|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-637 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 733.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLDRLA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VDYVLDGDSRLREIQAALAVAEAAHDGSALARLHTELDNADGYTADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNL 160
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 161 AQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSAFERTRAE 240
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 241 RLAQQQQAYEKQQAQRAHMESFIARFKAKATKARQAQSRIKALERLEELAPAHVDSPFNFSFRESDKISRPLLDLGEGRL 320
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQLDSLDPQASPLLHLQR 400
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 IAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGAV 480
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 481 LVVSHDRHLLKSTTDEFLLVADGRVVPFDGDLDDYARWLVDYRaRKAPQAETAPGAPTERT--DKRAQRQAAAALRQQLA 558
Cdd:PRK10636 481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQ-KQENQTDEAPKENNANSaqARKDQKRREAELRTQTQ 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 559 PHKREADKLERELGGLHEKLAAIEARLGDSALYDVSRKDELRELLSEQSSLKVREGELEERWLEALETLEALQKELEAS 637
Cdd:PRK10636 560 PLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN 638
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-518 |
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: 672.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLDRLAV-DYV 84
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVlDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 85 LDGDSRLREIQA-----ALAVAEAAHDGSALARLHTELDNADGYTADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLN 159
Cdd:COG0488 83 LDGDAELRALEAeleelEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 160 LAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSAFERTRA 239
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 240 ERLAQQQQAYEKQQAQRAHMESFIARFKAKATKARQAQSRIKALERLEELAPAHVDSPFNFSFRESDKISRPLLDLGEGR 319
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEGLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQlDSLDPQASPLLHLQ 399
Cdd:COG0488 323 KSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDELR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 400 RIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGA 479
Cdd:COG0488 402 DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGT 481
|
490 500 510
....*....|....*....|....*....|....*....
gi 15600445 480 VLVVSHDRHLLKSTTDEFLLVADGRVVPFDGDLDDYARW 518
Cdd:COG0488 482 VLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-519 |
1.89e-129 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 397.69 E-value: 1.89e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLfalLRgQLGQDAGDCLlPADWRIAHMRQEVDTLDRLAV 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTF---LR-YMAMHAIDGI-PKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDGD----------SRLREIQAALAVAEAAHDGSA--------------LARLHTELDNADGYTADARARKLLAGLG 137
Cdd:PLN03073 253 QCVLNTDiertqlleeeAQLVAQQRELEFETETGKGKGankdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 138 FSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVV 217
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 218 HLENRKLTLYRGGYSAFERTRAERLAQQQQAYEKQQAQRAHMESFIARFKAKATKARQAQSRIKALERLEELAPAHVDSP 297
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 298 FNFSF-RESDKISRPLLDLGEGRLGY-GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENL 375
Cdd:PLN03073 493 YKFEFpTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 376 AIGYFAQHQLDSLDPQASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLD 455
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 456 EPTNHLDLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFDGDLDDYARWL 519
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTL 716
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-517 |
1.37e-106 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 332.24 E-value: 1.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQevdtlDRLA 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ-----DQFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 ------VDYVLDGDSRLREIQAA-----LAVAEAAHDGSALARLHTELDNADGYTADARARKLLAGLGFSSEQMERRVGD 149
Cdd:PRK15064 76 feeftvLDTVIMGHTELWEVKQErdriyALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 150 FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRG 229
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 230 GYSAF--ERTRA-ERLAQQQQAYEKQQaqrAHMESFIARFKAKATKARQAQSRIKALER--LEELAPAHVDSPFnFSFRE 304
Cdd:PRK15064 236 NYDEYmtAATQArERLLADNAKKKAQI---AELQSFVSRFSANASKAKQATSRAKQIDKikLEEVKPSSRQNPF-IRFEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 305 SDKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQhq 384
Cdd:PRK15064 312 DKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 lDSLDPQASPLLHLQRIA----PGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNH 460
Cdd:PRK15064 390 -DHAYDFENDLTLFDWMSqwrqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 461 LDLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFDGDLDDYAR 517
Cdd:PRK15064 469 MDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLR 525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-633 |
1.45e-79 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 264.51 E-value: 1.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQ-----EVDT 75
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 76 LdrlaVDYVLDGDSRLREI--QAALAVAEAAHDGSA-----LARLHTELDNADGYTADARARKLLAGLGFSSEQmerRVG 148
Cdd:PRK11147 83 V----YDFVAEGIEEQAEYlkRYHDISHLVETDPSEknlneLAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 149 DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYR 228
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 229 GGYSAFERTRAERLAQQQQAYEKQQAQRAHMESFIaRFKAKATKARQaQSRIKAL--------ERLEELAPAhvdspfNF 300
Cdd:PRK11147 236 GNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWI-RQGIKARRTRN-EGRVRALkalrrersERREVMGTA------KM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 301 SFRESDKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYF 380
Cdd:PRK11147 308 QVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 381 AQHQLDsLDPQASPLLHLqriAPGEREQT-----------LKDFLggfdFRGVRVDEPVLNFSGGEKARLALALIAWQKP 449
Cdd:PRK11147 388 DQHRAE-LDPEKTVMDNL---AEGKQEVMvngrprhvlgyLQDFL----FHPKRAMTPVKALSGGERNRLLLARLFLKPS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 450 NLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVVSHDRHLLKST-TDEFLLVADGRVVPFDGDLDDYARWLVDYRARKAP 528
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTvTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 529 QAETAPGAPTERTDkraqrqaaaalrqqlaPHKREADKL----ERELGGLHEKLAAIEARL-------GDSALYDVSrKD 597
Cdd:PRK11147 540 AVKKKEEAAAPKAE----------------TVKRSSKKLsyklQRELEQLPQLLEDLEAEIealqaqvADADFFSQP-HE 602
|
650 660 670
....*....|....*....|....*....|....*....
gi 15600445 598 ELRELLSEqssLKVREGELE---ERWlealETLEALQKE 633
Cdd:PRK11147 603 QTQKVLAD---LADAEQELEvafERW----EELEALKNG 634
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-530 |
1.75e-69 |
|
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: 235.60 E-value: 1.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQR-LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqLGQD-AGDCLLPADWRIAHMRQE--VD-TLD-----RLAV 81
Cdd:TIGR03719 15 PPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDfNGEARPQPGIKVGYLPQEpqLDpTKTvrenvEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDGDSRLREIQAALAVAEAAHDGSA--LARLHTELDNADGYTADAR------ARKLLAGlgfsseqmERRVGDFSGG 153
Cdd:TIGR03719 94 AEIKDALDRFNEISAKYAEPDADFDKLAaeQAELQEIIDAADAWDLDSQleiamdALRCPPW--------DADVTKLSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 154 WRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSA 233
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 234 FERTRAERLaqqqqayekqqAQRAHMESfiARFKA---------KATKARQAQSriKA-LERLEELAPAHVDSPfnfsfR 303
Cdd:TIGR03719 246 WLEQKQKRL-----------EQEEKEES--ARQKTlkrelewvrQSPKGRQAKS--KArLARYEELLSQEFQKR-----N 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 304 ESDKISRPlldLGEgRLG------------YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLR 371
Cdd:TIGR03719 306 ETAEIYIP---PGP-RLGdkvieaenltkaFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 372 GENLAIGYFAQHQlDSLDPQASPLLH----LQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQ 447
Cdd:TIGR03719 382 GETVKLAYVDQSR-DALDPNKTVWEEisggLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 448 KPNLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFL-LVADGRVVPFDGDLDDYARwlvDYRARK 526
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILaFEGDSHVEWFEGNFSEYEE---DKKRRL 537
|
....
gi 15600445 527 APQA 530
Cdd:TIGR03719 538 GEDA 541
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-530 |
4.34e-62 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 215.75 E-value: 4.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 27 GQKAGLIGANGAGKSSLfalLRGQLGQDA---GDCLLPADWRIAHMRQEVDtLD---------RLAVDYVLDGDSRLREI 94
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTL---LRIMAGVDKefeGEARPAPGIKVGYLPQEPQ-LDpektvrenvEEGVAEVKAALDRFNEI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 95 QAALAVAEAAHDgsAL----ARLHTELDNADGYTADArarkllaglgfsseQMER------------RVGDFSGGWRMRL 158
Cdd:PRK11819 109 YAAYAEPDADFD--ALaaeqGELQEIIDAADAWDLDS--------------QLEIamdalrcppwdaKVTKLSGGERRRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSAFERTR 238
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 239 AERLAQQQQAyekqqaqrahmESfiARFKA---------KATKARQAQSriKA-LERLEELApahvdspfNFSFRESDKI 308
Cdd:PRK11819 253 AKRLAQEEKQ-----------EA--ARQKAlkrelewvrQSPKARQAKS--KArLARYEELL--------SEEYQKRNET 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRPLLDLGEgRLG------------YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLA 376
Cdd:PRK11819 310 NEIFIPPGP-RLGdkvieaenlsksFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 377 IGYFAQHQlDSLDPQAS---------PLLHLqriapGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQ 447
Cdd:PRK11819 389 LAYVDQSR-DALDPNKTvweeisgglDIIKV-----GNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 448 KPNLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVVSHDR--------HLLksttdefllvA---DGRVVPFDGDLDDYA 516
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRwfldriatHIL----------AfegDSQVEWFEGNFQEYE 532
|
570
....*....|....
gi 15600445 517 RwlvDYRARKAPQA 530
Cdd:PRK11819 533 E---DKKRRLGADA 543
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-236 |
8.65e-50 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 181.03 E-value: 8.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLD--R 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDpdK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 79 LAVDYVLDGDSRLREIQaalavaeaahdgsalarlhteldnadgytadarARKLLAGLGFSSEQMERRVGDFSGGWRMRL 158
Cdd:COG0488 395 TVLDELRDGAPGGTEQE---------------------------------VRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSAFER 236
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-504 |
1.16e-49 |
|
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: 169.55 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQhqldsldpqaspllhlq 399
Cdd:cd03221 8 KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 400 riapgereqtlkdflggfdfrgvrvdepvlnFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGA 479
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGT 119
|
170 180
....*....|....*....|....*
gi 15600445 480 VLVVSHDRHLLKSTTDEFLLVADGR 504
Cdd:cd03221 120 VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-223 |
2.95e-48 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 165.70 E-value: 2.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQevdtldrlav 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 dyvldgdsrlreiqaalavaeaahdgsalarlhteldnadgytadararkllaglgfsseqmerrvgdFSGGWRMRLNLA 161
Cdd:cd03221 71 --------------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRK 223
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
320-571 |
3.60e-39 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 151.37 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQ------------LDS 387
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPpldddltvldtvLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQASPLLHLQRI--------APGER----------------EQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALAL 443
Cdd:COG0488 86 DAELRALEAELEELeaklaepdEDLERlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 444 IAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFDGDLDDYARWlvdyR 523
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ----R 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15600445 524 ArkapqaetapgaptERtdkraqrqaaaaLRQQLAPHKREADKLEREL 571
Cdd:COG0488 242 A--------------ER------------LEQEAAAYAKQQKKIAKEE 263
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-514 |
5.20e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 139.27 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSL-FALLRgqlgqdagdcLLPADWRIAHmRQEVDTLDRLA 80
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLaLALMG----------LLPHGGRISG-EVLLDGRDLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 vdyvLDGDSRLREI----QAALAVAEAAHDGSALArLHTELDNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWRM 156
Cdd:COG1123 76 ----LSEALRGRRIgmvfQDPMTQLNPVTVGDQIA-EALENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLDLDA---ILWLEEWLKGYPG-TLVLISHDRDFLDAVVDHVVHLenrkltlyRGGYS 232
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVM--------DDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 233 AFERTRAERLAqqqqayekqqaqRAHMESFIARFKAKATKARQAQSRIKALERLEELapahvdspfNFSFRESDKisrpl 312
Cdd:COG1123 222 VEDGPPEEILA------------APQALAAVPRLGAARGRAAPAAAAAEPLLEVRNL---------SKRYPVRGK----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 313 ldlgegrlgyGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--------------DLPELGGRLLRGENLAIG 378
Cdd:COG1123 276 ----------GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSLRELRRRVQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 379 YFAQHQLDSLDPQ-------ASPLLHLQRIAPGEREQTLKDFLggfdfRGVRVDEPVLN-----FSGGEKARLALA--LI 444
Cdd:COG1123 346 MVFQDPYSSLNPRmtvgdiiAEPLRLHGLLSRAERRERVAELL-----ERVGLPPDLADrypheLSGGQRQRVAIAraLA 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 445 AwqKPNLLLLDEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:COG1123 421 L--EPKLLILDEPTSALDVSVQaqiLNLLRDLQrELGLTYLFISHDLAVVRYIADRVAVMYDGRIV-EDGPTEE 491
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
320-515 |
3.06e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLAIGYFAQHQldSLDPQ-- 391
Cdd:COG1121 14 VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPptsgtvRLFGKPPRRARRRIGYVPQRA--EVDWDfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 -------ASPLLH----LQRIAPGEREQTLK--DFLGGFDFRGVRVDEpvlnFSGGEKAR--LALALIawQKPNLLLLDE 456
Cdd:COG1121 92 itvrdvvLMGRYGrrglFRRPSRADREAVDEalERVGLEDLADRPIGE----LSGGQQQRvlLARALA--QDPDLLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 457 PTNHLDLEMRLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVvpFDGDLDDY 515
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEV 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-506 |
6.99e-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: 6.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA----------IGYFAQHQLDS 387
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvLLDGRDLAslsrrelarrIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LD------------PQASPllhLQRIAPGEREQTLK--DFLGGFDFRGVRVDEpvlnFSGGEKAR--LALALIawQKPNL 451
Cdd:COG1120 88 FGltvrelvalgryPHLGL---FGRPSAEDREAVEEalERTGLEHLADRPVDE----LSGGERQRvlIARALA--QEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 452 LLLDEPTNHLDLEMRLALTMALQEFSG----AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARergrTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
322-505 |
1.22e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 112.49 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLrgenlaigyfaqhqLDSLDPQASPLLHLQRI 401
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------------VLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 402 A--PGEReqTLKDFLGGFDFrgvrvdepvLNFSGGEKARLAL--ALIAwqKPNLLLLDEPTNHLDLEMRLALTMALQEFS 477
Cdd:cd03230 76 GylPEEP--SLYENLTVREN---------LKLSGGMKQRLALaqALLH--DPELLILDEPTSGLDPESRREFWELLRELK 142
|
170 180 190
....*....|....*....|....*....|.
gi 15600445 478 ---GAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:cd03230 143 kegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
320-506 |
3.13e-28 |
|
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: 111.37 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAigyfaqhqldsldpQASPLLHL 398
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEiLLDGKDLA--------------SLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 399 QRIA--PgereQTLKDfLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALtMAL--- 473
Cdd:cd03214 73 RKIAyvP----QALEL-LGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL-LELlrr 142
|
170 180 190
....*....|....*....|....*....|....*
gi 15600445 474 --QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03214 143 laRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-242 |
3.50e-28 |
|
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: 119.27 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLDrlavdyvl 85
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALD-------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 DGDSRLREIQaalavaeaahDGSALARLhteldnaDGYTADARArkLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALM 165
Cdd:TIGR03719 399 PNKTVWEEIS----------GGLDIIKL-------GKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 166 CPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLE-NRKLTLYRGGYSAFERTRAERL 242
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEDKKRRL 537
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
217-300 |
3.98e-28 |
|
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: 107.66 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 217 VHLENRKLTLYRGGYSAFERTRAERLAQQQQAYEKQQAQRAHMESFIARFKAKATKARQAQSRIKALERLEELAPAHVDS 296
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 15600445 297 P-FNF 300
Cdd:pfam12848 81 PkLRF 85
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
323-525 |
5.06e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 118.68 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQH-QLD-----------SLDP 390
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpQLDpektvrenveeGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 QASPLLHLQRIA------PGEREQTLK---------DFLGGFDF-RGVRV----------DEPVLNFSGGEKARLALALI 444
Cdd:PRK11819 98 VKAALDRFNEIYaayaepDADFDALAAeqgelqeiiDAADAWDLdSQLEIamdalrcppwDAKVTKLSGGERRRVALCRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 445 AWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFDGdldDYARWLVDYRA 524
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG---NYSSWLEQKAK 254
|
.
gi 15600445 525 R 525
Cdd:PRK11819 255 R 255
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
322-514 |
1.97e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLA----IGYFAQHqlDSLDPQ 391
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsgevRVLGEDVARDPAEvrrrIGYVPQE--PALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQRIA------PGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEM 465
Cdd:COG1131 88 LTVRENLRFFArlyglpRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600445 466 RLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:COG1131 167 RRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRIV-ADGTPDE 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
323-504 |
1.01e-26 |
|
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: 107.94 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA----------IGY---FAQHQLDSL 388
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGKDLTklslkelrrkVGLvfqNPDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQ---ASPLLHLQrIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEM 465
Cdd:cd03225 92 TVEeevAFGLENLG-LPEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 466 RLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGR 504
Cdd:cd03225 170 RRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
322-514 |
1.44e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 108.79 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLAI-GYFAQHQLDSLdPQASPL---- 395
Cdd:COG4555 11 YGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPDSGSILIDGEDVRKePREARRQIGVL-PDERGLydrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 -----LH----LQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR 466
Cdd:COG4555 90 tvrenIRyfaeLYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600445 467 LALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:COG4555 169 RLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
320-506 |
1.52e-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: 107.62 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLAIGYFAQH-QLD------ 386
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKptsgsiRVFGKPLEKERKRIGYVPQRrSIDrdfpis 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 387 -------SLDPQASPLLHLQRIAPGEREQTLKdFLGGFDFRGVRVDEpvlnFSGGEKARLALALIAWQKPNLLLLDEPTN 459
Cdd:cd03235 87 vrdvvlmGLYGHKGLFRRLSKADKAKVDEALE-RVGLSELADRQIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 460 HLDLEMR---LALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVaDGRVV 506
Cdd:cd03235 162 GVDPKTQediYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
328-459 |
3.34e-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: 104.65 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA----------IGYFAQHqlDSLDPQAS--- 393
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTiLLDGQDLTdderkslrkeIGYVFQD--PQLFPRLTvre 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 394 ------PLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTN 459
Cdd:pfam00005 79 nlrlglLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-217 |
6.33e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.60 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEVdtLDRLAV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV-LGEDVARDPAEV--RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 ---DYVLDGDSRLREIqaalavaeaahdgsalARLHTELDNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWRMRL 158
Cdd:COG1131 78 vpqEPALYPDLTVREN----------------LRFFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY--PGTLVLIS-HDRDFLDAVVDHVV 217
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-223 |
4.60e-24 |
|
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: 100.25 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLlpadWRIAHMRQEVDTLDRLA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VdYV-----LDGDSRLREiqaalavaeaahdgsaLARLHTELDNADGytADARARKLLAGLGFSsEQMERRVGDFSGGWR 155
Cdd:COG4133 78 A-YLghadgLKPELTVRE----------------NLRFWAALYGLRA--DREAIDEALEAVGLA-GLADLPVRQLSAGQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYP---GTLVLISHDRDFLDAvvDHVVHLENRK 223
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
317-504 |
1.06e-23 |
|
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: 97.70 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 317 EGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAigyfaqhqldsldpQASPL 395
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEiLIDGKDIA--------------KLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 LHLQRIApgereqtlkdFLGGFdfrgvrvdepvlnfSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQE 475
Cdd:cd00267 70 ELRRRIG----------YVPQL--------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|..
