LQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVN--KLQLLHGDVAF-GSNVS-----------VG 396
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLdGEDILelspderaragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 Y---YDQEQANLTSS---KRVLNELWDE--YPLQPEKEIRTILGNFLFTGDDVLKPV-SSLSGGQKARLALAKLMMQKSN 467
Cdd:COG0396 81 LafqYPVEIPGVSVSnflRTALNARRGEelSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPK 160
|
170
....*....|...
gi 446524828 468 LLILDEPTNHLDL 480
Cdd:COG0396 161 LAILDETDSGLDI 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-198 |
2.13e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.59 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 33 ALVGRNGAGKSTLLKIIAGelshdggeIIKPKDVSIGYLAQNTGLETSLTIWDEMLTVFTHLQ-QMETKLRRLEQEMGKE 111
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIG--------IEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVGSIVKYDVAFGLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 112 enfSNAATYEKLLADYDQL--QLDYKDQGGYQYEAdirsilsglgfpvethqttistLSGGQKTRLALGKLLLTKPDLLI 189
Cdd:PRK13648 111 ---NHAVPYDEMHRRVSEAlkQVDMLERADYEPNA----------------------LSGGQKQRVAIAGVLALNPSVII 165
|
....*....
gi 446524828 190 LDEPTNHLD 198
Cdd:PRK13648 166 LDEATSMLD 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
348-503 |
2.30e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 348 HVNMRL---TRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDvafgsnvsvgyydqeqanltsskrvlnelwDEYPLQpe 424
Cdd:cd03222 14 FLLVELgvvKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN------------------------------DEWDGI-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 425 keirTIlgnflftgddVLKPVS-SLSGGQKARLALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPGTLLF 499
Cdd:cd03222 62 ----TP----------VYKPQYiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALV 127
|
....
gi 446524828 500 VSHD 503
Cdd:cd03222 128 VEHD 131
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
167-198 |
2.71e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.15 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|..
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-479 |
2.78e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.88 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 356 GDSVALVGPNGIGKSTLLKSIVNKLQllhGDVAFGSNVSV--------------GYYDQE-------------------- 401
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSP---KGVKGSGSVLLngmpidakemraisAYVQQDdlfiptltvrehlmfqahlr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 402 -QANLTSSKRVL--NELWDEYPLQPEKEirTILGnflftgddVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHL 478
Cdd:TIGR00955 128 mPRRVTKKEKRErvDEVLQALGLRKCAN--TRIG--------VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
.
gi 446524828 479 D 479
Cdd:TIGR00955 198 D 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
167-199 |
3.12e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 3.12e-04
10 20 30
....*....|....*....|....*....|...
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
442-503 |
3.64e-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: 3.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 442 LKPVSSLSGGQKARLALAKLMMqksnlLILDepTNHLDLNSKEILENALIDypgtLLFVSHD 503
Cdd:COG0419 153 LDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
113-222 |
3.72e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 113 NFSNAATYE-KLLADYDQLQLD----YKDQGGYQYEAdIRSILSG----------LGFPVETHQTTISTLSGGQKTRLAL 177
Cdd:PRK00635 409 DYANAATWHgKTFAEFQQMSLQelfiFLSQLPSKSLS-IEEVLQGlksrlsilidLGLPYLTPERALATLSGGEQERTAL 487
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446524828 178 GKLLltKPDLL----ILDEPTNHL---DIETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK00635 488 AKHL--GAELIgityILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
167-201 |
4.22e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.47 E-value: 4.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET 201
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
166-222 |
4.47e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 4.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524828 166 TLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD-IETL-------TWLEQYlqgypgAILIVSHD 222
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLrieelmhELKEQY------TIIIVTHN 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-51 |
4.52e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446524828 3 LLQVNGLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAG 51
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
329-503 |
5.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.41 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 329 DVLQVKDATIGYDED---PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ------LLHGDVAFGSNV-----S 394
Cdd:PRK13650 3 NIIEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEaesgqiIIDGDLLTEENVwdirhK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 395 VGYYDQEQAN----LTSSKRVLNELWDE-YPLQPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLL 469
Cdd:PRK13650 83 IGMVFQNPDNqfvgATVEDDVAFGLENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524828 470 ILDEPTNHLD----LNSKEILENALIDYPGTLLFVSHD 503
Cdd:PRK13650 163 ILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-61 |
5.21e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.47 E-value: 5.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 3 LLQVNGLSKLYGAETIL---------ANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII 61
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-222 |
5.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524828 164 ISTLSGGQKT------RLALGKLLLTKPDLLILDEPTNHLDIET----LTWLEQYLQGYPGAIlIVSHD 222
Cdd:PRK03918 786 LTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERrrklVDIMERYLRKIPQVI-IVSHD 853
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
168-199 |
5.40e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 5.40e-04
10 20 30
....*....|....*....|....*....|..