gi 15600445 476 FSG---AVLVVSHDRHLLKSTTDEFLLVADGR 504
Cdd:cd00267 126 LAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-511 |
1.36e-23 |
|
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: 99.71 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLA-----IGY---FAQHQLdsl 388
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsgevLVDGKDITKKNLRelrrkVGLvfqNPDDQL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 dpqASP---------LLHLqRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALA-LIAwQKPNLLLLDEPT 458
Cdd:COG1122 89 ---FAPtveedvafgPENL-GLPREEIRERVEEALELVGLEHLA-DRPPHELSGGQKQRVAIAgVLA-MEPEVLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 459 NHLDLEMRLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRVVpFDGD 511
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRIV-ADGT 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
301-510 |
1.50e-23 |
|
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: 99.53 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 301 SFRESDKISRPLLDLG--EGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGEN---- 374
Cdd:cd03220 9 SYPTYKGGSSSLKKLGilGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 375 LAIGYFaqhqldsLDPQAS---------PLLHLQRIAPGEREQTLKDF--LGGFdfrgvrVDEPVLNFSGGEKARLALAL 443
Cdd:cd03220 89 LGLGGG-------FNPELTgreniylngRLLGLSRKEIDEKIDEIIEFseLGDF------IDLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 444 IAWQKPNLLLLDEPTNHLDLEMRLALTMALQEF---SGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDG 510
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKIR-FDG 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-242 |
2.77e-23 |
|
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: 99.16 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEVdtldRLA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREA----RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VDYVLDGD---SRL--REIqaalavaeaahdgsalARLHTELDNADGYTADARARKLLAGLGFsSEQMERRVGDFSGGWR 155
Cdd:COG4555 76 IGVLPDERglyDRLtvREN----------------IRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEE---WLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLtLYRGGYS 232
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGSLD 217
|
250
....*....|.
gi 15600445 233 AF-ERTRAERL 242
Cdd:COG4555 218 ELrEEIGEENL 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-223 |
2.88e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 98.31 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 5 LNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP----ADWRIAHMRQEVDTL---- 76
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRKVGLVfqnp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 -DRLAVDYVLDgdsrlrEIqaalavaeaahdgsALARLHTELDNADgytADARARKLLAGLGFSsEQMERRVGDFSGGWR 155
Cdd:cd03225 85 dDQFFGPTVEE------EV--------------AFGLENLGLPEEE---IEERVEEALELVGLE-GLRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG---TLVLISHDRDFLDAVVDHVVHLENRK 223
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-224 |
2.91e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.96 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR--IAHMR 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkplsampPPEWRrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 71 QEVDTLDRLAVDYvLDGDSRLREIQAAlavaeaahdgsalarlhteldnadgytaDARARKLLAGLGFSSEQMERRVGDF 150
Cdd:COG4619 81 QEPALWGGTVRDN-LPFPFQLRERKFD----------------------------RERALELLERLGLPPDILDKPVERL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 151 SGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDA----ILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
322-498 |
3.09e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 99.42 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQldSLDPQAsPLL--HLQ 399
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL--YLDTTL-PLTvnRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 400 RIAPGEREQTLKDFLGGFDfRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMAL----QE 475
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIdqlrRE 169
|
170 180
....*....|....*....|...
gi 15600445 476 FSGAVLVVSHDRHLLKSTTDEFL 498
Cdd:PRK09544 170 LDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
319-505 |
1.72e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.04 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA----------IGYFAQH-QL- 385
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTSGEIYLDGKPLSampppewrrqVAYVPQEpALw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 -DSLDPQASPLLHLQRIAPgeREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE 464
Cdd:COG4619 87 gGTVRDNLPFPFQLRERKF--DRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 465 MRLALTMALQEFS----GAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:COG4619 165 NTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
311-514 |
2.06e-22 |
|
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: 96.69 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 311 PLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP-------ELGGRLLRGENLA-----IG 378
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvRLFGERRGGEDVWelrkrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 379 YFAQHQLDSLDPQASPL------------LHlQRIAPGEREQTLK--DFLGGFDFRgvrvDEPVLNFSGGEKAR--LALA 442
Cdd:COG1119 82 LVSPALQLRFPRDETVLdvvlsgffdsigLY-REPTDEQRERAREllELLGLAHLA----DRPFGTLSQGEQRRvlIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 443 LIAwqKPNLLLLDEPTNHLDLEMRLALTMALQEFSG----AVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:COG1119 157 LVK--DPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTHHVEEIPPGITHVLLLKDGRVV-AAGPKEE 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
322-486 |
1.66e-21 |
|
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: 92.93 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENL---------AIGYFAQHqlDSLDPQ 391
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvLWNGEPIrdaredyrrRLAYLGHA--DGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASP---LLHLQRIAPGER-EQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRL 467
Cdd:COG4133 90 LTVrenLRFWAALYGLRAdREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180
....*....|....*....|..
gi 15600445 468 ALTMALQEFS---GAVLVVSHD 486
Cdd:COG4133 169 LLAELIAAHLargGAVLLTTHQ 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-225 |
3.30e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 91.93 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 10 QRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLDRLAVDYVLDGDS 89
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 90 RLREIQaalavaeaahdgsalarlhteLDNADGYTADARARKLLAGLGFsSEQMERRVGDFSGGWRMRLNLAQALMCPSD 169
Cdd:cd03226 89 VREELL---------------------LGLKELDAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 170 LLLLDEPTNHLDLDAILWLEEW---LKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLT 225
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-178 |
5.53e-21 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 89.63 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADWRIAHMRQEVDTLDRlavDYVLDGDSRLREIqaa 97
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdLTDDERKSLRKEIGYVFQ---DPQLFPRLTVREN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 98 lavaeaahdgSALARLHTELDNADgytADARARKLLAGLGFSsEQMERRVGD----FSGGWRMRLNLAQALMCPSDLLLL 173
Cdd:pfam00005 80 ----------LRLGLLLKGLSKRE---KDARAEEALEKLGLG-DLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLL 145
|
....*
gi 15600445 174 DEPTN 178
Cdd:pfam00005 146 DEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-506 |
5.64e-21 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 92.18 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--------------DLPELGGRLLRGENLAIGYFAQHQ 384
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRKIRRKEIQMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 LDSLDPQ-------ASPLLHLQRIAPGEREQTLKDFLggfdFRGVRVDEPVLN-----FSGGEKAR--LALALIAwqKPN 450
Cdd:cd03257 92 MSSLNPRmtigeqiAEPLRIHGKLSKKEARKEAVLLL----LVGVGLPEEVLNrypheLSGGQRQRvaIARALAL--NPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 451 LLLLDEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03257 166 LLIADEPTSALDVSVQaqiLDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-224 |
7.24e-21 |
|
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: 90.15 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADWRIAHMRQevdtld 77
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdIKKEPEEVKRR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 78 rlaVDYVLDGDSrlreiqaalavaeaahdgsalarLHTELdnadgytadaRARKLLaglgfsseqmerrvgDFSGGWRMR 157
Cdd:cd03230 75 ---IGYLPEEPS-----------------------LYENL----------TVRENL---------------KLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 158 LNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY---PGTLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
322-506 |
7.76e-21 |
|
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: 91.12 E-value: 7.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAIGYFAQHQLDSLdpQASPLLHLQR 400
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEiTFDGKSYQKNIEALRRIGAL--IEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 IApgeREQtLKDFLGGFDFRGVRVDE-------------PVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD----L 463
Cdd:cd03268 88 TA---REN-LRLLARLLGIRKKRIDEvldvvglkdsakkKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgiK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600445 464 EMRlALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03268 164 ELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
301-514 |
2.42e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 301 SFRESDKISRPLLD--LGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL---------------- 362
Cdd:COG1134 13 SYRLYHEPSRSLKEllLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILeptsgrvevngrvsal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 363 --------PELGGRllrgENlaIGYFAQhqldsldpqaspLLHLQRIAPGEREQTLKDF--LGGFdfrgvrVDEPVLNFS 432
Cdd:COG1134 93 lelgagfhPELTGR----EN--IYLNGR------------LLGLSRKEIDEKFDEIVEFaeLGDF------IDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 433 GGEKARLALALIAWQKPNLLLLDEptnhldlemrlAL-----------TMALQEF---SGAVLVVSHDRHLLKSTTDEFL 498
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDE-----------VLavgdaafqkkcLARIRELresGRTVIFVSHSMGAVRRLCDRAI 217
|
250
....*....|....*.
gi 15600445 499 LVADGRVVpFDGDLDD 514
Cdd:COG1134 218 WLEKGRLV-MDGDPEE 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-239 |
3.13e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 94.57 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQevDTLDRLAVDY-V 84
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ--DHAYDFENDLtL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 85 LDGDSRLReiqaalavaeaahdgsalarlhTELDNadgytaDARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQAL 164
Cdd:PRK15064 402 FDWMSQWR----------------------QEGDD------EQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 165 MCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSAFERTRA 239
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQG 528
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
3.21e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 90.15 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL------PADWRIAHM--RQE 72
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 73 VDTLDRLAV-DYVLDGdsRLREIqaalavaeaahdgSALARLHTEldnadgytADARARKLLAGLGFSsEQMERRVGDFS 151
Cdd:COG1121 86 VDWDFPITVrDVVLMG--RYGRR-------------GLFRRPSRA--------DREAVDEALERVGLE-DLADRPIGELS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 152 GGWRMRLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLeNRKL 224
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAateEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
321-499 |
4.18e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQ--LDSLD--------- 389
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSevPDSLPltvrdlvam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 ---PQASPLLHLQRIAPGEREQTLkDFLGGFDFRGVRVDEpvlnFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR 466
Cdd:NF040873 81 grwARRGLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600445 467 LALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLL 499
Cdd:NF040873 156 ERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
322-506 |
5.72e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.83 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLrgenlaigyFAQHQLDSLD-----------P 390
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR---------LNGRPLADWSpaelarrravlP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 QASPL-------------LHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQ------KPNL 451
Cdd:PRK13548 83 QHSSLsfpftveevvamgRAPHGLSRAEDDALVAAALAQVDLAHLA-GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 452 LLLDEPTNHLDLE-----MRLALTMALQEfSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13548 162 LLLDEPTSALDLAhqhhvLRLARQLAHER-GLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-504 |
8.14e-20 |
|
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: 87.05 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA-IGYFAQHQLDSLDPQASPLLHlqr 400
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEiLIDGVDLRdLDLESLRKNIAYVPQDPFLFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 iapgereQTLKDflggfdfrgvrvdepvlN-FSGGEKARLALA--LIawQKPNLLLLDEPTNHLDLEMRLALTMALQEFS 477
Cdd:cd03228 90 -------GTIRE-----------------NiLSGGQRQRIAIAraLL--RDPPILILDEATSALDPETEALILEALRALA 143
|
170 180
....*....|....*....|....*....
gi 15600445 478 G--AVLVVSHDRHLLKStTDEFLLVADGR 504
Cdd:cd03228 144 KgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-506 |
9.38e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENlAIGYFAQHQLD---SLDPQA---- 392
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-PISMLSSRQLArrlALLPQHhltp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 -------------SPLLHL-QRIAPGER-------EQTLKDFLggfdfrgvrVDEPVLNFSGGEKARLALALIAWQKPNL 451
Cdd:PRK11231 89 egitvrelvaygrSPWLSLwGRLSAEDNarvnqamEQTRINHL---------ADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 452 LLLDEPTNHLDLEMRLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQgktVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
320-506 |
1.29e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.02 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLaigyfAQHQLDSLD------PQA 392
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvRLNGRPL-----AAWSPWELArrravlPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPL-------------LHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKAR--LA--LALIaWQ----KPNL 451
Cdd:COG4559 84 SSLafpftveevvalgRAPHGSSAAQDRQIVREALALVGLAHLA-GRSYQTLSGGEQQRvqLArvLAQL-WEpvdgGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 452 LLLDEPTNHLDLE-----MRLALTMALQEfsGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG4559 162 LFLDEPTSALDLAhqhavLRLARQLARRG--GGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-462 |
1.63e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 92.00 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 15 RLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADwRIAHMRQEvdTLDRLAVDyvldgdsrlrEI 94
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFS-HITRLSFE--QLQKLVSD----------EW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 95 QaalavaeaahdgsalaRLHTELDNAD----GYTA----------DARARKLLAGLGFSSeQMERRVGDFSGGWRMRLNL 160
Cdd:PRK10938 84 Q----------------RNNTDMLSPGeddtGRTTaeiiqdevkdPARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 161 AQALMCPSDLLLLDEPTNHLDLDAILWLEEWL-----KGYpgTLVLISHDRDFLDAVVDHVVHLENRKLTLyrggysafE 235
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLaslhqSGI--TLVLVLNRFDEIPDFVQFAGVLADCTLAE--------T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 236 RTRAERLaqqqqayekqqaqrahmesfiarfkakatkarqAQSRIKALERLEELAPAHVDSPFNFSFRESDKISRPLLDL 315
Cdd:PRK10938 217 GEREEIL---------------------------------QQALVAQLAHSEQLEGVQLPEPDEPSARHALPANEPRIVL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 316 GEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPE--------LGGRLLRGENL-----AIGYfaq 382
Cdd:PRK10938 264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgysndltlFGRRRGSGETIwdikkHIGY--- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 383 hqldsldpqASPLLHLQ-RI--------------------APGEREQTLKD-FLGGFDFRGVRVDEPVLNFSGGEKaRLA 440
Cdd:PRK10938 341 ---------VSSSLHLDyRVstsvrnvilsgffdsigiyqAVSDRQQKLAQqWLDILGIDKRTADAPFHSLSWGQQ-RLA 410
|
490 500
....*....|....*....|...
gi 15600445 441 LALIAWQK-PNLLLLDEPTNHLD 462
Cdd:PRK10938 411 LIVRALVKhPTLLILDEPLQGLD 433
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
327-506 |
1.67e-19 |
|
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: 87.31 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENL-------AIGYFAQ---HQLDSlDPQASPL 395
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSiLLNGKPIkakerrkSIGYVMQdvdYQLFT-DSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 LHLQRIAPGEREQT---LKDfLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE-MR----L 467
Cdd:cd03226 94 LLGLKELDAGNEQAetvLKD-LDLYALK----ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnMErvgeL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600445 468 ALTMALQEfsGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03226 169 IRELAAQG--KAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-521 |
1.93e-19 |
|
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: 87.94 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENL----------AIGYFAQHQLDS 387
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvTFDGRPVtrrrrkafrrRVQMVFQDPYAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQ-------ASPLLHLQRIAPGER-EQTLKDF-LGGfDFRGVRVDEpvlnFSGGEKARLAL--ALIAwqKPNLLLLDE 456
Cdd:COG1124 92 LHPRhtvdrilAEPLRIHGLPDREERiAELLEQVgLPP-SFLDRYPHQ----LSGGQRQRVAIarALIL--EPELLLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 457 PTNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV-------PFDGDLDDYARWLVD 521
Cdd:COG1124 165 PTSALDVSVQaeiLNLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVMQNGRIVeeltvadLLAGPKHPYTRELLA 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-229 |
3.55e-19 |
|
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: 86.12 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwRIAHMRQEVDTLDRLAV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF----DGKSYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 dyvldgdsrLREIQAALAVAEAAHDGSALARLHTELDNadgytadaRARKLLAGLGFSSEQmERRVGDFSGGWRMRLNLA 161
Cdd:cd03268 77 ---------LIEAPGFYPNLTARENLRLLARLLGIRKK--------RIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYP--GTLVLI-SHDRDFLDAVVDHVVHLENRKLtLYRG 229
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRIGIINKGKL-IEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
323-506 |
4.45e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 90.97 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA----------IGYFAQH-QL--DSL 388
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSiLINGVDLSdldpaswrrqIAWVPQNpYLfaGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 -------DPQASPlLHLQRIApgerEQT-LKDFL----GGFDFrgvRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDE 456
Cdd:COG4988 428 renlrlgRPDASD-EELEAAL----EAAgLDEFVaalpDGLDT---PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600445 457 PTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLKStTDEFLLVADGRVV 506
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
322-510 |
5.49e-19 |
|
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: 85.71 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGArIGLLGPNGAGKSTLIKTLAGDLPELGGRLL--------RGENL--AIGYFAQH-------- 383
Cdd:cd03264 10 YGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLrrRIGYLPQEfgvypnft 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 QLDSLDPQASpllhLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:cd03264 89 VREFLDYIAW----LKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 464 EMRLALTMALQEFS-GAVLVVS-HDRHLLKSTTDEFLLVADGRVVpFDG 510
Cdd:cd03264 164 EERIRFRNLLSELGeDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-510 |
5.81e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.64 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 27 GQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADW------------------------RIAHMRQEVDTLDRlavd 82
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdevlkrfrgtelqnyfkklyngeiKVVHKPQYVDLIPK---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 83 yVLDGdsRLREIqaalavaeaahdgsalarlhteLDNAD--GytadaRARKLLAGLGFSsEQMERRVGDFSGGWRMRLNL 160
Cdd:PRK13409 175 -VFKG--KVREL----------------------LKKVDerG-----KLDEVVERLGLE-NILDRDISELSGGELQRVAI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 161 AQALMCPSDLLLLDEPTNHLD----LDAILWLEEWLKGYPgtLVLISHDRDFLDAVVDhVVHLenrkltLY--RGGYSAF 234
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLDirqrLNVARLIRELAEGKY--VLVVEHDLAVLDYLAD-NVHI------AYgePGAYGVV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 235 ERTRAERlaqqqqayekqQAQRAHMESFIA----RFKakatkarqaqsrikalerleelapahvDSPFNFSFR--ESDKI 308
Cdd:PRK13409 295 SKPKGVR-----------VGINEYLKGYLPeenmRIR---------------------------PEPIEFEERppRDESE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRPLLDLGEGRLGYGDkAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLrgENLAIGYfaqhqldsl 388
Cdd:PRK13409 337 RETLVEYPDLTKKLGD-FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISY--------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 dpqaSPllhlQRIAPgEREQTLKDFLGG----FD--------FRGVRVDE----PVLNFSGGEKARLALALIAWQKPNLL 452
Cdd:PRK13409 405 ----KP----QYIKP-DYDGTVEDLLRSitddLGssyykseiIKPLQLERlldkNVKDLSGGELQRVAIAACLSRDADLY 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 453 LLDEPTNHLDLEMRLALTMALQ----EFSGAVLVVSHDRHLLKsttdeflLVADgRVVPFDG 510
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHDIYMID-------YISD-RLMVFEG 529
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
282-507 |
5.98e-19 |
|
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: 90.60 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 282 ALERLEELAPAHVDSPFnfSFRESDKISRPLLDLGEGRLGY--GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLA 359
Cdd:COG4987 305 AARRLNELLDAPPAVTE--PAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 360 GDLPELGGR-LLRGENLA----------IGYFAQHQ-------LDSL---DPQASP--LLH-LQRIAPGEREQTLKDflg 415
Cdd:COG4987 383 RFLDPQSGSiTLGGVDLRdldeddlrrrIAVVPQRPhlfdttlRENLrlaRPDATDeeLWAaLERVGLGDWLAALPD--- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 416 GFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLkST 493
Cdd:COG4987 460 GLD---TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGL-ER 535
|
250
....*....|....
gi 15600445 494 TDEFLLVADGRVVP 507
Cdd:COG4987 536 MDRILVLEDGRIVE 549
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
323-506 |
6.69e-19 |
|
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: 86.79 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA----------IGYFAQHQLDSLDPQ 391
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALrPDAGTVDLAGVDLHglsrrararrVALVEQDSDTAVPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQRI--------APGEREQTLKDFLGGFDFRGVrVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:TIGR03873 92 VRDVVALGRIphrslwagDSPHDAAVVDRALARTELSHL-ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 464 EMRLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:TIGR03873 171 RAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
273-486 |
1.15e-18 |
|
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: 89.73 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 273 ARQAQSRIKALERLEELAPAHVDSPFNFSFRESDKISR-PLLDLGEGRLGY-GDKAVLEKVKLQLVPGARIGLLGPNGAG 350
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGkPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 351 KSTLIKTLAGDLPELGGRL-LRGENLA----------IGYFAQ--HQLDSL--------DPQASP---LLHLQRIAPGER 406
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVtLDGVPVSsldqdevrrrVSVCAQdaHLFDTTvrenlrlaRPDATDeelWAALERVGLADW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 407 EQTLKDFLggfdfrGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLA-LTMALQEFSG-AVLVVS 484
Cdd:TIGR02868 454 LRALPDGL------DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAALSGrTVVLIT 527
|
..
gi 15600445 485 HD 486
Cdd:TIGR02868 528 HH 529
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
330-507 |
1.29e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 84.65 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 330 KVKLQLvPGARIGLLGPNGAGKSTLIKTLAG-DLPE-----LGGRLL----RGENL-----AIGY-FAQHQL-DSLDPQA 392
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGlEKPDggtivLNGTVLfdsrKKINLppqqrKIGLvFQQYALfPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPLLHLQRIAPGEREQTLKDFLGGFDFRGVrVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMA 472
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600445 473 LQE----FSGAVLVVSHDRHLLKSTTDEFLLVADGRVVP 507
Cdd:cd03297 174 LKQikknLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
310-506 |
1.88e-18 |
|
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: 88.81 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 310 RPLLDLGEGRLGY--GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP---ELGGR-LLRGENLA------- 376
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEvLLDGRDLLelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 377 ---IGYFAQHQLDSLDP-----QASPLLHLQRIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALALIAWQK 448
Cdd:COG1123 82 grrIGMVFQDPMTQLNPvtvgdQIAEALENLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 449 PNLLLLDEPTNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG1123 161 PDLLIADEPTTALDVTTQaeiLDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
319-505 |
2.29e-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: 83.03 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLrgenlaigyfaqhqLDSLDpqaspllhL 398
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR--------------LDGAD--------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 399 QRIAPGEREQTL-----KDFLggfdFRGVRVDepvlN-FSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMA 472
Cdd:cd03246 67 SQWDPNELGDHVgylpqDDEL----FSGSIAE----NiLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600445 473 LQEFSGA---VLVVSHDRHLLKStTDEFLLVADGRV 505
Cdd:cd03246 139 IAALKAAgatRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
282-506 |
2.79e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.12 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 282 ALERLEELAPAHVDSPFNFSFRESDKIsrplldlgEGRL-------GYGD--KAVLEKVKLQLVPGARIGLLGPNGAGKS 352
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPRL--------KGDIelenvsfRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 353 TLIKTLAGDLPELGGR-LLRGENLA----------IGYFAQHQL---DSL-------DPQASP--LLHLQRIApGereqt 409
Cdd:COG2274 516 TLLKLLLGLYEPTSGRiLIDGIDLRqidpaslrrqIGVVLQDVFlfsGTIrenitlgDPDATDeeIIEAARLA-G----- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 410 LKDFL----GGFDfrgVRVDEPVLNFSGGEKARLALA--LIawQKPNLLLLDEPTNHLDLEMRLALTMALQEFSG--AVL 481
Cdd:COG2274 590 LHDFIealpMGYD---TVVGEGGSNLSGGQRQRLAIAraLL--RNPRILILDEATSALDAETEAIILENLRRLLKgrTVI 664
|
250 260
....*....|....*....|....*
gi 15600445 482 VVSHDRHLLKStTDEFLLVADGRVV 506
Cdd:COG2274 665 IIAHRLSTIRL-ADRIIVLDKGRIV 688
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
321-486 |
4.22e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 83.32 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA---------IGYFAQHqlDSLDP 390
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTaYINGYSIRtdrkaarqsLGYCPQF--DALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 QASPLLHLQRIAP--GEREQTLK----DFLGGFDFRGVRvDEPVLNFSGGEKARL--ALALIAwqKPNLLLLDEPTNHLD 462
Cdd:cd03263 89 ELTVREHLRFYARlkGLPKSEIKeeveLLLRVLGLTDKA-NKRARTLSGGMKRKLslAIALIG--GPSVLLLDEPTSGLD 165
|
170 180
....*....|....*....|....*.
gi 15600445 463 LEMRLALTMALQEFSG--AVLVVSHD 486
Cdd:cd03263 166 PASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
323-506 |
4.57e-18 |
|
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: 82.96 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--DLPELGGR-LLRGENL---------AIGYFaqhqldsLDP 390
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEiLFKGEDItdlppeeraRLGIF-------LAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 QASPllhlqRIaPGereQTLKDFLggfdfRGVRVdepvlNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE-MRLA- 468
Cdd:cd03217 84 QYPP-----EI-PG---VKNADFL-----RYVNE-----GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDaLRLVa 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600445 469 -LTMALQEFSGAVLVVSHDRHLLKS-TTDEFLLVADGRVV 506
Cdd:cd03217 145 eVINKLREEGKSVLIITHYQRLLDYiKPDRVHVLYDGRIV 184
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-223 |
4.72e-18 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 81.52 E-value: 4.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwriahmrqevdtldrlavdyvl 85
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 dgdsrlreiqaalavaeaahDGSALARLhteldnadgytadaRARKLLAGLGFsseqmerrVGDFSGGWRMRLNLAQALM 165
Cdd:cd00267 59 --------------------DGKDIAKL--------------PLEELRRRIGY--------VPQLSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 166 CPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG---TLVLISHDRDFLDAVVDHVVHLENRK 223
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-224 |
6.03e-18 |
|
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: 82.97 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPA-----DW-RIAHMRQ--EVDTLD 77
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekERkRIGYVPQrrSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 78 RLAV-DYVLDGdsRLREIqaalavaeaahdgsalaRLHTELDNADgytaDARARKLLAGLGFSsEQMERRVGDFSGGWRM 156
Cdd:cd03235 84 PISVrDVVLMG--LYGHK-----------------GLFRRLSKAD----KAKVDEALERVGLS-ELADRQIGELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLeNRKL 224
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-506 |
6.46e-18 |
|
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: 82.80 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL----------RGENLAIGYFAQHQldSLDPQ 391
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRRRIGIVFQDL--SVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQ---RIA--PG----EREQTLKDFLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:cd03265 88 LTGWENLYihaRLYgvPGaerrERIDELLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 463 LEMRLALTMALQ----EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03265 164 PQTRAHVWEYIEklkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-219 |
8.66e-18 |
|
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: 83.33 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAD-----------WRIAHMR 70
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 71 QEVDTLDRLAVdyvldgdsrlreiqaalavaeaaHDGSALARL-HTELDNADGYTADARARKLLAGLGFSSeQMERRVGD 149
Cdd:TIGR03873 82 QDSDTAVPLTV-----------------------RDVVALGRIpHRSLWAGDSPHDAAVVDRALARTELSH-LADRDMST 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 150 FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLK--GYPGTLVLIS-HDRDFLDAVVDHVVHL 219
Cdd:TIGR03873 138 LSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHDLNLAASYCDHVVVL 210
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
323-513 |
1.06e-17 |
|
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: 83.08 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGD---LPELGGRLLRGENLA---------IGYFAQHQLDSLDP 390
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsyEVTSGTILFKGQDLLelepderarAGLFLAFQYPEEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 QASPLLHLQRIAPGEREQTLKDFLGGFDFRGV--------RVDEPVLN------FSGGEKARLALALIAWQKPNLLLLDE 456
Cdd:TIGR01978 91 GVSNLEFLRSALNARRSARGEEPLDLLDFEKLlkeklallDMDEEFLNrsvnegFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 457 PTNHLDLEmrlALTMA------LQEFSGAVLVVSHDRHLLKSTTDEFLLV-ADGRVVpFDGDLD 513
Cdd:TIGR01978 171 IDSGLDID---ALKIVaeginrLREPDRSFLIITHYQRLLNYIKPDYVHVlLDGRIV-KSGDVE 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-506 |
1.28e-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: 86.39 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRG--QLGQDAGDCllpadwrIAHM---------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI-------IYHValcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQEVD---------TLDRLAVDYVLDGDSRLREIQAALAVAEAAhdGSALARLHTELDNA------DGYTADA---RARK 131
Cdd:TIGR03269 74 RPSKVgepcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQR--TFALYGDDTVLDNVlealeeIGYEGKEavgRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 132 LLAGLgfsseQMERRVG----DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-LDAIL---WLEEWLKGYPGTLVLIS 203
Cdd:TIGR03269 152 LIEMV-----QLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLvhnALEEAVKASGISMVLTS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 204 HDRDFLDAVVDHVVHLENrkltlyrgGYSAFERTRAErlaqqqqayekqqaqrahmesFIARFKAKATKARQAQSRI--K 281
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLEN--------GEIKEEGTPDE---------------------VVAVFMEGVSEVEKECEVEvgE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 282 ALERLEELAPAHVdspfnfsfresdKISRPLLdlgegrlgygdKAVlEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGD 361
Cdd:TIGR03269 278 PIIKVRNVSKRYI------------SVDRGVV-----------KAV-DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 362 LPELGGRL-----------------LRGE-NLAIGYFaqHQLDSLDPQASPLLHL-QRIA---PGEREQ-----TLKdfL 414
Cdd:TIGR03269 334 LEPTSGEVnvrvgdewvdmtkpgpdGRGRaKRYIGIL--HQEYDLYPHRTVLDNLtEAIGlelPDELARmkaviTLK--M 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 415 GGFDFRGVR--VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALT----MALQEFSGAVLVVSHDRH 488
Cdd:TIGR03269 410 VGFDEEKAEeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThsilKAREEMEQTFIIVSHDMD 489
|
570
....*....|....*...
gi 15600445 489 LLKSTTDEFLLVADGRVV 506
Cdd:TIGR03269 490 FVLDVCDRAALMRDGKIV 507
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
322-509 |
2.38e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 81.03 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLR-GENLA--------IGYFAQH-----QLDS 387
Cdd:cd03259 10 YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnIGMVFQDyalfpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQASPlLHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALA--LIawQKPNLLLLDEPTNHLDLEM 465
Cdd:cd03259 90 AENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALAraLA--REPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 466 RLALTMALQEFSGA----VLVVSHDRHLLKSTTDEFLLVADGRVVPFD 509
Cdd:cd03259 166 REELREELKELQRElgitTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-224 |
2.90e-17 |
|
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: 81.22 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQR-LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADWRIAHMRQEV--- 73
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 74 ----------DTldrlavdyVLDgdsrlrEIqaalavaeaahdgsALARLHTELDNADgytADARARKLLAGLGFSsEQM 143
Cdd:COG1122 81 fqnpddqlfaPT--------VEE------DV--------------AFGPENLGLPREE---IRERVEEALELVGLE-HLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 144 ERRVGDFSGGWRMRLNLAQAL-MCPsDLLLLDEPTNHLDLDAILWLEEWLKGYPG---TLVLISHDRDFLDAVVDHVVHL 219
Cdd:COG1122 129 DRPPHELSGGQKQRVAIAGVLaMEP-EVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVL 207
|
....*
gi 15600445 220 ENRKL 224
Cdd:COG1122 208 DDGRI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
322-504 |
4.82e-17 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 79.15 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA------------IGY-FAQHQLDS 387
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGSILIDGEDLTdledelpplrrrIGMvFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 ldpqaspllHLQRIapgereqtlkdflggfdfrgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR- 466
Cdd:cd03229 90 ---------HLTVL-----------------------ENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRr 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600445 467 --LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGR 504
Cdd:cd03229 138 evRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
5.31e-17 |
|
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: 81.24 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADW--RIAHM 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQEVDTLDRLAV-DYVldgdsrlreiqaalavaeaahdgsALARL-HTELDNADGYTADARARKLLAGLGfSSEQMERRV 147
Cdd:COG1120 81 PQEPPAPFGLTVrELV------------------------ALGRYpHLGLFGRPSAEDREAVEEALERTG-LEHLADRPV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 148 GDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL----DAILWLEEWLKGYPGTLVLISHD 205
Cdd:COG1120 136 DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
319-514 |
5.53e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 80.62 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA-------------IGYFAQHQ 384
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvLIDGEDISglseaelyrlrrrMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 --LDSL---DPQASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVlNFSGGEKARLALA--LIAwqKPNLLLLDEP 457
Cdd:cd03261 87 alFDSLtvfENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA-ELSGGMKKRVALAraLAL--DPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 458 TNHLD---LEMRLALTMALQEFSGA-VLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:cd03261 164 TAGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEE 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-495 |
6.87e-17 |
|
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: 80.87 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTLAGDL-PELGG-----------RLLRGENLAIgYFAQHQLDSLDPQASP--LLHLQRIA 402
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLkPNLGKfddppdwdeilDEFRGSELQN-YFTKLLEGDVKVIVKPqyVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 403 PGEREQTL--KDFLGGFD-------FRGVrVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMAL 473
Cdd:cd03236 104 KGKVGELLkkKDERGKLDelvdqleLRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180
....*....|....*....|....*
gi 15600445 474 QEFS---GAVLVVSHDRHLLKSTTD 495
Cdd:cd03236 183 RELAeddNYVLVVEHDLAVLDYLSD 207
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
323-506 |
8.40e-17 |
|
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: 80.62 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA-------------IGYFAQHQLDSL 388
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKPAQGTVSFRGQDLYqldrkqrrafrrdVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQAS-------PLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:TIGR02769 102 NPRMTvrqiigePLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 462 DLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:TIGR02769 182 DMVLQaviLELLRKLQQAFGtAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
1.07e-16 |
|
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: 83.66 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQR--GPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADWRIAHMRQevdt 75
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdLRDLDEDDLRR---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 76 ldRLAV----DYVLDGDSR--LReiqaalavaeaahdgsaLARlhtelDNADgytaDARARKLL--AGLGFSSEQMER-- 145
Cdd:COG4987 410 --RIAVvpqrPHLFDTTLRenLR-----------------LAR-----PDAT----DEELWAALerVGLGDWLAALPDgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 146 --RVGD----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL---DAIL-WLEEWLKGypGTLVLISHDRDFLDAvVDH 215
Cdd:COG4987 462 dtWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQALLaDLLEALAG--RTVLLITHRLAGLER-MDR 538
|
250
....*....|
gi 15600445 216 VVHLENRKLT 225
Cdd:COG4987 539 ILVLEDGRIV 548
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
1.30e-16 |
|
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: 83.27 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQR-LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR--IAHM 69
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdlsdldPASWRrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQEvdtldrlavDYVLDGDsrLREIqaalavaeaahdgsaLARLHTELDNADGYTA--DARARKLLAGLgfsSEQMERRV 147
Cdd:COG4988 417 PQN---------PYLFAGT--IREN---------------LRLGRPDASDEELEAAleAAGLDEFVAAL---PDGLDTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 148 GD----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLD--AILW--LEEWLKGYpgTLVLISHDRDFLDAvVDHVVHL 219
Cdd:COG4988 468 GEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKGR--TVILITHRLALLAQ-ADRILVL 544
|
....*.
gi 15600445 220 ENRKLT 225
Cdd:COG4988 545 DDGRIV 550
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-506 |
1.33e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 78.12 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLAIGYFAQHQLDSLDPQASPLLhlqria 402
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 403 pgerEQTLKDFLGgfdfrgvrvdepvLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEF--SGAV 480
Cdd:cd03247 88 ----DTTLRNNLG-------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTL 150
|
170 180
....*....|....*....|....*..
gi 15600445 481 LVVSHdrHLLK-STTDEFLLVADGRVV 506
Cdd:cd03247 151 IWITH--HLTGiEHMDKILFLENGKII 175
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
333-506 |
1.37e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 333 LQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAI----------GYFAQHQldsLDPQASPL-----LH 397
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDwsaaelarhrAYLSQQQ---SPPFAMPVfqylaLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 398 LQRIAPGEREQT----------LKDFLGgfdfrgvrvdEPVLNFSGGEKARLALALIAWQ-------KPNLLLLDEPTNH 460
Cdd:COG4138 94 QPAGASSEAVEQllaqlaealgLEDKLS----------RPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 461 LDLEMRLALTMALQEFS---GAVLVVSHD-----RHllkstTDEFLLVADGRVV 506
Cdd:COG4138 164 LDVAQQAALDRLLRELCqqgITVVMSSHDlnhtlRH-----ADRVWLLKQGKLV 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
341-510 |
1.38e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 79.76 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 341 IGLLGPNGAGKSTLIKTLAGDLPELGGRLLRgENLAIGYFAQHQLDSLDPQASPLLHLQRIAPGEREQTLKDFLGGFDFR 420
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEIAKPLQIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 421 GVrVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEF----SGAVLVVSHDRHLLKsttde 496
Cdd:cd03237 107 QI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMID----- 180
|
170
....*....|....