gi 446524828 168 SGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-198 |
5.57e-04 |
|
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: 42.25 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKII-------AGELSHDGGEIIKPKDV--------SIGYLAQNTGLetslti 83
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKVLIDGQDIAAMSRKelrelrrkKISMVFQSFAL------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 84 wdemltvFTHLQQMETKLRRLE-QEMGKEENFSNAAtyeklladyDQLQL----DYKDQggyqyeadirsilsglgFPVE 158
Cdd:cd03294 114 -------LPHRTVLENVAFGLEvQGVPRAEREERAA---------EALELvgleGWEHK-----------------YPDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524828 159 thqttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:cd03294 161 --------LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-107 |
5.58e-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: 40.82 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 28 TKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpkdVSIGYLAQNTGLETSLTIWDEMLTVFTHLQQMETKLRRLEQE 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
443-529 |
5.65e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 443 KPVSSLSGGQKARLALAKLMM---QKSNLLILDEPTNHL---DLNSKEILENALIDYPGTLLFVSHDRYFInRVTTTVVE 516
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLE 883
|
90
....*....|...
gi 446524828 517 LSTEGAQeyLGDY 529
Cdd:PRK00635 884 LGPEGGN--LGGY 894
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-61 |
5.70e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446524828 8 GLSKLYGAETILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEII 61
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIL 56
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-503 |
5.79e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 41.73 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 345 IIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGSNVSVGYYDQEQANLTSskRVLNELWDEYPLQPE 424
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRN--QKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 425 keiRTILGNF---LFTGD-----------DVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK11629 102 ---FTALENVampLLIGKkkpaeinsralEMLAAVglehranhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180
....*....|....*....|....*..
gi 446524828 481 -NSKEILE--NALIDYPGT-LLFVSHD 503
Cdd:PRK11629 179 rNADSIFQllGELNRLQGTaFLVVTHD 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
164-328 |
5.84e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 164 ISTLSGGQKTRLALGKLLLT---KPDLLILDEPTNHL---DIETLTWLEQYL--QGYpgAILIVSHDRYFLdKLVTQVYE 235
Cdd:PRK00635 807 LSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLthQGH--TVVIIEHNMHVV-KVADYVLE 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 236 ISNKEsrrfvGNYSKYLdLKSALYEQEIKR----------YEKQQDEIAKLEDFVQK-NIARASTTKRA-QSRRKQLD-- 301
Cdd:PRK00635 884 LGPEG-----GNLGGYL-LASCSPEELIHLhtptakalrpYLSSPQELPYLPDPSPKpPVPADITIKNAyQHNLKHIDls 957
|
170 180 190
....*....|....*....|....*....|
gi 446524828 302 -RMELLTRPLGDSKSA--SFHFDIEKQSGN 328
Cdd:PRK00635 958 lPRNALTAVTGPSASGkhSLVFDILYAAGN 987
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
167-223 |
5.94e-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: 42.88 E-value: 5.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIETltwlEQYLQgypGAILIVSHDR 223
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT----ERAIQ---AALREVARGR 544
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
165-227 |
6.39e-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: 6.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 165 STLSGGQKTRLALGKLLL--TKPDLLILDEPTNHLDIETLTWLEQYLQGY---PGAILIVSHDRYFLD 227
Cdd:cd03238 86 STLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLS 153
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
446-502 |
6.63e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.55 E-value: 6.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524828 446 SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKEILENAL------IDYPgtLLFVSH 502
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLerlareINIP--ILYVSH 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-198 |
6.71e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 18 ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKPKdvSIGYLAQNTGLETSlTIWDEMLtVFThlqqm 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAWIMNA-TVRGNIL-FFD----- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 98 etklrrleqemgkEENfsnaatyEKLLADYDQLQldykdqggyQYEADIRSILSGLgfpvethQTTIS----TLSGGQKT 173
Cdd:PTZ00243 746 -------------EED-------AARLADAVRVS---------QLEADLAQLGGGL-------ETEIGekgvNLSGGQKA 789
|
170 180
....*....|....*....|....*
gi 446524828 174 RLALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PTZ00243 790 RVSLARAVYANRDVYLLDDPLSALD 814
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
346-503 |
7.14e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFGsNVSVGYYDQEQANLTSSKRV-------LNELWDE 418
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRPVRKRIgmvfqfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 419 yplQPEKEIR------------------TILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDL 480
Cdd:PRK13646 102 ---TVEREIIfgpknfkmnldevknyahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180
....*....|....*....|....*..