gi 15600445 497 flLVADgRVVPFDG 510
Cdd:cd03237 181 --YLAD-RLIVFEG 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
311-505 |
2.28e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 311 PLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLAigyfaqhqldSLD 389
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVLVAGDDVE----------ALS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 PQASPllhlQRIAPGEREQTLK-DF-------------LGGF------DFRGVR-----------VDEPVLNFSGGEKAR 438
Cdd:PRK09536 72 ARAAS----RRVASVPQDTSLSfEFdvrqvvemgrtphRSRFdtwtetDRAAVEramertgvaqfADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 439 LALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQvrtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-516 |
3.04e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 78.76 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--------------DLPELGGRLLRGENLAIGY-FAQHQLDS 387
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgtDINKLKGKALRQLRRQIGMiFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQASPLLH------------LQRIAPGEREQTLK--DFLGGFDFRGVRVDEpvlnFSGGEKARLALALIAWQKPNLLL 453
Cdd:cd03256 92 RLSVLENVLSgrlgrrstwrslFGLFPKEEKQRALAalERVGLLDKAYQRADQ----LSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 454 LDEPTNHLDLE-----MRLALTMAlQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDG---DLDDYA 516
Cdd:cd03256 168 ADEPVASLDPAssrqvMDLLKRIN-REEGITVIVSLHQVDLAREYADRIVGLKDGRIV-FDGppaELTDEV 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-510 |
7.25e-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: 80.98 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 27 GQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADW------------------------RIAHMRQEVDTLDRlavd 82
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWdevlkrfrgtelqdyfkklangeiKVAHKPQYVDLIPK---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 83 yVLDGdsRLREIqaalavaeaahdgsalarlhteLDNAD--GyTADARARKLlaGLgfsSEQMERRVGDFSGGWRMRLNL 160
Cdd:COG1245 175 -VFKG--TVREL----------------------LEKVDerG-KLDELAEKL--GL---ENILDRDISELSGGELQRVAI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 161 AQALMCPSDLLLLDEPTNHLDL-------DAILWLEEWLKgypgTLVLISHDRDFLDAVVDhVVHLenrkltLY--RGGY 231
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDIyqrlnvaRLIRELAEEGK----YVLVVEHDLAILDYLAD-YVHI------LYgePGVY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 232 SAFertraerlaqqqqayekqqaqrahmesfiarfkakaTKARQAQSRIKALerLEELAPAH----VDSPFNFSFRES-- 305
Cdd:COG1245 293 GVV------------------------------------SKPKSVRVGINQY--LDGYLPEEnvriRDEPIEFEVHAPrr 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 306 DKISRPLLDLGEGRLGYGDkAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLlrGENLAIGYfaqhql 385
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGG-FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISY------ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 dslDPQaspllHLQRIAPGEREQTLKDFLGG-FD--------FRGVRV----DEPVLNFSGGEKARLALALIAWQKPNLL 452
Cdd:COG1245 406 ---KPQ-----YISPDYDGTVEEFLRSANTDdFGssyykteiIKPLGLekllDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 453 LLDEPTNHLDLEMRLALTMALQEF----SGAVLVVSHDRHLLksttDeflLVADgRVVPFDG 510
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLI----D---YISD-RLMVFEG 531
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-227 |
7.35e-16 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 75.93 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwriahmrqevdtldrlavdyvl 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 dgdsrlreiqaalavaeaahDGSALARlhteldnadgYTADARARKLlaglGFSSEQME---------RRVGDFSGGWRM 156
Cdd:cd03214 59 --------------------DGKDLAS----------LSPKELARKI----AYVPQALEllglahladRPFNELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLDL---DAIL-WLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLY 227
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIahqIELLeLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-506 |
8.53e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.86 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA----------IGYFAQH--------- 383
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLDGTDIRqldpadlrrnIGYVPQDvtlfygtlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 -QLDSLDPQASPllhlQRIAPGEREQTLKDFLG----GFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPT 458
Cdd:cd03245 96 dNITLGAPLADD----ERILRAAELAGVTDFVNkhpnGLD---LQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 459 NHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLkSTTDEFLLVADGRVV 506
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGdkTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
322-510 |
1.67e-15 |
|
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: 76.22 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL---------RGENLA-IGY-FAQHQ------ 384
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrRKKFLRrIGVvFGQKTqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 --LDSLdpqaSPLLHLQRIAPGEREQTLKDFLGGFDFRGVrVDEPVLNFSGGE--KARLALALIawQKPNLLLLDEPTNH 460
Cdd:cd03267 111 pvIDSF----YLLAAIYDLPPARFKKRLDELSELLDLEEL-LDTPVRQLSLGQrmRAEIAAALL--HEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 461 LDLEMRLALTMALQEFS----GAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDG 510
Cdd:cd03267 184 LDVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRLL-YDG 236
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
327-505 |
1.81e-15 |
|
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: 75.60 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLP-----ELGGRLLRGENLA---------IGY-FAQHQL----D 386
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRPtsgevRVDGTDISKLSEKelaafrrrhIGFvFQSFNLlpdlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 387 SLDPQASPlLHLQRIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALA--LIawQKPNLLLLDEPTNHLDLE 464
Cdd:cd03255 99 ALENVELP-LLLAGVPKKERRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIAraLA--NDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 465 MR---LALTMALQEFSG-AVLVVSHDRhLLKSTTDEFLLVADGRV 505
Cdd:cd03255 175 TGkevMELLRELNKEAGtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-220 |
2.77e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 75.55 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNL----TL-QRGPQRL--LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP-----------A 62
Cdd:COG4778 4 LLEVENLsktfTLhLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 63 DWRIAHMRQEV--------DTLDRL-AVDYVLDgdsRLREiqaalavaeaahDGSALArlhteldnadgyTADARARKLL 133
Cdd:COG4778 84 PREILALRRRTigyvsqflRVIPRVsALDVVAE---PLLE------------RGVDRE------------EARARARELL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 134 AGLGfsseqMERRVGD-----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPGTLVLISHD 205
Cdd:COG4778 137 ARLN-----LPERLWDlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHD 211
|
250
....*....|....*
gi 15600445 206 RDFLDAVVDHVVHLE 220
Cdd:COG4778 212 EEVREAVADRVVDVT 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-506 |
3.97e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 74.70 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA-------------IGY-FAQHQL-- 385
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvLVNGQDLSrlkrreipylrrrIGVvFQDFRLlp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 -----DSLdpqASPLlHLQRIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLAL--ALIAwqKPNLLLLDEPT 458
Cdd:COG2884 93 drtvyENV---ALPL-RVTGKSRKEIRRRVREVLDLVGLSD-KAKALPHELSGGEQQRVAIarALVN--RPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600445 459 NHLDLEMRLALTMALQEF--SG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG2884 166 GNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-217 |
6.43e-15 |
|
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: 75.08 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCL--------LPAdWRIAHM---R--QEVDTLDRLAV-DYVLDG 87
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditgLPP-HRIARLgiaRtfQNPRLFPELTVlENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 88 -DSRLREiqaalavaeaahdGSALARLHTELDNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMC 166
Cdd:COG0411 104 aHARLGR-------------GLLAALLRLPRARREEREARERAEELLERVGLA-DRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 167 PSDLLLLDEPT---NHLDLDAILWLEEWLKGYPG-TLVLISHDRDFLDAVVDHVV 217
Cdd:COG0411 170 EPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
322-506 |
6.89e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.29 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA--------IGYFAQHqlDSLDPqa 392
Cdd:COG3842 15 YGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRiLLDGRDVTglppekrnVGMVFQD--YALFP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 spllHL------------QRIAPGEREQTLKDFL-----GGFDFRgvRVDEpvLnfSGGEKARLALA--LIAwqKPNLLL 453
Cdd:COG3842 91 ----HLtvaenvafglrmRGVPKAEIRARVAELLelvglEGLADR--YPHQ--L--SGGQQQRVALAraLAP--EPRVLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 454 LDEPTNHLDL----EMRLALTMALQEFSGAVLVVSHDRhllksttDEFLLVADgRVV 506
Cdd:COG3842 159 LDEPLSALDAklreEMREELRRLQRELGITFIYVTHDQ-------EEALALAD-RIA 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-221 |
8.41e-15 |
|
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: 74.45 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGP----QRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADWRIAHMRQE 72
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 73 V--------DTLD-RLAVDYVLdgdsrlreiqaalavaeaahdgSALARLHTELDnadgytADARARKLLAGLGFSSEQM 143
Cdd:COG1124 81 VqmvfqdpyASLHpRHTVDRIL----------------------AEPLRIHGLPD------REERIAELLEQVGLPPSFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 144 ERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPG-TLVLISHDRDFLDAVVDHVVHL 219
Cdd:COG1124 133 DRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqAEILNLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVM 212
|
..
gi 15600445 220 EN 221
Cdd:COG1124 213 QN 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
323-490 |
1.37e-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: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLA-----IGYFAQHQL---DSL 388
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDptegsiAVNGVPLADADADswrdqIAWVPQHPFlfaGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 -------DPQASPLL---HLQRIAPGEREQTLKDFLggfdfrGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPT 458
Cdd:TIGR02857 413 aenirlaRPDASDAEireALERAGLDEFVAALPQGL------DTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|....
gi 15600445 459 NHLDLEMRLALTMALQEFSG--AVLVVSHDRHLL 490
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQgrTVLLVTHRLALA 520
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-491 |
1.55e-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: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHqldsldpqasPLLhlqriAP 403
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR----------PYL-----PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 404 GereqTLKDFLggfdfrgVRVDEPVLnfSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVV 483
Cdd:cd03223 78 G----TLREQL-------IYPWDDVL--SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
....*...
gi 15600445 484 SHDRHLLK 491
Cdd:cd03223 145 GHRPSLWK 152
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
323-504 |
1.90e-14 |
|
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: 76.71 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKaVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQLDSL----DPQASPLLHL 398
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgtlrDQIIYPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 399 QRIAPGEREQTLKDFL------------GGFDfrGVRVDEPVLnfSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR 466
Cdd:TIGR00954 543 DMKRRGLSDKDLEQILdnvqlthilereGGWS--AVQDWMDVL--SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600445 467 LALTMALQEFSGAVLVVSHDRHLLKSttDEFLLVADGR 504
Cdd:TIGR00954 619 GYMYRLCREFGITLFSVSHRKSLWKY--HEYLLYMDGR 654
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
337-486 |
2.40e-14 |
|
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: 76.36 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTLAGDL-PELGgrllRGENLA-----IGYFAQHQLDSldpqaspllHLQRIAPGE----- 405
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkPNLG----DYDEEPswdevLKRFRGTELQD---------YFKKLANGEikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 406 REQ-----------TLKDFLGGFDFRGVrVDE--------PVLN-----FSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:COG1245 165 KPQyvdlipkvfkgTVRELLEKVDERGK-LDElaeklgleNILDrdiseLSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*...
gi 15600445 462 DLEMRLALTMALQEFSG---AVLVVSHD 486
Cdd:COG1245 244 DIYQRLNVARLIRELAEegkYVLVVEHD 271
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-219 |
2.42e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLDRL---AVDYVLDGD 88
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLpltVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 89 SRLReiqaalavaeaahdgsALARLHTELDNADgyTADARARKLLAGLGfsseqmERRVGDFSGGWRMRLNLAQALMCPS 168
Cdd:NF040873 83 WARR----------------GLWRRLTRDDRAA--VDDALERVGLADLA------GRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 169 DLLLLDEPTNHLDLDAILWLEEWLKGYPG---TLVLISHDRDfLDAVVDHVVHL 219
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE-LVRRADPCVLL 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
328-506 |
2.42e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAI----------GYFAQHQldsldpqaSPL-- 395
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAwsaaelarhrAYLSQQQ--------TPPfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 --------LHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALA---LIAWQKPN----LLLLDEPTNH 460
Cdd:PRK03695 84 mpvfqyltLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvLQVWPDINpagqLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 461 LDLEMRLALTMALQEFS---GAVLVVSHD-RHLLKStTDEFLLVADGRVV 506
Cdd:PRK03695 164 LDVAQQAALDRLLSELCqqgIAVVMSSHDlNHTLRH-ADRVWLLKQGKLL 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
142-506 |
3.26e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 142 QMERRVGDF----SGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDA---ILWLEEWLKGYPG-TLVLISHDRDFLDAVV 213
Cdd:PRK15134 145 QAAKRLTDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQELNmGLLFITHNLSIVRKLA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 214 DHVVHLENRKltlyrggysAFERTRAERLaqqqqayekqqaqrahmesfiarFKAKATKARQaqsRIKALERLEELAPAH 293
Cdd:PRK15134 225 DRVAVMQNGR---------CVEQNRAATL-----------------------FSAPTHPYTQ---KLLNSEPSGDPVPLP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 294 VDSPfnfsfresdkisrPLLDLGEGRLGY-----------GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL 362
Cdd:PRK15134 270 EPAS-------------PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 363 PELGGRLLRGENL-------AIGYFAQHQLDSLDPQAS--PLLH-LQRIAPG-----------EREQTLKDFLG--GFDf 419
Cdd:PRK15134 337 NSQGEIWFDGQPLhnlnrrqLLPVRHRIQVVFQDPNSSlnPRLNvLQIIEEGlrvhqptlsaaQREQQVIAVMEevGLD- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 420 RGVRVDEPVlNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTD 495
Cdd:PRK15134 416 PETRHRYPA-EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQaqiLALLKSLQQKHQlAYLFISHDLHVVRALCH 494
|
410
....*....|.
gi 15600445 496 EFLLVADGRVV 506
Cdd:PRK15134 495 QVIVLRQGEVV 505
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
321-514 |
3.46e-14 |
|
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: 72.08 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA-----------IGYFAQHQldSL 388
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSiRFDGRDITglppheraragIGYVPEGR--RI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQASP----LLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLAL--ALIAwqKPNLLLLDEPTNHLD 462
Cdd:cd03224 87 FPELTVeenlLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIarALMS--RPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 463 ---LEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:cd03224 165 pkiVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV-LEGTAAE 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
319-506 |
3.69e-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: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG------DLPELGGRLLRGENLAigyfaqhqLDSLDP-- 390
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPDEGEVLLDGKDIY--------DLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 ----------QASPL-----------LHLQRIAPG-EREQTLKDFLggfdfRGVRVDEPV------LNFSGGEKARLALA 442
Cdd:cd03260 79 lrrrvgmvfqKPNPFpgsiydnvaygLRLHGIKLKeELDERVEEAL-----RKAALWDEVkdrlhaLGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 443 LiAWQ-KPNLLLLDEPTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03260 154 R-ALAnEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-514 |
5.84e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL---------RGENLA-IGY-FAQHQ--------LDSLDpqaspLL- 396
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkrRKEFARrIGVvFGQRSqlwwdlpaIDSFR-----LLk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 397 HLQRIAPGEREQTLKDF-----LGGFdfrgvrVDEPVLNFSGGE--KARLALALIawQKPNLLLLDEPTNHLDLEMRLAL 469
Cdd:COG4586 122 AIYRIPDAEYKKRLDELvelldLGEL------LDTPVRQLSLGQrmRCELAAALL--HRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 470 TMALQEFS---GA-VLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:COG4586 194 REFLKEYNrerGTtILLTSHDMDDIEALCDRVIVIDHGRII-YDGSLEE 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-506 |
6.25e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.64 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA---------IGYFAQHqldsldpq 391
Cdd:COG1118 12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPDSGRIVLNGRDLFtnlpprerrVGFVFQH-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 asPLL--HL---QRIA---------PGEREQTLKDFLGgfdfrgvRVDEPVL------NFSGGEKARLALA--LIAwqKP 449
Cdd:COG1118 84 --YALfpHMtvaENIAfglrvrppsKAEIRARVEELLE-------LVQLEGLadrypsQLSGGQRQRVALAraLAV--EP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 450 NLLLLDEPTNHLD----LEMRLALTMALQEFSGAVLVVSHDRhllksttDEFLLVADgRVV 506
Cdd:COG1118 153 EVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQ-------EEALELAD-RVV 205
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
322-510 |
6.92e-14 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 72.81 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL----------RGENLAIGYFAQHQldSLDPQ 391
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARvagydvvrepRKVRRSIGIVPQYA--SVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQRIA-----PG-EREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEM 465
Cdd:TIGR01188 81 LTGRENLEMMGrlyglPKdEAEERAEELLELFELGEAA-DRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 466 RLA---LTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFDG 510
Cdd:TIGR01188 160 RRAiwdYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGT 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-506 |
8.08e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 71.23 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--------------DLPELGGR---LLRGENlaIGY-F 380
Cdd:COG1136 15 GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldrptsgevlidgqDISSLSERelaRLRRRH--IGFvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 381 AQHQL-DSLD-------PqasplLHLQRIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALA--LIAwqKPN 450
Cdd:COG1136 93 QFFNLlPELTalenvalP-----LLLAGVSRKERRERARELLERVGLGD-RLDHRPSQLSGGQQQRVAIAraLVN--RPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 451 LLLLDEPTNHLDLE-----MRLALTMAlQEFSGAVLVVSHDRHLLkSTTDEFLLVADGRVV 506
Cdd:COG1136 165 LILADEPTGNLDSKtgeevLELLRELN-RELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
335-486 |
1.02e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 335 LVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGG-----------RLLRGENLAiGYFAqhqlDSLDPQASPLLHLQRI- 401
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELiPNLGDyeeepswdevlKRFRGTELQ-NYFK----KLYNGEIKVVHKPQYVd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 402 -APGEREQTLKDFLGGFDFRGVR------------VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLA 468
Cdd:PRK13409 171 lIPKVFKGKVRELLKKVDERGKLdevverlgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLN 250
|
170 180
....*....|....*....|
gi 15600445 469 LTMALQEFSG--AVLVVSHD 486
Cdd:PRK13409 251 VARLIRELAEgkYVLVVEHD 270
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-506 |
1.19e-13 |
|
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: 68.99 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLlrgenlaigYFAQHQLDSLDPQASpllhlQRi 401
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------LVDGKEVSFASPRDA-----RR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 402 apgereqtlkdflggfdfRGVRVdepVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL---EMRLALTMALQEFSG 478
Cdd:cd03216 75 ------------------AGIAM---VYQLSVGERQMVEIARALARNARLLILDEPTAALTPaevERLFKVIRRLRAQGV 133
|
170 180
....*....|....*....|....*...
gi 15600445 479 AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03216 134 AVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
327-514 |
1.36e-13 |
|
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: 70.83 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA--------IGYFAQHQldSLDPQASPL-- 395
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKiLLNGKDITnlppekrdISYVPQNY--ALFPHMTVYkn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 ----LHLQRIAPGEREQTLKDFLGgfdFRGVR--VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE----M 465
Cdd:cd03299 92 iaygLKKRKVDKKEIERKVLEIAE---MLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRtkekL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 466 RLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFdGDLDD 514
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
319-510 |
1.44e-13 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 70.19 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLAIGYFAQHqlDSLDPQA 392
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQQ--DALLPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPL------LHLQRIAPGEREQTLKDFL---GGFDFRGVRVDEpvlnFSGGEKARLALA--LIawQKPNLLLLDEPTNHL 461
Cdd:cd03293 89 TVLdnvalgLELQGVPKAEARERAEELLelvGLSGFENAYPHQ----LSGGMRQRVALAraLA--VDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 462 D----LEMRLALTMALQEFSGAVLVVSHDrhllkstTDEFLLVADgRVVPFDG 510
Cdd:cd03293 163 DaltrEQLQEELLDIWRETGKTVLLVTHD-------IDEAVFLAD-RVVVLSA 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
1.72e-13 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 70.50 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwriahmrQEVDTLDRla 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG--------------NDVRLFGE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 vdyVLDGDSrLREIQAalavaeaaHDG---SALARLHTELDNA---------------DGYTAD--ARARKLLAGLGFSs 140
Cdd:COG1119 67 ---RRGGED-VWELRK--------RIGlvsPALQLRFPRDETVldvvlsgffdsiglyREPTDEqrERARELLELLGLA- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 141 EQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWL-----KGYPgTLVLISHDRDFLDAVVDH 215
Cdd:COG1119 134 HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdklaaEGAP-TLVLVTHHVEEIPPGITH 212
|
....*.
gi 15600445 216 VVHLEN 221
Cdd:COG1119 213 VLLLKD 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
322-514 |
2.15e-13 |
|
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: 70.16 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRG---------------------------- 372
Cdd:cd03219 10 FGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvLFDGeditglppheiarlgigrtfqiprlfpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 373 ----ENLAIGYFAQHQLDSLDPQASPLLHLQRiapgEREQTLKDFLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQK 448
Cdd:cd03219 90 ltvlENVMVAAQARTGSGLLLARARREEREAR----ERAEELLERVGLADLA----DRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 449 PNLLLLDEPTNHLDLEMR---LALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETeelAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI-AEGTPDE 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
326-506 |
2.16e-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: 69.70 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 326 AVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLrgenlaigyfaqhqLDSLDPQASPLLHLQRI---- 401
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT--------------VDGFDVVKEPAEARRRLgfvs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 402 ------------------------APGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEP 457
Cdd:cd03266 85 dstglydrltarenleyfaglyglKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600445 458 TNHLDLEMRLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
327-506 |
2.51e-13 |
|
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: 70.45 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRG---------------------------E 373
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRDITGlpphriarlgiartfqnprlfpeltvlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 374 NLAIGYFAQHQLDSLdpqaSPLLHLQRIAPGEREQTLK-----DFLGGFDFRgvrvDEPVLNFSGGEKARL--ALALIAw 446
Cdd:COG0411 99 NVLVAAHARLGRGLL----AALLRLPRARREEREARERaeellERVGLADRA----DEPAGNLSYGQQRRLeiARALAT- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 447 qKPNLLLLDEPT---NHLDLEMRLALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG0411 170 -EPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-506 |
3.08e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 70.12 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENLAIGYFAQHqlDSLDPQASPL- 395
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDRGVVFQE--PALLPWLTVLd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 -----LHLQRIAPGEREQTLKDFLGGF---DFRGVRVDEpvLnfSGGEKARLALA--LIawQKPNLLLLDEPTNHLD--- 462
Cdd:COG1116 100 nvalgLELRGVPKAERRERARELLELVglaGFEDAYPHQ--L--SGGMRQRVAIAraLA--NDPEVLLMDEPFGALDalt 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 463 -LEMRLALTMALQEFSGAVLVVSHDrhllkstTDEFLLVADgRVV 506
Cdd:COG1116 174 rERLQDELLRLWQETGKTVLFVTHD-------VDEAVFLAD-RVV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-224 |
3.12e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 69.45 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADwRIAHMRQEVDTLDRLAV 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-DISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDG----DS---------RLREiqaalavaeaahdgsalarlHTELDNAdgyTADARARKLLAGLGFSSEQmERRVG 148
Cdd:cd03261 80 GMLFQSgalfDSltvfenvafPLRE--------------------HTRLSEE---EIREIVLEKLEAVGLRGAE-DLYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 149 DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKgypGTLVLISHDRDFLDAVVDHVVHLEN 221
Cdd:cd03261 136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFAIADRIAVLYD 212
|
...