gi 446524828 481 NSK----EILENALIDYPGTLLFVSHD 503
Cdd:PRK13646 179 QSKrqvmRLLKSLQTDENKTIILVSHD 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
346-485 |
7.64e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFgSNVSVGYYDQEQA------------NLTSSKRVLN 413
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-QGKEIDFKSSKEAlengismvhqelNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 414 ELW-DEYPLQ-----PEKEIRTILGNFLFTGDDV--LKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNhlDLNSKEI 485
Cdd:PRK10982 93 NMWlGRYPTKgmfvdQDKMYRDTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS--SLTEKEV 170
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-198 |
8.45e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.65 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 19 LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGEIIKpKDVSIGYLAQNTgletsltiwdemltvfthlqqme 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV-DDTLITSTSKNK----------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 99 tKLRRLEQEMGKEENFSNAATYEK-LLADydqLQLDYKDQGGYQYEAD--IRSILSGLGFPVETHQTTISTLSGGQKTRL 175
Cdd:PRK13649 79 -DIKQIRKKVGLVFQFPESQLFEEtVLKD---VAFGPQNFGVSQEEAEalAREKLALVGISESLFEKNPFELSGGQMRRV 154
|
170 180
....*....|....*....|...
gi 446524828 176 ALGKLLLTKPDLLILDEPTNHLD 198
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLD 177
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-222 |
1.12e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 1 MILLQVNGLSKLYGAETI----LANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHdggeiikPKDVSIGYLAQNTg 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-------PGRVMAEKLEFNG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 77 letsltiwdemltvfTHLQQMETKLRRleQEMGKEEN--FSNAATyeKLLADYD---QLQLDYK-DQGGYQYEADIRSI- 149
Cdd:PRK11022 73 ---------------QDLQRISEKERR--NLVGAEVAmiFQDPMT--SLNPCYTvgfQIMEAIKvHQGGNKKTRRQRAId 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 150 -LSGLGFP-------VETHQttistLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD-------IETLTWLEQYLQgypG 214
Cdd:PRK11022 134 lLNQVGIPdpasrldVYPHQ-----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQKEN---M 205
|
....*...