gi 15600445 222 RKL 224
Cdd:cd03261 213 GKI 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
333-514 |
3.55e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.40 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 333 LQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL-RGENLAigyfaqhqldSLDPQASPL----------LHL--- 398
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwNGQDLT----------ALPPAERPVsmlfqennlfPHLtva 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 399 QRIA----PGER---------EQTLKDF-LGGFDFRgvRVDEpvlnFSGGEKARLALA--LIawQKPNLLLLDEPTNHLD 462
Cdd:COG3840 90 QNIGlglrPGLKltaeqraqvEQALERVgLAGLLDR--LPGQ----LSGGQRQRVALArcLV--RKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 463 ----LEMrLALTMALQEFSGA-VLVVSHD----RHLlkstTDEFLLVADGRVVPfDGDLDD 514
Cdd:COG3840 162 palrQEM-LDLVDELCRERGLtVLMVTHDpedaARI----ADRVLLVADGRIAA-DGPTAA 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
325-506 |
3.74e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPE---------LGGRLLRGENLA-IGYFAQHQLDSLDPQAS- 393
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarvTGDVTLNGEPLAaIDAPRLARLRAVLPQAAq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 --------PLLHLQRIAPGEREQTLKDFLGGFDFRGVR-------VDEPVLNFSGGEKARLALALI---------AWQKP 449
Cdd:PRK13547 94 pafafsarEIVLLGRYPHARRAGALTHRDGEIAWQALAlagatalVGRDVTTLSGGELARVQFARVlaqlwpphdAAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 450 NLLLLDEPTNHLDL--EMRLALTM--ALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13547 174 RYLLLDEPTAALDLahQHRLLDTVrrLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-224 |
4.05e-13 |
|
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: 68.77 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR--IAHMRQEVD----TL-DRLA 80
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldPADLRrnIGYVPQDVTlfygTLrDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VDYVLDGDSRLreiqaalavaeaahdgsalarlhteLDNADGYTADARARKLLAGlgfsseqMERRVGD----FSGGWRM 156
Cdd:cd03245 100 LGAPLADDERI-------------------------LRAAELAGVTDFVNKHPNG-------LDLQIGErgrgLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG--TLVLISHDRDFLDaVVDHVVHLENRKL 224
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-229 |
4.14e-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: 68.93 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLT----LQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEVdtl 76
Cdd:cd03266 1 MITADALTkrfrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDVVKEPAEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 dRLAVDYVLDGDS---RL--REIQAAlavaeaahdgsaLARLHteldNADGYTADARARKLLAGLGFSsEQMERRVGDFS 151
Cdd:cd03266 77 -RRRLGFVSDSTGlydRLtaRENLEY------------FAGLY----GLKGDELTARLEELADRLGME-ELLDRRVGGFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 152 GGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG---TLVLISHDRDFLDAVVDHVVHLeNRKLTLYR 228
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVL-HRGRVVYE 217
|
.
gi 15600445 229 G 229
Cdd:cd03266 218 G 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-466 |
5.04e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 303 RESDKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL-------AGDLPELGGRLLRGENL 375
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdAGKITVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 376 A---IGYFAqhQLDSLDPQASPLLHLQ------RIAPGEREQTLKDFLgGFDFRGVRVDEPVLNFSGGEKARLALALIAW 446
Cdd:PRK13536 112 ArarIGVVP--QFDNLDLEFTVRENLLvfgryfGMSTREIEAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180
....*....|....*....|
gi 15600445 447 QKPNLLLLDEPTNHLDLEMR 466
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHAR 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
306-466 |
5.67e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 306 DKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGEnlAIGYFAQH- 383
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSISLCGE--PVPSRARHa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 --------QLDSLDPQASPLLHLQRIA-----PGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPN 450
Cdd:PRK13537 79 rqrvgvvpQFDNLDPDFTVRENLLVFGryfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170
....*....|....*.
gi 15600445 451 LLLLDEPTNHLDLEMR 466
Cdd:PRK13537 159 VLVLDEPTTGLDPQAR 174
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-224 |
6.22e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 68.30 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPA---DWRIAHMRQEV------DTL-DRLAVdyvldgdsrl 91
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysiRTDRKAARQSLgycpqfDALfDELTV---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 92 REiqaalavaeaahdgsaLARLHTELDNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLL 171
Cdd:cd03263 93 RE----------------HLRFYARLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 172 LLDEPTNHLDLDA--ILW--LEEWLKGYpgTLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:cd03263 156 LLDEPTSGLDPASrrAIWdlILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
322-515 |
6.82e-13 |
|
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: 68.42 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA--------IGYFAQH-----QLDS 387
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEILLDGKDITnlpphkrpVNTVFQNyalfpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQASPlLHLQRIAPGEREQTLKDFL-----GGFDFRgvRVDEpvlnFSGGEKARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:cd03300 90 FENIAFG-LRLKKLPKAEIKERVAEALdlvqlEGYANR--KPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 463 L----EMRLALtMALQEFSGAVLV-VSHDRHLLKSTTDEFLLVADGRVVPFDGDLDDY 515
Cdd:cd03300 163 LklrkDMQLEL-KRLQKELGITFVfVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-182 |
6.94e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 68.99 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADW-------RIAHM 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLngrpLAAWspwelarRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQEVdtldRLAVDYvldgdsRLREIqaalavaeaahdgSALARLHTELDNADgytADARARKLLA--GL-GFSseqmERR 146
Cdd:COG4559 81 PQHS----SLAFPF------TVEEV-------------VALGRAPHGSSAAQ---DRQIVREALAlvGLaHLA----GRS 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600445 147 VGDFSGGWRMRLNLAQAL---MCPSD----LLLLDEPTNHLDL 182
Cdd:COG4559 131 YQTLSGGEQQRVQLARVLaqlWEPVDggprWLFLDEPTSALDL 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
318-506 |
7.89e-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: 67.58 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 318 GRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR---LLRGENL-------AIGYFAQHqlDS 387
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSgevLINGRPLdkrsfrkIIGYVPQD--DI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQaspllhlqriapgereQTLKDFLggfDF----RGVrvdepvlnfSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:cd03213 93 LHPT----------------LTVRETL---MFaaklRGL---------SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 464 EMRLALTMALQEFSGA---VLVVSHD-RHLLKSTTDEFLLVADGRVV 506
Cdd:cd03213 145 SSALQVMSLLRRLADTgrtIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
325-506 |
8.00e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA-------------IGYFAQHQLDSLDP 390
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQGNVSWRGEPLAklnraqrkafrrdIQMVFQDSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 Q-------ASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:PRK10419 105 RktvreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 464 EMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK10419 185 VLQagvIRLLKKLQQQFGtACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
322-506 |
8.86e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLAIGYFAQH------QLDSLDPQASP 394
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTEGQIFIDGEDVTHRSIQQRdicmvfQSYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 L------LHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLA 468
Cdd:PRK11432 96 GenvgygLKMLGVPKEERKQRVKEALELVDLAGFE-DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 469 LTMAL----QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11432 175 MREKIrelqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-506 |
1.25e-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: 67.61 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--------------DLPELGGRLLRGENLAIGYFAQH--- 383
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKELRKARRRIGMIFQHfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 --QLDSLDPQASPL--LHLQRIAPGEREQTLKDFLGGFDFRGVRVDepvlNFSGGEKARLALALIAWQKPNLLLLDEPTN 459
Cdd:cd03258 94 lsSRTVFENVALPLeiAGVPKAEIEERVLELLELVGLEDKADAYPA----QLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600445 460 HLDLEMR---LALTMAL-QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03258 170 ALDPETTqsiLALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-504 |
1.31e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.46 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGD-LPElGGRLL-----RGENLA--------------IGYFAQH--- 383
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNyLPD-SGSILvrhdgGWVDLAqaspreilalrrrtIGYVSQFlrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 --QLDSLDPQASPLLHLQrIAPGEREQTLKDFLGGFdfrgvRVDE-----PVLNFSGGEKAR--LALALIAwqKPNLLLL 454
Cdd:COG4778 105 ipRVSALDVVAEPLLERG-VDREEARARARELLARL-----NLPErlwdlPPATFSGGEQQRvnIARGFIA--DPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 455 DEPTNHLDLEMRLALTMALQEF--SGAVLV-VSHDRHLLKSTTDEFLLVADGR 504
Cdd:COG4778 177 DEPTASLDAANRAVVVELIEEAkaRGTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
323-485 |
1.52e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.75 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL---------RGENLAIGYFAQHQlDSLDPQAS 393
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggpldfqRDSIARGLLYLGHA-PGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 PLLHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL--EMRLALTM 471
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKagVARFAEAM 168
|
170
....*....|....*
gi 15600445 472 ALQ-EFSGAVLVVSH 485
Cdd:cd03231 169 AGHcARGGMVVLTTH 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
322-506 |
1.91e-12 |
|
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: 66.92 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL-RGENLA------IGYFAQHQldSLDPQ--- 391
Cdd:cd03269 10 FGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLDiaarnrIGYLPEER--GLYPKmkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQRIAPGEREQTLKDF------LGGFDFRGVRVDEpvLNFSGGEKARLALALIawQKPNLLLLDEPTNHLD--- 462
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRRIdewlerLELSEYANKRVEE--LSKGNQQKVQFIAAVI--HDPELLILDEPFSGLDpvn 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600445 463 LEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-506 |
2.61e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLAI---GYFA------------QHQL 385
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLDYskrGLLAlrqqvatvfqdpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 DSLDPQASPLLHLQRIAPGERE--QTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEitRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 464 EMRLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
309-506 |
2.64e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGG--------------------- 367
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhyrmrdgqlrdlyalseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 368 --RLLRGEnlaIGYFAQHQLDSLDPQAS-------PLLhlqriAPGER-----EQTLKDFLGGFDFRGVRVDEPVLNFSG 433
Cdd:PRK11701 83 rrRLLRTE---WGFVHQHPRDGLRMQVSaggnigeRLM-----AVGARhygdiRATAGDWLERVEIDAARIDDLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 434 GEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMAL-QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQarlLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-182 |
2.71e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.10 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP----ADWRIAHMRQevdtl 76
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrplADWSPAELAR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 dRLAV---DYVLDGDSRLREIQAALavaeaahdGSALARLHTELDNAdgyTADARARKLLAGLGfsseqmERRVGDFSGG 153
Cdd:PRK13548 77 -RRAVlpqHSSLSFPFTVEEVVAMG--------RAPHGLSRAEDDAL---VAAALAQVDLAHLA------GRDYPQLSGG 138
|
170 180 190
....*....|....*....|....*....|....*
gi 15600445 154 WRMRLNLAQALM---CPSD---LLLLDEPTNHLDL 182
Cdd:PRK13548 139 EQQRVQLARVLAqlwEPDGpprWLLLDEPTSALDL 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-181 |
2.83e-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: 66.45 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQkAGLIGANGAGKSSLFALL-------RGQL---GQDAGDCLLPADWRIAHMRQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILatltppsSGTIridGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 72 EVDTLDRLAVDYVLDGDSRLREIqaalavaeaahdgsalarlhteldnaDGYTADARARKLLAGLGFsSEQMERRVGDFS 151
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGI--------------------------PSKEVKARVDEVLELVNL-GDRAKKKIGSLS 132
|
170 180 190
....*....|....*....|....*....|
gi 15600445 152 GGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:cd03264 133 GGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
3.79e-12 |
|
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: 69.48 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQR--LLEAAELTLHAGQKAGLIGANGAGKSSLFALL-------RGQL---GQDAGDcLLPADWR--IA 67
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglyeptSGRIlidGIDLRQ-IDPASLRrqIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 68 HMRQEVD----------TLDRLAVDyvldgDSRLREIqaalavaeaahdgSALARLHTELDN-ADGYtadararkllagl 136
Cdd:COG2274 553 VVLQDVFlfsgtireniTLGDPDAT-----DEEIIEA-------------ARLAGLHDFIEAlPMGY------------- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 137 gfsseqmERRVGD----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLD--AILW--LEEWLKGypGTLVLISHDRDF 208
Cdd:COG2274 602 -------DTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAEteAIILenLRRLLKG--RTVIIIAHRLST 672
|
250
....*....|....*.
gi 15600445 209 LDAvVDHVVHLENRKL 224
Cdd:COG2274 673 IRL-ADRIIVLDKGRI 687
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
322-514 |
4.25e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 66.53 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGEN-----------LAIGYFAQH-----Q 384
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKiLIDGQDithlpmherarLGIGYLPQEasifrK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 LDSLDPQASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARL--ALALIAwqKPNLLLLDEPTNHLD 462
Cdd:TIGR04406 91 LTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVeiARALAT--NPKFILLDEPFAGVD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 463 ----LEMRlALTMALQEFSGAVLVVSHD-RHLLkSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:TIGR04406 168 piavGDIK-KIIKHLKERGIGVLITDHNvRETL-DICDRAYIISDGKVL-AEGTPAE 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-223 |
4.47e-12 |
|
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: 64.71 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR--IAHMRQEVdtldrla 80
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdlrdldLESLRknIAYVPQDP------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 vdYVLDGdsrlreiqaalavaeaahdgsalarlhTELDNadgytadararkLLaglgfsseqmerrvgdfSGGWRMRLNL 160
Cdd:cd03228 86 --FLFSG---------------------------TIREN------------IL-----------------SGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 161 AQALMCPSDLLLLDEPTNHLDLD--AILW--LEEWLKGYpgTLVLISHdRDFLDAVVDHVVHLENRK 223
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPEteALILeaLRALAKGK--TVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
322-486 |
5.93e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.26 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQH----QLDSLDPQASPL-- 395
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvvfQNEGLLPWRNVQdn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 ----LHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL----EMRL 467
Cdd:PRK11248 91 vafgLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftreQMQT 169
|
170
....*....|....*....
gi 15600445 468 ALTMALQEFSGAVLVVSHD 486
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHD 188
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
322-514 |
6.75e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL-------AGDL---------PELGGRLLRGEnlAIGYFAQH-- 383
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglkvndPKVDERLIRQE--AGMVFQQFyl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 --QLDSLDPQASPLLHLQRIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:PRK09493 89 fpHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 462 DLEMR---LALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPfDGDLDD 514
Cdd:PRK09493 168 DPELRhevLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE-DGDPQV 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
322-514 |
7.85e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 65.26 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGEN-----------LAIGYFAQhqldsld 389
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKiLLDGQDitklpmhkrarLGIGYLPQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 pQAS------------PLLHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEP 457
Cdd:cd03218 83 -EASifrkltveenilAVLEIRGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 458 TNHLD----LEMRlALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:cd03218 161 FAGVDpiavQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVL-AEGTPEE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
9.13e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 65.22 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTL----QRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSL-FALLRgqLGQDAGDCLLPADWRIAHMRQEVDT 75
Cdd:cd03257 1 LLEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLaRAILG--LLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 76 LDRLAVDYV-------LD-----GDSrLREIqaalavaeaahdgsalARLHTELDNADgyTADARARKLLAGLGFSSEQM 143
Cdd:cd03257 79 IRRKEIQMVfqdpmssLNprmtiGEQ-IAEP----------------LRIHGKLSKKE--ARKEAVLLLLVGVGLPEEVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 144 ERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLeewLKG----YPGTLVLISHDRDFLDAVVDHV 216
Cdd:cd03257 140 NRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQILDL---LKKlqeeLGLTLLFITHDLGVVAKIADRV 216
|
.
gi 15600445 217 V 217
Cdd:cd03257 217 A 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
322-457 |
9.65e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.44 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGEN-----------LAIGYFAQHqldsld 389
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRiFLDGEDithlpmhkrarLGIGYLPQE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 pqAS------------PLLHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARL--ALALIAwqKPNLLLLD 455
Cdd:COG1137 87 --ASifrkltvednilAVLELRKLSKKEREERLEELLEEFGITHLR-KSKAYSLSGGERRRVeiARALAT--NPKFILLD 161
|
..
gi 15600445 456 EP 457
Cdd:COG1137 162 EP 163
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-217 |
1.00e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 65.15 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCL--------LPADwRIAHM---R--QEVDTLDRLAV-DYVLDG 87
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditgLPPH-EIARLgigRtfQIPRLFPELTVlENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 88 dsrlreiqaalavaEAAHDGSALARLHTELDNADgytADARARKLLAGLGFsSEQMERRVGDFSGGWRMRLNLAQALMCP 167
Cdd:cd03219 100 --------------AQARTGSGLLLARARREERE---ARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 168 SDLLLLDEPT---NHLDLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVV 217
Cdd:cd03219 162 PKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
10-217 |
1.18e-11 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 64.72 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 10 QRGPQRL--LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQ----EVDTLDRLAVDY 83
Cdd:TIGR02324 15 QQGGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQasprEVLEVRRKTIGY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 84 VldgDSRLREIQAALAVAEAAHDGSALARLHTEldnadgytADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQA 163
Cdd:TIGR02324 95 V---SQFLRVIPRVSALEVVAEPLLERGVPREA--------ARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 164 LMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVV 217
Cdd:TIGR02324 164 FIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
323-506 |
1.27e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.50 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAigyfaQHQLDSLD------PQASPL 395
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRiLIDGVDIR-----DLTLESLRrqigvvPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 LH---LQRIAPGEREQT------------LKDFL----GGFDF----RGVrvdepvlNFSGGEKARLALA--LIAwqKPN 450
Cdd:COG1132 426 FSgtiRENIRYGRPDATdeeveeaakaaqAHEFIealpDGYDTvvgeRGV-------NLSGGQRQRIAIAraLLK--DPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 451 LLLLDEPTNHLDLEMRLALTMALQEFSG--AVLVVSHdRhLlkST---TDEFLLVADGRVV 506
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKgrTTIVIAH-R-L--STirnADRILVLDDGRIV 553
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
327-509 |
1.33e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 64.36 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAgdlpelggRLLRGENLAIgyfaqhQLDSLDPQASPLLHLQR---IAP 403
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALF--------RFLEAEEGKI------EIDGIDISTIPLEDLRSsltIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 404 GER---EQTLKDFLGGFD-------FRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMAL 473
Cdd:cd03369 89 QDPtlfSGTIRSNLDPFDeysdeeiYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600445 474 -QEFSGA-VLVVSHDRHLLkSTTDEFLLVADGRVVPFD 509
Cdd:cd03369 169 rEEFTNStILTIAHRLRTI-IDYDKILVMDAGEVKEYD 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
263-506 |
1.80e-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: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 263 IARFKAKATKARQAQsrikalERLEELApaHVDSPFNFSfRESDKISRPLLDLGEGRL----GYGDKaVLEKVKLQLVPG 338
Cdd:TIGR01193 431 IINLQPKLQAARVAN------NRLNEVY--LVDSEFINK-KKRTELNNLNGDIVINDVsysyGYGSN-ILSDISLTIKMN 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 339 ARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA----------IGYFAQHQ-------LDSLDPQASPLLHLQR 400
Cdd:TIGR01193 501 SKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKdidrhtlrqfINYLPQEPyifsgsiLENLLLGAKENVSQDE 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 IAPG----EREQTLKDFLGGFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL--EMR-LALTMAL 473
Cdd:TIGR01193 581 IWAAceiaEIKDDIENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTitEKKiVNNLLNL 657
|
250 260 270
....*....|....*....|....*....|...