gi 446524828 215 AILIVSHD 222
Cdd:PRK11022 206 ALVLITHD 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-479 |
1.45e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 355 RGDSVALVGPNGIGKSTLLKsivnklqLLHGDVA--FGSnvsvgyYDQEqanlTSSKRVLN-----ELWDEYPLQPEKEI 427
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALK-------ILSGELKpnLGD------YDEE----PSWDEVLKrfrgtELQDYFKKLANGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 428 RTILGN-------FLFTG---------------DDVL----------KPVSSLSGGQKARLALAKLMMQKSNLLILDEPT 475
Cdd:COG1245 161 KVAHKPqyvdlipKVFKGtvrellekvdergklDELAeklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 446524828 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 ... |
446-484 |
1.60e-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: 40.11 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446524828 446 SSLSGG--QKArlALAKLMMQKSNLLILDEPTNHLDLNSKE 484
Cdd:cd03215 103 SLLSGGnqQKV--VLARWLARDPRVLILDEPTRGVDVGAKA 141
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
330-529 |
1.66e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 330 VLQVKDATIGYDEDPIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNK--LQLLHGDVAFGSN--------------- 392
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllelspedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 393 ------------VSVGYYDQEQANLTSSKRVLNELwDEYPLQP--EKEIRtilgnFLFTGDDVL-KPVS-SLSGGQKARL 456
Cdd:PRK09580 81 fmafqypveipgVSNQFFLQTALNAVRSYRGQEPL-DRFDFQDlmEEKIA-----LLKMPEDLLtRSVNvGFSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524828 457 ALAKLMMQKSNLLILDEPTNHLDLNSKEILE---NALIDYPGTLLFVSHDRYFINRVTTTVVELSTEGAQEYLGDY 529
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
132-199 |
1.78e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 132 LDYKDQGGYQYEADIRSILSG----LGFPVETHQTTISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLDI 199
Cdd:PRK15439 365 LTHNRRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
448-479 |
2.10e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.60 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|..
gi 446524828 448 LSGGQKARLALAKLMMQKSNLLILDEPTNHLD 479
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
302-503 |
3.01e-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: 39.93 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 302 RMELLTRPLGDSKSASFHFDIEKQSGNDVLQVKDATIGydedpiIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQ 381
Cdd:cd03294 2 KIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVG------VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 382 LLHGDVAF-GSNVSvgyydqeqanlTSSKRVLNEL--------WDEYPLQPEkeiRTILGNFLF--------------TG 438
Cdd:cd03294 76 PTSGKVLIdGQDIA-----------AMSRKELRELrrkkismvFQSFALLPH---RTVLENVAFglevqgvpraereeRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 439 DDVLKPV----------SSLSGGQKARLALAKLMMQKSNLLILDEPTNHLD-LNSKEiLENALID----YPGTLLFVSHD 503
Cdd:cd03294 142 AEALELVglegwehkypDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRRE-MQDELLRlqaeLQKTIVFITHD 220
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
444-521 |
3.03e-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: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 444 PVSSLSGGQKARLALAKLMMQKSN---LLILDEPTN--HLDlNSKEILE--NALIDYPGTLLFVSHDRYFInRVTTTVVE 516
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTglHFD-DIKKLLEvlQRLVDKGNTVVVIEHNLDVI-KTADYIID 903
|
....*
gi 446524828 517 LSTEG 521
Cdd:TIGR00630 904 LGPEG 908
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-485 |
3.04e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 3.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446524828 440 DVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSK-EI 485
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKyEI 443
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-222 |
3.64e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 39.69 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 3 LLQVNGLSKLYGAET---ILANIKLEVQTKDRIALVGRNGAGKSTLLKIIAGELSHDGGeIIKPKDVSIgylaqntgleT 79
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELL----------T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 80 SLTIWDEMltvfthlqqmetklRRLEQEMGKEENFSNAATYEklladyDQLQLDYKDQGGYQYEADIRSILSGLGFPVET 159
Cdd:PRK13642 73 AENVWNLR--------------RKIGMVFQNPDNQFVGATVE------DDVAFGMENQGIPREEMIKRVDEALLAVNMLD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524828 160 HQT-TISTLSGGQKTRLALGKLLLTKPDLLILDEPTNHLD----IETLTWLEQYLQGYPGAILIVSHD 222
Cdd:PRK13642 133 FKTrEPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
344-376 |
3.79e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.83 E-value: 3.79e-03
10 20 30
....*....|....*....|....*....|...