gi 15600445 474 QEfsGAVLVVSHdRHLLKSTTDEFLLVADGRVV 506
Cdd:TIGR01193 658 QD--KTIIFVAH-RLSVAKQSDKIIVLDHGKII 687
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
1.97e-11 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 66.93 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTL-QRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR--IAHM 69
Cdd:TIGR02857 322 LEFSGVSVaYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadADSWRdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQevdtldrlaVDYVLDGdSRLREIQAALAvaeaahDGSAlarlhTELDNAdgyTADARARKLLAGLGfssEQMERRVGD 149
Cdd:TIGR02857 402 PQ---------HPFLFAG-TIAENIRLARP------DASD-----AEIREA---LERAGLDEFVAALP---QGLDTPIGE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 150 ----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG--TLVLISHDRDFLdAVVDHVVHL 219
Cdd:TIGR02857 455 ggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-506 |
1.97e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA----------IGYFAQHQLDSL--- 388
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILkPTSGSVLIRGEPITkenirevrkfVGLVFQNPDDQIfsp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 ----DPQASPL-LHLQRIAPGEREQTLKDFLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:PRK13652 95 tveqDIAFGPInLGLDEETVAHRVSSALHMLGLEELR----DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 464 EMRLALTMALQEFS---GAVLVVS-HDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13652 171 QGVKELIDFLNDLPetyGMTVIFStHQLDLVPEMADYIYVMDKGRIV 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
324-506 |
2.33e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.71 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENL------------AIGYFAQHQLDSL-- 388
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPIkydkksllevrkTVGIVFQNPDDQLfa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 -----DPQASPL-LHLQRiapGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:PRK13639 94 ptveeDVAFGPLnLGLSK---EEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 463 LEMRLALTMALQEFS--GAVLVVS-HDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13639 170 PMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMSDGKII 216
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
327-487 |
2.44e-11 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 63.95 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGD-LPELGGRLLRGE----NLA--------------IGYFAQH---- 383
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANyLPDSGRILVRHEgawvDLAqasprevlevrrktIGYVSQFlrvi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 -QLDSLDPQASPLLHL--QRIAPGEREQTLkdflggfdFRGVRVDE-----PVLNFSGGEKAR--LALALIAwqKPNLLL 453
Cdd:TIGR02324 103 pRVSALEVVAEPLLERgvPREAARARAREL--------LARLNIPErlwhlPPATFSGGEQQRvnIARGFIA--DYPILL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600445 454 LDEPTNHLDLEMRLALTMALQEF--SGAVLV-VSHDR 487
Cdd:TIGR02324 173 LDEPTASLDAANRQVVVELIAEAkaRGAALIgIFHDE 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
304-487 |
2.98e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 304 ESDKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLAIGYFAQ 382
Cdd:PRK11607 11 KTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 383 HQLDSLDPQASPLLHL------------QRIAPGEREQTLKDFLGGFDFRGVRVDEPvLNFSGGEKARLALALIAWQKPN 450
Cdd:PRK11607 91 RPINMMFQSYALFPHMtveqniafglkqDKLPKAEIASRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600445 451 LLLLDEPTNHLDLE----MRLALTMALQEFSGAVLVVSHDR 487
Cdd:PRK11607 170 LLLLDEPMGALDKKlrdrMQLEVVDILERVGVTCVMVTHDQ 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
322-505 |
3.10e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 63.32 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA------------IGYFAQH----- 383
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEPDSGTIIIDGLKLTddkkninelrqkVGMVFQQfnlfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 QLDSLDPQASPLLHLQRIAPGEREQTLKDFLggfdfRGVRVDE-----PVlNFSGGEKARLALALIAWQKPNLLLLDEPT 458
Cdd:cd03262 90 HLTVLENITLAPIKVKGMSKAEAEERALELL-----EKVGLADkadayPA-QLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 459 NHLDLEM---------RLA---LTMalqefsgavLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:cd03262 164 SALDPELvgevldvmkDLAeegMTM---------VVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
323-506 |
3.42e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAvLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELG-----GRLLRGENL-----AIGYFAQHQLDSL--- 388
Cdd:PRK13647 17 GTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGrvkvmGREVNAENEkwvrsKVGLVFQDPDDQVfss 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 ----DPQASPL-LHLQRIAPGEREQTLKDFLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:PRK13647 96 tvwdDVAFGPVnMGLDKDEVERRVEEALKAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 464 EMRLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13647 172 RGQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
320-506 |
3.47e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA----------IGYFAQHQLDSL 388
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQhyaskevarrIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQASPLLHLQRIaPGE------REQTLKDFLGGFDFRGVR--VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNH 460
Cdd:PRK10253 95 DITVQELVARGRY-PHQplftrwRKEDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 461 LDLEMRLALTMALQEFS---GAVL-VVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK10253 174 LDISHQIDLLELLSELNrekGYTLaAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-506 |
3.55e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQLDSLD---------- 389
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEfrrrvgmlfq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 -PQASPLLHLQRIAPGEREQTL---KDF----------LGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLD 455
Cdd:PRK14271 109 rPNPFPMSIMDNVLAGVRAHKLvprKEFrgvaqarlteVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 456 EPTNHLDlemrLALTMALQEFSGA------VLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK14271 189 EPTSALD----PTTTEKIEEFIRSladrltVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-491 |
3.61e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA--------------IGYFAQ-HQL----D 386
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTSGDVIFNGQPMSklssaakaelrnqkLGFIYQfHHLlpdfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 387 SLDPQASPLLhLQRIAPGEREQTLKDFLG--GFDFRGV-RVDEpvlnFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:PRK11629 104 ALENVAMPLL-IGKKKPAEINSRALEMLAavGLEHRANhRPSE----LSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|..
gi 15600445 464 EMRLALTMALQEFS----GAVLVVSHDRHLLK 491
Cdd:PRK11629 179 RNADSIFQLLGELNrlqgTAFLVVTHDLQLAK 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
333-514 |
3.63e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 333 LQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRL-LRGENLAIGYFAQHQLDSLDPQASPLLHL---QRIA----PG 404
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTTPPSRRPVSMLFQENNLFSHLtvaQNIGlglnPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 405 -----EREQTLKDFLGgfdfrgvRVD-EPVLN-----FSGGEKARLALA--LIAwQKPnLLLLDEPTNHLD----LEMRL 467
Cdd:PRK10771 100 lklnaAQREKLHAIAR-------QMGiEDLLArlpgqLSGGQRQRVALArcLVR-EQP-ILLLDEPFSALDpalrQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 468 ALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA-WDGPTDE 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
323-506 |
4.63e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.55 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDlPEL---GGR-LLRGENLA-----------IGYFAQHqlds 387
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYevtSGSiLLDGEDILelspderaragIFLAFQY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 ldPQASP------LLHLQRIAPGEREQTLKDFLGGFD--FRGVRVDEPVLN------FSGGEKARLALALIAWQKPNLLL 453
Cdd:COG0396 86 --PVEIPgvsvsnFLRTALNARRGEELSAREFLKLLKekMKELGLDEDFLDryvnegFSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 454 LDEPTNHLDLEmrlALTM------ALQEFSGAVLVVSHDRHLLKSTTDEFLLV-ADGRVV 506
Cdd:COG0396 164 LDETDSGLDID---ALRIvaegvnKLRSPDRGILIITHYQRILDYIKPDFVHVlVDGRIV 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
323-485 |
5.32e-11 |
|
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: 62.38 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAIGYFAQHQ-------LDSLDPQASP 394
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEvRWNGTPLAEQRDEPHEnilylghLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 LLHLQRIAP--GEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD---LEMRLAL 469
Cdd:TIGR01189 91 LENLHFWAAihGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagVALLAGL 169
|
170
....*....|....*.
gi 15600445 470 TMALQEFSGAVLVVSH 485
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
304-506 |
5.42e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 304 ESDKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLaGDLPELGGRLLRGENLAIgYFAQH 383
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIYDSKIKVDGKVL-YFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 --QLDSLD---------PQASPLLHLQ---RIAPGEREQTLKDF-------------LGGFDFRGVRVDEPVLNFSGGEK 436
Cdd:PRK14246 80 ifQIDAIKlrkevgmvfQQPNPFPHLSiydNIAYPLKSHGIKEKreikkiveeclrkVGLWKEVYDRLNSPASQLSGGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 437 ARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
330-517 |
6.31e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 64.36 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 330 KVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRL-LRGENL--------------AIGYFAQhqldsldpQASP 394
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvLNGRTLfdsrkgiflppekrRIGYVFQ--------EARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 LLHL----------QRIAPGER---EQTLKDFLGgfdfRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:TIGR02142 87 FPHLsvrgnlrygmKRARPSERrisFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 462 DLEMRLALTMALQ----EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFdGDLDDYAR 517
Cdd:TIGR02142 163 DDPRKYEILPYLErlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWA 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
338-519 |
6.77e-11 |
|
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: 61.43 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 338 GARIGLLGPNGAGKSTLIKTLAGDLPELGGRllrgenlaigyfaqhqlDSLDpqaspllhlqRIAPGEREQTLKdflggf 417
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-----------------DEWD----------GITPVYKPQYID------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 418 dfrgvrvdepvlnFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFS----GAVLVVSHDRHLLKST 493
Cdd:cd03222 72 -------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeegkKTALVVEHDLAVLDYL 138
|
170 180
....*....|....*....|....*.
gi 15600445 494 TDefllvadgRVVPFDGDLDDYARWL 519
Cdd:cd03222 139 SD--------RIHVFEGEPGVYGIAS 156
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-505 |
7.90e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGEnlaiGYFAQHQLDS-LDPQASPLLHLQR 400
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAEAREDTrLMFQDARLLPWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 I----APGEREQTLKDFLGGFDFRGV--RVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD----LEMRLALT 470
Cdd:PRK11247 98 VidnvGLGLKGQWRDAALQALAAVGLadRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 15600445 471 MALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
328-506 |
1.06e-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: 62.10 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA------IGYFAQHQL-DSLDPQASPLLHLQ 399
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQITepgpdrMVVFQNYSLlPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 400 RIAP----GEREQTLKDFLggfDFRGVR--VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMAL 473
Cdd:TIGR01184 81 RVLPdlskSERRAIVEEHI---ALVGLTeaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600445 474 ----QEFSGAVLVVSHDrhllkstTDEFLLVADgRVV 506
Cdd:TIGR01184 158 mqiwEEHRVTVLMVTHD-------VDEALLLSD-RVV 186
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-224 |
1.08e-10 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 61.74 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 5 LNLTLQRGPQRL--LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQevDTLDRLavd 82
Cdd:cd03255 6 LSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV-DGTDISKLSE--KELAAF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 83 yvldgdsRLREI----QaalavaeaahDGSALARLhTELDNA---------DGYTADARARKLLAGLGFSsEQMERRVGD 149
Cdd:cd03255 80 -------RRRHIgfvfQ----------SFNLLPDL-TALENVelplllagvPKKERRERAEELLERVGLG-DRLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 150 FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLD---AIL-WLEEWLKGYPGTLVLISHDRDFLDAvVDHVVHLENRKL 224
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkEVMeLLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-506 |
1.09e-10 |
|
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: 64.32 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKS-SLFALLRgqlgqdagdcLLPADWRIAHMRQEVDTLDRLAVDyvldgDSRLREIQaalav 100
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvTALSILR----------LLPDPAAHPSGSILFDGQDLLGLS-----ERELRRIR----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 101 aeaahdGSALA------------------------RLHTELDNADgytADARARKLLAGLGFssEQMERRVGDF----SG 152
Cdd:COG4172 91 ------GNRIAmifqepmtslnplhtigkqiaevlRLHRGLSGAA---ARARALELLERVGI--PDPERRLDAYphqlSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 153 GWRMRLNLAQALMCPSDLLLLDEPTNHLD--LDA-ILWLEEWLKGYPGT-LVLISHD----RDFldavVDHVVHLENRKL 224
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqILDLLKDLQRELGMaLLLITHDlgvvRRF----ADRVAVMRQGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 225 TlyrggysafERTRAERLaqqqqayekqqaqrahmesfiarFKAkatkARQAQSR--IKALERLEELAPAHVDSP----- 297
Cdd:COG4172 236 V---------EQGPTAEL-----------------------FAA----PQHPYTRklLAAEPRGDPRPVPPDAPPllear 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 298 -FNFSFResdkISRPLLDLGEGRLgygdKAVlEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLA 376
Cdd:COG4172 280 dLKVWFP----IKRGLFRRTVGHV----KAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 377 igYFAQHQLDSL---------DPQASpL-------------LHLQRIAPG--EREQTLKDFLggfdfRGVRVDEPVLN-- 430
Cdd:COG4172 351 --GLSRRALRPLrrrmqvvfqDPFGS-LsprmtvgqiiaegLRVHGPGLSaaERRARVAEAL-----EEVGLDPAARHry 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 431 ---FSGGEKARLALA--LIAwqKPNLLLLDEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVA 501
Cdd:COG4172 423 pheFSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDVSVQaqiLDLLRDLQrEHGLAYLFISHDLAVVRALAHRVMVMK 500
|
....*
gi 15600445 502 DGRVV 506
Cdd:COG4172 501 DGKVV 505
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-506 |
1.24e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA-------------IGY-FAQHQL-- 385
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPSAGKIWFSGHDITrlknrevpflrrqIGMiFQDHHLlm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 --DSLDPQASPLLhlqrIAPGEREQTLKDFLGGFDFRGV--RVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:PRK10908 93 drTVYDNVAIPLI----IAGASGDDIRRRVSAALDKVGLldKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 462 DLEMRLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK10908 169 DDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-506 |
1.29e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.35 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 333 LQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLAIGYFAQHQLDSL----------------DPQASPL 395
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPPADRPVSMLfqennlfahltveqnvGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 LHLQRIAPGEREQTLKDF-LGGFDFRgvRVDEpvlnFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTM 471
Cdd:cd03298 99 LKLTAEDRQAIEVALARVgLAGLEKR--LPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRaemLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600445 472 AL-QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03298 173 DLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
307-487 |
1.39e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.65 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 307 KISRPLLDLGEgrLGY--GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA------- 376
Cdd:PRK10247 2 QENSPLLQLQN--VGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEGEDIStlkpeiy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 377 ---IGYFAQHQL---DSL-DPQASPLLhLQRIAPgeREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKP 449
Cdd:PRK10247 80 rqqVSYCAQTPTlfgDTVyDNLIFPWQ-IRNQQP--DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 450 NLLLLDEPTNHLDLEMRL----ALTMALQEFSGAVLVVSHDR 487
Cdd:PRK10247 157 KVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDK 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
322-506 |
1.67e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 61.12 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQH-------QLDSLDPQ--- 391
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamvfQNYALYPHmtv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ----ASPLlHLQRIAPGEREQTLKDFLggfdfRGVRVDEpVLN-----FSGGEKARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:cd03301 90 ydniAFGL-KLRKVPKDEIDERVREVA-----ELLQIEH-LLDrkpkqLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 463 ----LEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:cd03301 163 aklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-458 |
1.74e-10 |
|
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: 61.54 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAigyfaqhqldSLDPqaspllhlQ 399
Cdd:COG0410 12 GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSiRFDGEDIT----------GLPP--------H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 400 RIA-------PGER--------EQTLKdfLGGFDFRGV-----RVDE-----PVL---------NFSGGEKARLAL--AL 443
Cdd:COG0410 74 RIArlgigyvPEGRrifpsltvEENLL--LGAYARRDRaevraDLERvyelfPRLkerrrqragTLSGGEQQMLAIgrAL 151
|
170
....*....|....*
gi 15600445 444 IAwqKPNLLLLDEPT 458
Cdd:COG0410 152 MS--RPKLLLLDEPS 164
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-505 |
2.07e-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: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENL------AIGYFAQH------------ 383
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTIRVNGQDVsdlrgrAIPYLRRKigvvfqdfrllp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 QLDSLDPQASPLLHLQrIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:cd03292 92 DRNVYENVAFALEVTG-VPPREIRKRVPAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 464 EMRLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:cd03292 170 DTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
337-513 |
2.08e-10 |
|
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: 59.31 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRgenlaigyfaqhqldsLDPQASPLLHLQRIapgereqtlkdflgg 416
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------IDGEDILEEVLDQL--------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 417 fdfRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDE 496
Cdd:smart00382 50 ---LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
170
....*....|....*..
gi 15600445 497 FLLVADGRVVPFDGDLD 513
Cdd:smart00382 127 KDLGPALLRRRFDRRIV 143
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
2.18e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.21 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLT--LQRGPQRL--LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQevDTL 76
Cdd:COG1136 4 LLELRNLTksYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI-DGQDISSLSE--REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 DRLavdyvldgdsRLREIqaalavaeaahdG------------SAL--ARLHTELDNADGYTADARARKLLAGLGFSsEQ 142
Cdd:COG1136 81 ARL----------RRRHI------------GfvfqffnllpelTALenVALPLLLAGVSRKERRERARELLERVGLG-DR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 143 MERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAilwLEEWLKGYPGTLVLISHDRDfLDAVVDH 215
Cdd:COG1136 138 LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDPE-LAARADR 213
|
250
....*....|
gi 15600445 216 VVHLENRKLT 225
Cdd:COG1136 214 VIRLRDGRIV 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-486 |
2.30e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 62.40 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLP-----ELGGRLL-------RG---------------- 372
Cdd:COG3839 13 YGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPtsgeiLIGGRDVtdlppkdRNiamvfqsyalyphmtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 373 -ENLAIGyfaqhqldsldpqasplLHLQRIAPGEREQtlkdflggfdfrgvRVDE--------PVLN-----FSGGEKAR 438
Cdd:COG3839 93 yENIAFP-----------------LKLRKVPKAEIDR--------------RVREaaellgleDLLDrkpkqLSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 439 LAL--ALIAwqKPNLLLLDEPTNHLD----LEMRLALtMALQEFSGAVLV-VSHD 486
Cdd:COG3839 142 VALgrALVR--EPKVFLLDEPLSNLDaklrVEMRAEI-KRLHRRLGTTTIyVTHD 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-224 |
2.57e-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: 61.36 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 11 RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqLGQdagdcllPADWRIAHMRQEVDTLDRlavdyvldgdSR 90
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LEK-------PAQGTVSFRGQDLYQLDR----------KQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 91 LREIQAALAVAEAAHDGSALARLHTE---------LDNADGYTADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLA 161
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPSAVNPRMTVRqiigeplrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 162 QALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPGT-LVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
324-505 |
2.73e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.95 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYfaQHQ-------LDSLDPQAS--- 393
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKylhskvsLVGQEPVLFars 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 ---------PLLHLQRIAPGEREQTLKDFLGGF-DFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:cd03248 104 lqdniayglQSCSFECVKEAAQKAHAHSFISELaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600445 464 EMRLALTMALQEF--SGAVLVVSHdRHLLKSTTDEFLLVADGRV 505
Cdd:cd03248 184 ESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-205 |
2.81e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 60.66 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdclLPADWRIAHMRQEVDTLDRLAV 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---APDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 dyvldgdSRLREI----QAALAVAEAAHDGSALA-RLHTELDNADgytADARARKLLAGLGFSSEQMER-RVGDFSGGWR 155
Cdd:cd03260 78 -------ELRRRVgmvfQKPNPFPGSIYDNVAYGlRLHGIKLKEE---LDERVEEALRKAALWDEVKDRlHALGLSGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY--PGTLVLISHD 205
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-505 |
3.11e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.27 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 311 PLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLAiGYFAQH------ 383
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPDSGRIMLDGQDIT-HVPAENrhvntv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 -QLDSLDPQASPL------LHLQRIAPGEREQTLKDFLggfdfRGVRVDE----PVLNFSGGEKARLALALIAWQKPNLL 452
Cdd:PRK09452 92 fQSYALFPHMTVFenvafgLRMQKTPAAEITPRVMEAL-----RMVQLEEfaqrKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 453 LLDEPTNHLDLEMRLALTM---ALQEFSGAVLV-VSHDRHLLKSTTDEFLLVADGRV 505
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNelkALQRKLGITFVfVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-506 |
3.17e-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: 60.82 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA--------IGYFAQHQldsldpqa 392
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPDSGTILFGGEDATdvpvqernVGFVFQHY-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPLLHL---QRIAPGEREQTLKDFLGGFDFRGvRVDEpVLNF--------------SGGEKARLALALIAWQKPNLLLLD 455
Cdd:cd03296 84 ALFRHMtvfDNVAFGLRVKPRSERPPEAEIRA-KVHE-LLKLvqldwladrypaqlSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 456 EPTNHLDLEMRLALTMALQEFSGAV----LVVSHDRhllksttDEFLLVADgRVV 506
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQ-------EEALEVAD-RVV 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
337-506 |
3.34e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTLAGDLPE----LGGRLLRGENL------AIGYFAQhQLDSLDPQASPLLHLQ------- 399
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkgSGSVLLNGMPIdakemrAISAYVQ-QDDLFIPTLTVREHLMfqahlrm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 400 --RIAPGEREQTLKDFL---GGFDFRGVRVDEP--VLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMA 472
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLqalGLRKCANTRIGVPgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600445 473 LQEFS----GAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:TIGR00955 209 LKGLAqkgkTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
325-486 |
3.36e-10 |
|
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: 61.61 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVlEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELG---GR-LLRGENLA--------------IGYFAQHQLD 386
Cdd:COG0444 19 KAV-DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEiLFDGEDLLklsekelrkirgreIQMIFQDPMT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 387 SLDP------Q-ASPLLHLQRIAPGEREQTLKDFLggfdfRGVRVDEP--VLN-----FSGGEKAR--LALALIAwqKPN 450
Cdd:COG0444 98 SLNPvmtvgdQiAEPLRIHGGLSKAEARERAIELL-----ERVGLPDPerRLDrypheLSGGMRQRvmIARALAL--EPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600445 451 LLLLDEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHD 486
Cdd:COG0444 171 LLIADEPTTALDVTIQaqiLNLLKDLQrELGLAILFITHD 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
3.46e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 60.87 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQ----RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP------ADWRIAHMR 70
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 71 QEvdtlDRL-----AVDYVldgdsrlreiqaalavaeaahdgsalaRLHTELDNADGYTADARARKLLA--GLgfsSEQM 143
Cdd:COG1116 87 QE----PALlpwltVLDNV---------------------------ALGLELRGVPKAERRERARELLElvGL---AGFE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 144 ERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHldLDAIL------WLEEWLKGYPGTLVLISHDRDflDAVV--DH 215
Cdd:COG1116 133 DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGA--LDALTrerlqdELLRLWQETGKTVLFVTHDVD--EAVFlaDR 208
|
....*..
gi 15600445 216 VVHLENR 222
Cdd:COG1116 209 VVVLSAR 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-205 |
3.48e-10 |
|
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: 62.76 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL----PADWRIAHMRQEVDTLDRLAvdYVLDG 87
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpVSSLDQDEVRRRVSVCAQDA--HLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 88 DSRlreiqaalavaeaahDGSALARlhTELDNADGYTADARAR--KLLAGLgfsSEQMERRVGD----FSGGWRMRLNLA 161
Cdd:TIGR02868 424 TVR---------------ENLRLAR--PDATDEELWAALERVGlaDWLRAL---PDGLDTVLGEggarLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLDAIL-WLEEWLKGYPG-TLVLISHD 205
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-462 |
3.57e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR---IAHMRQEVDTLDRLAV-DY 83
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngPKSSQeagIGIIHQELNLIPQLTIaEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 84 VLDGdsrlREIQaalavaeaahdgSALARLhtelDNADGYtadARARKLLAGLG--FSSEqmeRRVGDFSGGWRMRLNLA 161
Cdd:PRK10762 100 IFLG----REFV------------NRFGRI----DWKKMY---AEADKLLARLNlrFSSD---KLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 162 QALMCPSDLLLLDEPTNHL---DLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVvhlenrklTLYRGGysafertr 238
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDV--------TVFRDG-------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 239 aerlaqqqqayekqqaqrahmeSFIARfkaKATKARQAQSRIKAL--ERLEELAPaHVDSPfnfsfresdkisrplldLG 316
Cdd:PRK10762 218 ----------------------QFIAE---REVADLTEDSLIEMMvgRKLEDQYP-RLDKA-----------------PG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 317 EGRL------GYGdkavLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRL-LRGENLA-----------IG 378
Cdd:PRK10762 255 EVRLkvdnlsGPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtLDGHEVVtrspqdglangIV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 379 YFAQHQ----------------LDSLDPQASPLLHLQRiapGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALA 442
Cdd:PRK10762 331 YISEDRkrdglvlgmsvkenmsLTALRYFSRAGGSLKH---ADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIA 407
|
490 500
....*....|....*....|
gi 15600445 443 LIAWQKPNLLLLDEPTNHLD 462
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-221 |
3.96e-10 |
|
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: 59.12 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEVDTLDRlAV 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDLTDLEDELPPLRR-RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVldgdsrlreIQAalavaeaahdgSALARLHTELDNadgytadararkLLAGLgfsseqmerrvgdfSGGWRMRLNLA 161
Cdd:cd03229 79 GMV---------FQD-----------FALFPHLTVLEN------------IALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLDAILWLEEWLK------GYpgTLVLISHDRDFLDAVVDHVVHLEN 221
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKslqaqlGI--TVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-217 |
4.66e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 60.42 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDC----LLPADWRIAHMRQEVDTL---DRLAVDY-VLDGDSRLRE 93
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRRIGVVFgqkTQLWWDLpVIDSFYLLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 94 IQaalavaeaahdgsalarlhtELDnadgytaDARARKLLAGLgfsSEQME------RRVGDFSGGWRMRLNLAQALMCP 167
Cdd:cd03267 122 IY--------------------DLP-------PARFKKRLDEL---SELLDleelldTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 168 SDLLLLDEPTNHLDLDAILWLEEWLKGY----PGTLVLISHDRDFLDAVVDHVV 217
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
322-486 |
5.08e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.48 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGR---------------LLRGEN------ 374
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPpdsgevLVDGLdvattpsrelakrlaILRQENhinsrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 375 -----LAIGYFAQHQ--LDSLDPQAspllhlqrIapgerEQTLkDFLGGFDFRGVRVDEpvlnFSGGEKARlalALIAW- 446
Cdd:COG4604 91 tvrelVAFGRFPYSKgrLTAEDREI--------I-----DEAI-AYLDLEDLADRYLDE----LSGGQRQR---AFIAMv 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 447 --QKPNLLLLDEPTNHLDL----EMRLALTMALQEFSGAVLVVSHD 486
Cdd:COG4604 150 laQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-217 |
6.40e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.11 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADwRIAHMRQEVDTldrlavdyvlDGDSRLREIqa 96
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKA----------DYEGTVRDL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 97 alavaeaahdgsalarLHTELDNAdgYTADARARKLLAGLGFSSeQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEP 176
Cdd:cd03237 82 ----------------LSSITKDF--YTHPYFKTEIAKPLQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 177 TNHLDLDAILWLEEWLKGY----PGTLVLISHDRDFLDAVVDHVV 217
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLI 187
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-489 |
8.71e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.75 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQH---QLDSLDPQASPLLHLQR 400
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylPLGTLREALLYPATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 IAPGEREQTLKDF-LGGFDFRgvrVDEP-----VLnfSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQ 474
Cdd:COG4178 455 FSDAELREALEAVgLGHLAER---LDEEadwdqVL--SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
170 180
....*....|....*....|....*
gi 15600445 475 EFSGAVLVVS----------HDRHL 489
Cdd:COG4178 530 EELPGTTVISvghrstlaafHDRVL 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
319-506 |
9.51e-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: 59.17 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGD-KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--DlPELGGRLLRGENLAigyfaQHQLDSLD------ 389
Cdd:cd03253 7 TFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfyD-VSSGSILIDGQDIR-----EVTLDSLRraigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 PQASPLLH---LQRIAPGEREQT----------------LKDFLGGFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPN 450
Cdd:cd03253 81 PQDTVLFNdtiGYNIRYGRPDATdeevieaakaaqihdkIMRFPDGYD---TIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 451 LLLLDEPTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLkSTTDEFLLVADGRVV 506
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHRLSTI-VNADKIIVLKDGRIV 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
322-506 |
1.13e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL-------------AG---DLP----ELGGRLLRGEnlaIGY-F 380
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdsgqlniAGhqfDFSqkpsEKAIRLLRQK---VGMvF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 381 AQHQL-------DSLDPQASPLLHLQRIAPGEREQTLKDFLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLL 453
Cdd:COG4161 89 QQYNLwphltvmENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKA----DRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 454 LDEPTNHLDLEMRLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-216 |
1.31e-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: 58.54 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL--------PADWR--IAHMRQEvdt 75
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvrePREVRrrIGIVFQD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 76 ldrLAVDYVLDGDSRLReiqaalavaeaahdgsalarLHTELDNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWR 155
Cdd:cd03265 82 ---LSVDDELTGWENLY--------------------IHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAI--LW--LEEWLKGYPGTLVLISHDRDFLDAVVDHV 216
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
312-499 |
1.34e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 312 LLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGdlpelggrLLRGENLAIGYFAQH---QLDSL 388
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--------LLNPEKGEILFERQSikkDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQASPLLHLQRIAPG--EREQTLKDFlgGFDFRGVRVDEPVLNF-------------SGGEKARLALALIAWQKPNLLL 453
Cdd:PRK13540 73 QKQLCFVGHRSGINPYltLRENCLYDI--HFSPGAVGITELCRLFslehlidypcgllSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 454 LDEPTNHLDLEMRLALTMALQEF---SGAVLVVSH-DRHLLKSTTDEFLL 499
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHrakGGAVLLTSHqDLPLNKADYEEYHL 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-485 |
1.36e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRL-LRGENLAIGYFAQ------HQlDSLDPQASPL 395
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDPDVAEachylgHR-NAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 LHLQ---RIApGEREQTLKDFLGGFDFRGVrVDEPVLNFSGGEKARLALA--LIAWQkpNLLLLDEPTNHLDL---EMRL 467
Cdd:PRK13539 92 ENLEfwaAFL-GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALArlLVSNR--PIWILDEPTAALDAaavALFA 167
|
170
....*....|....*...
gi 15600445 468 ALTMALQEFSGAVLVVSH 485
Cdd:PRK13539 168 ELIRAHLAQGGIVIAATH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
1.53e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.60 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQ----RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwRIAHMRQEVDTL 76
Cdd:COG4181 8 IIELRGLTKTvgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSG--------TVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 DRlavdyvlDGDSRLReiqaalavaeAAHDG------------SAL--ARLHTELDNADGytADARARKLLA--GLGfss 140
Cdd:COG4181 80 DE-------DARARLR----------ARHVGfvfqsfqllptlTALenVMLPLELAGRRD--ARARARALLErvGLG--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 141 EQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPG-TLVLISHDRDfLDAVVDHV 216
Cdd:COG4181 138 HRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHDPA-LAARCDRV 216
|
....*....
gi 15600445 217 VHLENRKLT 225
Cdd:COG4181 217 LRLRAGRLV 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
1.56e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.87 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHM--RQEVDTLDR 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-GDKPISMLssRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 79 LAVDYVLDGDSRLREIQAALAVAEAAHDGsalaRLHTElDNADGYTADARARkllaglgfSSEQMERRVGDFSGGWRMRL 158
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWG----RLSAE-DNARVNQAMEQTR--------INHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLD---AILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLT 225
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-227 |
1.92e-09 |
|
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: 58.06 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAdwriahmrQEVDTLDRLAV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYV-----LDGDSRLREIQAAlavaeaahdgsaLARLHteldnadGYT---ADARARKLLAGLGFsSEQMERRVGDFSGG 153
Cdd:cd03269 73 GYLpeergLYPKMKVIDQLVY------------LAQLK-------GLKkeeARRRIDEWLERLEL-SEYANKRVEELSKG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 154 WRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKgypgTLVLISHDRDFLDAVVDHVVHLENRKLTL 226
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDpvnvellKDVIRELARAGK----TVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
.
gi 15600445 227 Y 227
Cdd:cd03269 209 Y 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
311-462 |
1.92e-09 |
|
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: 58.44 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 311 PLLDLGEGRLGYGDKA-VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELG---GR-LLRGENLAIGYFAQH-- 383
Cdd:cd03234 5 PWWDVGLKAKNWNKYArILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQiLFNGQPRKPDQFQKCva 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 ---QLDSLDPQA--------SPLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVL-NFSGGEKARLALALIAWQKPNL 451
Cdd:cd03234 85 yvrQDDILLPGLtvretltyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQLLWDPKV 164
|
170
....*....|.
gi 15600445 452 LLLDEPTNHLD 462
Cdd:cd03234 165 LILDEPTSGLD 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-506 |
1.95e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLagDLPELGgrllRGENLAIgyfAQHQLD-SLDPQASPLLHLQR 400
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLLEMP----RSGTLNI---AGNHFDfSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 ---------------------I-AP-----------GEREQTLKDFLGGFDFrgvrVDEPVLNFSGGEKARLALALIAWQ 447
Cdd:PRK11124 83 nvgmvfqqynlwphltvqqnlIeAPcrvlglskdqaLARAEKLLERLRLKPY----ADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 448 KPNLLLLDEPTNHLDLEMRLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-514 |
2.05e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.97 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA------IGY--------------- 379
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSGEVLWDGEPLDpedrrrIGYlpeerglypkmkvge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 380 ----FAQ-HQLDSLDPQASPLLHLQRIAPGEReqtlkdflggfdfRGVRVDEpvlnFSGGE--KARLALALIAwqKPNLL 452
Cdd:COG4152 91 qlvyLARlKGLSKAEAKRRADEWLERLGLGDR-------------ANKKVEE----LSKGNqqKVQLIAALLH--DPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 453 LLDEPTNHLDLEMRLALTMALQEF--SGA-VLVVSHDRHLLKSTTDEFLLVADGRVVpFDGDLDD 514
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELaaKGTtVIFSSHQMELVEELCDRIVIINKGRKV-LSGSVDE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
2.10e-09 |
|
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: 57.91 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWRIAHMRQe 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvpPERRNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 73 vdtldrlavDYVLDGDSRLRE-IqaalavaeaahdGSALARLHTELDNADgytadARARKLLAGLGFSsEQMERRVGDFS 151
Cdd:cd03259 80 ---------DYALFPHLTVAEnI------------AFGLKLRGVPKAEIR-----ARVRELLELVGLE-GLLNRYPHELS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 152 GGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG----TLVLISHDRDFLDAVVDHVVHLEN 221
Cdd:cd03259 133 GGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIAVMNE 206
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
324-506 |
2.13e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--DLPELGGRLL-RGENL---------AIGYFAQHQLDSLDPQ 391
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEfKGKDLlelspedraGEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQRIAPGEREQTLKDFLGGFDF-------------------RGVRVdepvlNFSGGEKARLALALIAWQKPNLL 452
Cdd:PRK09580 93 VSNQFFLQTALNAVRSYRGQEPLDRFDFqdlmeekiallkmpedlltRSVNV-----GFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 453 LLDEPTNHLDLEmrlALTM------ALQEFSGAVLVVSHDRHLLKSTTDEFLLVA-DGRVV 506
Cdd:PRK09580 168 ILDESDSGLDID---ALKIvadgvnSLRDGKRSFIIVTHYQRILDYIKPDYVHVLyQGRIV 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
331-506 |
2.16e-09 |
|
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: 59.73 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 331 VKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLL----RGENL-----AIGY-FaqhQLDSLDPqasp 394
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERpdsgriRLGGEVLqdsaRGIFLpphrrRIGYvF---QEARLFP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 llHL----------QRIAPGEReqtlkdflgGFDFRGVrVD----EPVLNF-----SGGEKARLAL--ALIAwqKPNLLL 453
Cdd:COG4148 91 --HLsvrgnllygrKRAPRAER---------RISFDEV-VEllgiGHLLDRrpatlSGGERQRVAIgrALLS--SPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 454 LDEPTNHLDLEMRLA----LTMALQEFSGAVLVVSHD----RHLlkstTDEFLLVADGRVV 506
Cdd:COG4148 157 MDEPLAALDLARKAEilpyLERLRDELDIPILYVSHSldevARL----ADHVVLLEQGRVV 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
2.19e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGD---CLLPADWRIAHMRQEVDTLDR 78
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSislCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 79 LAvdyVLDGDSRLREIQAALAVAEAAHDGSALARLHTELDNAdgytadararKLlaglgfsSEQMERRVGDFSGGWRMRL 158
Cdd:PRK13537 88 FD---NLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFA----------KL-------ENKADAKVGELSGGMKRRL 147
|
170 180 190
....*....|....*....|....*....|.