gi 446524828 344 PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSI 376
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV 50
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
328-503 |
3.83e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.22 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 328 NDVLQVKDATIGYDED----PIIEHVNMRLTRGDSVALVGPNGIGKSTLLKSIVNKLQLLHGDVAFG-------SNVSVG 396
Cdd:PRK10261 10 RDVLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 397 YYDQEQANL----------------TS-------------SKRVLNELWDEYPLQPEK---------EIRTILGNFlftg 438
Cdd:PRK10261 90 LSEQSAAQMrhvrgadmamifqepmTSlnpvftvgeqiaeSIRLHQGASREEAMVEAKrmldqvripEAQTILSRY---- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 439 ddvlkpVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLN-SKEILEnaLI-----DYPGTLLFVSHD 503
Cdd:PRK10261 166 ------PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiQAQILQ--LIkvlqkEMSMGVIFITHD 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
167-231 |
3.91e-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: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524828 167 LSGGQKTRLALGKLLLTKPDLLILDEPTNHLDIET---------LTWLEQYLQGYPGAILIVSHDRYFLDKLVT 231
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
346-441 |
4.11e-03 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 39.28 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDS---VALVGPNGIGKSTLLKSIVNKLQLLHG--DVAFGSNVSvGYYDQEQANLTSSKRVL--NELWDE 418
Cdd:pfam00931 5 VEKVIGKLSEKDEpgiVGIHGMGGVGKTTLAAQIFNDFDEVEGhfDSVAWVVVS-KTFTISTLQQTILQNLGlsEDDWDN 83
|
90 100
....*....|....*....|....*.
gi 446524828 419 YP-LQPEKEIRTIL--GNFLFTGDDV 441
Cdd:pfam00931 84 KEeGELARKIRRALltKRFLLVLDDV 109
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
346-492 |
6.12e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.00 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 346 IEHVNMRLTRGDSVALVGPNGIGKSTLLKSI------------VNKLQLLHGDVAFGSNVSVGYYDQEQANLTSSKRVLN 413
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLagmieptsgellIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 414 ELwdEYPL---------QPEKEIRTILGNFLFTGDDVLKPVSSLSGGQKARLALAKLMMQKSNLLILDEPTNHLDLNSKE 484
Cdd:PRK15112 109 IL--DFPLrlntdlepeQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
....*...
gi 446524828 485 ILENALID 492
Cdd:PRK15112 187 QLINLMLE 194
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
585-641 |
6.13e-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: 6.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524828 585 IEELEQNIVSLEEEIATLEDQlclpEIYADYEKASEITTKKQTLQEQLEACMAEWEE 641
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKE----QDEASFERLAELRDELAELEEELEALKARWEA 465
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
34-50 |
6.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.59 E-value: 6.62e-03
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-87 |
6.71e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 6.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 36 GRNGAGKSTLLKIIAGELSHDGGEIIKpKDVSI--------GYLAQNTGLETSLTIWDEM 87
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-KNCNInniakpycTYIGHNLGLKLEMTVFENL 91
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
434-508 |
6.79e-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: 38.91 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 434 FLFTGDDVLKPVSSLSGGQKARLALAKLMM---QKSNLLILDEPTNHLD-LNSKEILE--NALIDYPGTLLFVSHDRYFI 507
Cdd:pfam13304 223 LLENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHpKLLRRLLEllKELSRNGAQLILTTHSPLLL 302
|
.
gi 446524828 508 N 508
Cdd:pfam13304 303 D 303
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
562-643 |
7.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524828 562 AQEKLNYLEEKER----KQLERQRTRK-IEELEQNIVSLEEEIATLEDQLCLPEIYADYEKASEITTKKQTLQEQLEACM 636
Cdd:COG4717 76 LEEELKEAEEKEEeyaeLQEELEELEEeLEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
....*..
gi 446524828 637 AEWEELH 643
Cdd:COG4717 156 EELRELE 162
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
445-504 |
7.31e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 7.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524828 445 VSSLSGGQKA------RLALAKLMMQKSNLLILDEPTNHLD----LNSKEILENALIDYPG--TLLFVSHDR 504
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrrTNLKDIIEYSLKDSSDipQVIMISHHR 870
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
164-221 |
8.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 8.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524828 164 ISTLSGGQKT------RLALGKLLLTKPDLLILDEPTNHLDIETLTWLEQYLQ-------GYPGAILIVSH 221
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEyslkdssDIPQVIMISHH 869
|
|
| |