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDA--ILW 187
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQArhLMW 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
308-462 |
2.20e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.63 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 308 ISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL--AGDL-PEL---GGRLLRGENL------ 375
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLnPEVtitGSIVYNGHNIysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 376 ------AIGYFAQHqldsldPQASPLLHLQRIAPGEREQTLKD----------FLGG---FDFRGVRVDEPVLNFSGGEK 436
Cdd:PRK14239 81 tvdlrkEIGMVFQQ------PNPFPMSIYENVVYGLRLKGIKDkqvldeavekSLKGasiWDEVKDRLHDSALGLSGGQQ 154
|
170 180
....*....|....*....|....*.
gi 15600445 437 ARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
325-509 |
2.29e-09 |
|
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: 57.89 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA-IGYFAQHQLDSLDPQaSPLLH----- 397
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSiLIDGVDISkIGLHDLRSRISIIPQ-DPVLFsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 398 -----LQRIAPGEREQTLKD---------FLGGFDFRgvrVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:cd03244 96 snldpFGEYSDEELWQALERvglkefvesLPGGLDTV---VEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 464 EmrlalTMAL------QEFSGA-VLVVSHD-RHLLKSttDEFLLVADGRVVPFD 509
Cdd:cd03244 173 E-----TDALiqktirEAFKDCtVLTIAHRlDTIIDS--DRILVLDKGRVVEFD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-205 |
2.62e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDC---------LLPADWRIahMRQEVDTL 76
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplakLNRAQRKA--FRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 DRLAVDYVlDGDSRLREIQaalavaeaahdGSALARLhTELDNADgytADARARKLLAGLGFSSEQMERRVGDFSGGWRM 156
Cdd:PRK10419 95 FQDSISAV-NPRKTVREII-----------REPLRHL-LSLDKAE---RLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLDL---DAILWLEEWLKGYPGT-LVLISHD 205
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHD 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-182 |
3.42e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.79 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAG----DCLLPADW-------RIAHM 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGevlvDGLDVATTpsrelakRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQEVDTLDRLAV-DYVLDG-----DSRLREIQaalavaeAAHDGSALARLhtELDNadgytadararklLAglgfsseqm 143
Cdd:COG4604 81 RQENHINSRLTVrELVAFGrfpysKGRLTAED-------REIIDEAIAYL--DLED-------------LA--------- 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600445 144 ERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL 182
Cdd:COG4604 130 DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
327-506 |
3.47e-09 |
|
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: 57.88 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA----------IGYFAQHQL-------DSL 388
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfYVPENGRVLVDGHDLAladpawlrrqVGVVLQENVlfnrsirDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 dPQASPLLHLQRIAPGEREQTLKDFLG----GFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE 464
Cdd:cd03252 97 -ALADPGMSMERVIEAAKLAGAHDFISelpeGYD---TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600445 465 MRLALTMALQEFSG--AVLVVSHDRHLLKsTTDEFLLVADGRVV 506
Cdd:cd03252 173 SEHAIMRNMHDICAgrTVIIIAHRLSTVK-NADRIIVMEKGRIV 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-183 |
3.75e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.08 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADwriahmrqEVDTLDRLA 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD--------DVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VdyvldgdSRLREIQAALAVAEAAHDGSALARL--HTELDNADGYT-ADARARKLLAGLGFSSEQMERRVGDFSGGWRMR 157
Cdd:PRK09536 75 A-------SRRVASVPQDTSLSFEFDVRQVVEMgrTPHRSRFDTWTeTDRAAVERAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180
....*....|....*....|....*.
gi 15600445 158 LNLAQALMCPSDLLLLDEPTNHLDLD 183
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDIN 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-225 |
4.57e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 56.98 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTL-QRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALL-------RGQL---GQDAGDclLPaDWRIAHM 69
Cdd:COG2884 1 MIRFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLygeerptSGQVlvnGQDLSR--LK-RREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQevdtldRLAVdyVLDgDSRLreiqaalavaeaahdgsaLARLhTELDN---------ADGYTADARARKLLA--GLgf 138
Cdd:COG2884 78 RR------RIGV--VFQ-DFRL------------------LPDR-TVYENvalplrvtgKSRKEIRRRVREVLDlvGL-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 139 sSEQMERRVGDFSGGWRMRLNLAQAL-MCPsDLLLLDEPTNHLDLDAILWLEEWLKGY--PGTLVLI-SHDRDFLDAVVD 214
Cdd:COG2884 128 -SDKAKALPHELSGGEQQRVAIARALvNRP-ELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPK 205
|
250
....*....|.
gi 15600445 215 HVVHLENRKLT 225
Cdd:COG2884 206 RVLELEDGRLV 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-226 |
5.22e-09 |
|
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: 56.17 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQR--LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---PADWRIAHMRQEVDTL 76
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 DRLAvdYVLDGdsrlreiqaalavaeaahdgsalarlhTELDNadgytadararkllagLGfsseqmeRRvgdFSGGWRM 156
Cdd:cd03247 81 NQRP--YLFDT---------------------------TLRNN----------------LG-------RR---FSGGERQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLD----LDAILWLEEWLKGypGTLVLISHDrdfLDAV--VDHVVHLENRKLTL 226
Cdd:cd03247 106 RLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD--KTLIWITHH---LTGIehMDKILFLENGKIIM 176
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-225 |
5.49e-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: 58.20 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 20 AELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEVD-TLDRLAVDYVLDgDSRLreiqaal 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGRTLFDSRKGIFlPPEKRRIGYVFQ-EARL------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 99 avaeAAHDGSAlARLHTELDNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTN 178
Cdd:TIGR02142 87 ----FPHLSVR-GNLRYGMKRARPSERRISFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600445 179 HLDL---DAIL-WLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLT 225
Cdd:TIGR02142 161 ALDDprkYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-205 |
6.48e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLrGQLGQDAGdcllpADWRIAHmrQEVDTLDRlavdyvlDGDSRLREiqa 96
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTS-----GTYRVAG--QDVATLDA-------DALAQLRR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 97 alavaeaAHDGSALARLH--TELDNADGYTADA------------RARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQ 162
Cdd:PRK10535 86 -------EHFGFIFQRYHllSHLTAAQNVEVPAvyaglerkqrllRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 163 ALMCPSDLLLLDEPTNHLD------LDAILwleEWLKGYPGTLVLISHD 205
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDshsgeeVMAIL---HQLRDRGHTVIIVTHD 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-181 |
6.59e-09 |
|
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: 56.81 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRG-PQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAG-----DCLLPADW---------RI 66
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsvlidGTDINKLKgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 67 AHMRQEVDTLDRL-AVDYVLDGdsRLreiqaalavaEAAHDGSALARLHTELDNadgytadARARKLLAGLGFsSEQMER 145
Cdd:cd03256 81 GMIFQQFNLIERLsVLENVLSG--RL----------GRRSTWRSLFGLFPKEEK-------QRALAALERVGL-LDKAYQ 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600445 146 RVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:cd03256 141 RADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
322-506 |
8.01e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP-------------ELGGRLLRgENLAIGYFAQHQLDSL 388
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgsPLKASNIR-DTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQASPllhLQRIAPGErEQTLKDFLGGFD---------FRGVRVDE-----PVLNFSGGEKARLALALIAWQKPNLLLL 454
Cdd:TIGR02633 90 VPELSV---AENIFLGN-EITLPGGRMAYNamylraknlLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 455 DEPTNHL---DLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:TIGR02633 166 DEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-219 |
1.12e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.61 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqlgqdagdcllpadwriaHMRQEVDtldrlavdyvl 85
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG------------------HPKYEVT----------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 DGDSRLreiqaalavaeaahDGSALarlhTELdnadgyTADARARKLLaGLGFSS---------EQMERRVGD-FSGGWR 155
Cdd:cd03217 56 EGEILF--------------KGEDI----TDL------PPEERARLGI-FLAFQYppeipgvknADFLRYVNEgFSGGEK 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY--PGT-LVLISHDRDFLDAVVDHVVHL 219
Cdd:cd03217 111 KRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYIKPDRVHV 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
322-506 |
1.24e-08 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 56.16 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL-------AGDLpELGGRLL--RGENLA-----IGYFAQH---- 383
Cdd:COG1126 11 FGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI-TVDGEDLtdSKKDINklrrkVGMVFQQfnlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 -QLDSLDPQASPLLHLQRIAPGEREQTLKDFL---GGFDFRGVRVDEpvLnfSGGEK-----ARlALALiawqKPNLLLL 454
Cdd:COG1126 90 pHLTVLENVTLAPIKVKKMSKAEAEERAMELLervGLADKADAYPAQ--L--SGGQQqrvaiAR-ALAM----EPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 455 DEPTNHLDLEM---------RLA---LTMalqefsgavLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:COG1126 161 DEPTSALDPELvgevldvmrDLAkegMTM---------VVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-224 |
1.37e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.93 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 14 QRLLEAAELTLHAGQKAGLIGANGAGKSSLF-ALL-----RGQL---GQDAGDcLLPADWR--IAHMRQEVDTLDRLAVD 82
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLnALLgflpyQGSLkinGIELRE-LDPESWRkhLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 83 YVLDGDSRLREiqaalavaeaahdgsalARLHTELDNADgytADARARKLLAGLGFS-SEQMERrvgdFSGGWRMRLNLA 161
Cdd:PRK11174 442 NVLLGNPDASD-----------------EQLQQALENAW---VSEFLPLLPQGLDTPiGDQAAG----LSVGQAQRLALA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLD---AILW-LEEWLKGYpgTLVLISHDRDFLDAvVDHVVHLENRKL 224
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHseqLVMQaLNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
125-220 |
1.43e-08 |
|
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: 55.61 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEwlKGYpg 197
Cdd:cd03262 112 AEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvgevLDVMKDLAE--EGM-- 186
|
90 100
....*....|....*....|...
gi 15600445 198 TLVLISHDRDFLDAVVDHVVHLE 220
Cdd:cd03262 187 TMVVVTHEMGFAREVADRVIFMD 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
324-506 |
1.46e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLA----------IGYFAQhQLdsldPQA 392
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEiLLDAQPLEswsskafarkVAYLPQ-QL----PAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPLL------------H--LQRIAPGEREQTLK--DFLGGFDFRGVRVDepvlNFSGGEKARLALALIAWQKPNLLLLDE 456
Cdd:PRK10575 98 EGMTvrelvaigrypwHgaLGRFGAADREKVEEaiSLVGLKPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 457 PTNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK10575 174 PTSALDIAHQvdvLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
301-491 |
1.47e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 301 SFRESDKISRPLLDLGEG---RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG---DLPELGGRLLR--- 371
Cdd:COG2401 16 VYSSVLDLSERVAIVLEAfgvELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalkGTPVAGCVDVPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 372 -GENLAIgyfaqhqLDSLDPQASPLLHLQRIApgereqtlkdflggfdfrGVRVDEPVL------NFSGGEKARLALALI 444
Cdd:COG2401 96 fGREASL-------IDAIGRKGDFKDAVELLN------------------AVGLSDAVLwlrrfkELSTGQKFRFRLALL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600445 445 AWQKPNLLLLDEPTNHLDLE--MRLALTM--ALQEFSGAVLVVSHDRHLLK 491
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQtaKRVARNLqkLARRAGITLVVATHHYDVID 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
322-462 |
1.57e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGEN------------LAIGYFAQH-----Q 384
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYLPQEasifrR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 385 LDSLDPQASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:PRK10895 93 LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-204 |
1.75e-08 |
|
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: 54.81 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAdwriahmrqevdtldrlavdyvl 85
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 DGDSRLREIQAALAVAEAAHDG-----SALARLH-TELDNADGYTADARARKLLAGLGfsseqmERRVGDFSGGWRMRLN 159
Cdd:cd03231 62 GPLDFQRDSIARGLLYLGHAPGikttlSVLENLRfWHADHSDEQVEEALARVGLNGFE------DRPVAQLSAGQQRRVA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 160 LAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYP---GTLVLISH 204
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
328-506 |
1.81e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.01 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGE-----------NL--AIGYFAQ---HQLDSL--- 388
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmKLreSVGMVFQdpdNQLFSAsvy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 -DPQASPL-LHLQRIAPGEREQTLKDFLGGFDFRgvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE-- 464
Cdd:PRK13636 102 qDVSFGAVnLKLPEDEVRKRVDNALKRTGIEHLK----DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMgv 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 465 ---MRLALTMAlQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13636 178 seiMKLLVEMQ-KELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-462 |
1.85e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.86 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENlaIGYFAQHQLDSL------DPQA--SP- 394
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSiLIDGKD--VTKLPEYKRAKYigrvfqDPMMgtAPs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 -------LLHLQR---------IAPGEREQtLKDFLGGFDfRGV--RVDEPVLNFSGGEkaRLALALI--AWQKPNLLLL 454
Cdd:COG1101 97 mtieenlALAYRRgkrrglrrgLTKKRREL-FRELLATLG-LGLenRLDTKVGLLSGGQ--RQALSLLmaTLTKPKLLLL 172
|
....*...
gi 15600445 455 DEPTNHLD 462
Cdd:COG1101 173 DEHTAALD 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-505 |
1.94e-08 |
|
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: 57.14 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRG--QLGQDAGDCLLP-ADWRIAHMRqevdtld 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSgSPLKASNIR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 78 rlavdyvldgDSRLREIQAALAVAEAAHDGSALAR--LHTELDNADGYTADA----RARKLLAGLGFSSEQMERRVGDFS 151
Cdd:TIGR02633 74 ----------DTERAGIVIIHQELTLVPELSVAENifLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGDYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 152 GGWRMRLNLAQALMCPSDLLLLDEPTNHL---DLDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDhvvhlenrKLTLYR 228
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCD--------TICVIR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 229 GGysafertraERLAQQQQAYEKQQAQRAHMesfIARfKAKATKARQAQSRIKALERLEELAPAHVDSPfnfsfresdKI 308
Cdd:TIGR02633 216 DG---------QHVATKDMSTMSEDDIITMM---VGR-EITSLYPHEPHEIGDVILEARNLTCWDVINP---------HR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRplldlgegrlgygdkavLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPelggrllrGENLAIGYFAQHQLDSL 388
Cdd:TIGR02633 274 KR-----------------VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP--------GKFEGNVFINGKPVDIR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQASpLLHLQRIAPGEREQ-------------TLKdFLGGFDFRGvRVDE-----------------------PVLNFS 432
Cdd:TIGR02633 329 NPAQA-IRAGIAMVPEDRKRhgivpilgvgkniTLS-VLKSFCFKM-RIDAaaelqiigsaiqrlkvktaspflPIGRLS 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 433 GGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyeiYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
313-506 |
2.00e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 55.13 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 313 LDLGEGRLgygdkAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLA--------------I 377
Cdd:COG4181 18 VGTGAGEL-----TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPTSGTVRLAGQDLFaldedararlrarhV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 378 GYFAQ--HQLDSL----------------DPQASPLLHLQRIAPGEREQTLKDFLggfdfrgvrvdepvlnfSGGEKARL 439
Cdd:COG4181 93 GFVFQsfQLLPTLtalenvmlplelagrrDARARARALLERVGLGHRLDHYPAQL-----------------SGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 440 ALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMALQEFSGAVLV-VSHDRHLLKStTDEFLLVADGRVV 506
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGeqiIDLLFELNRERGTTLVlVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
322-506 |
2.04e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRL---------LRGENLAIGYFAQH-----QLDS 387
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQHyalfrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQASPLLHLQRiapgeREQTLKDFLggfDFRGVRVDEPV----------LNFSGGEKARLALALIAWQKPNLLLLDEP 457
Cdd:PRK10851 92 FDNIAFGLTVLPR-----RERPNAAAI---KAKVTQLLEMVqlahladrypAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 458 TNHLDLEMRLALTMAL----QEFSGAVLVVSHDRhllksttDEFLLVADgRVV 506
Cdd:PRK10851 164 FGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQ-------EEAMEVAD-RVV 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
319-506 |
2.33e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVK---LQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL-RGENLAIGYFA----------QHQ 384
Cdd:PRK15112 17 RTGWFRRQTVEAVKplsFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiDDHPLHFGDYSyrsqrirmifQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 LDSLDPQAS-------PLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEP 457
Cdd:PRK15112 97 STSLNPRQRisqildfPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 458 TNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK15112 177 LASLDMSMRsqlINLMLELQEKQGiSYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
337-485 |
2.38e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTLAGDLPELGG-RLLRGENLAIGYFAQH-------QLDSLDPQASPLLHLQ-----RIAP 403
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGKSILTNISDVHqnmgycpQFDAIDDLLTGREHLYlyarlRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 404 GEREQTLKDFlgGFDFRGVRV--DEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLAL---TMALQEFSG 478
Cdd:TIGR01257 2044 AEEIEKVANW--SIQSLGLSLyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwntIVSIIREGR 2121
|
....*..
gi 15600445 479 AVLVVSH 485
Cdd:TIGR01257 2122 AVVLTSH 2128
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
321-470 |
3.02e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 55.25 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQH----QLDSLDPQASPL- 395
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRgvvfQKDALLPWLNVLd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 -----LHLQRIAPGEREQTLKDFLGGFDFRGVRvDEPVLNFSGGEKAR--LALALIAwqKPNLLLLDEPTNHLDlemrlA 468
Cdd:COG4525 96 nvafgLRLRGVPKAERRARAEELLALVGLADFA-RRRIWQLSGGMRQRvgIARALAA--DPRFLLMDEPFGALD-----A 167
|
..
gi 15600445 469 LT 470
Cdd:COG4525 168 LT 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-224 |
3.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 15 RLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQL----GQD-AGDCLLPADWR----IAHMRQEVDTLDRLAvDYVL 85
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetGQTiVGDYAIPANLKkikeVKRLRKEIGLVFQFP-EYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 DGDSRLREIqaalavaeaahdgsALARLHTELDNADGYTadaRARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALM 165
Cdd:PRK13645 104 FQETIEKDI--------------AFGPVNLGENKQEAYK---KVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 166 CPSDLLLLDEPTNHLD----LDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-222 |
3.75e-08 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 54.40 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQ----RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwriahMRQEVDTLD 77
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV--------DGEPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 78 RlAVDYVLDGDSRL--REIQaalavaeaahDGSALARLHTELDNADgytADARARKLLA--GL-GFSSeqmeRRVGDFSG 152
Cdd:cd03293 73 P-DRGYVFQQDALLpwLTVL----------DNVALGLELQGVPKAE---ARERAEELLElvGLsGFEN----AYPHQLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 153 GWRMRLNLAQALMCPSDLLLLDEPTNHLD----LDAILWLEEWLKGYPGTLVLISHDRDflDAVV--DHVVHLENR 222
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHDID--EAVFlaDRVVVLSAR 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
4.15e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLR------------GQLGQDAGDCLLPADWRIAH 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 69 MRQEVDTL--------DRLAVDYVLDGDSRLREIQAALavaeaahdgsalarlhteldnadgytADARARKLLAGLGFSS 140
Cdd:PRK11264 83 LRQHVGFVfqnfnlfpHRTVLENIIEGPVIVKGEPKEE--------------------------ATARARELLAKVGLAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 141 EQ--MERRVgdfSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKgypgTLVLISHDRDFLDA 211
Cdd:PRK11264 137 KEtsYPRRL---SGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQEKR----TMVIVTHEMSFARD 209
|
....*.
gi 15600445 212 VVDHVV 217
Cdd:PRK11264 210 VADRAI 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
320-506 |
5.45e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.01 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 320 LGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGenlaigyfaqHQLDSLDP--------- 390
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKING----------IELRELDPeswrkhlsw 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 --QASPLLH---LQRIAPG-------EREQTLK-----DFL----GGFDFRgvrVDEPVLNFSGGEKARLALALIAWQKP 449
Cdd:PRK11174 428 vgQNPQLPHgtlRDNVLLGnpdasdeQLQQALEnawvsEFLpllpQGLDTP---IGDQAAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 450 NLLLLDEPTNHLDLEMRLALTMALQEFSGA--VLVVSHDRHLLKStTDEFLLVADGRVV 506
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTHQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-216 |
5.65e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 55.12 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSL-FALLR------GQL---GQDAGDcLLPADWRiaHMRQEV-----DTLDRLavdyvld 86
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLgRLLLRleeptsGEIlfdGQDITG-LSGRELR--PLRRRMqmvfqDPYASL------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 87 gDSRLREiqaalavaeaahdGSALA---RLHTELDNADgytADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQA 163
Cdd:COG4608 109 -NPRMTV-------------GDIIAeplRIHGLASKAE---RRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 164 LMCPSDLLLLDEPTNHLDLD---AILWLEEWLKGYPG-TLVLISHDrdfLdAVVDHV 216
Cdd:COG4608 172 LALNPKLIVCDEPVSALDVSiqaQVLNLLEDLQDELGlTYLFISHD---L-SVVRHI 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-464 |
5.66e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLaGDLPEL-------GGRLLRGENL----AIGYFAQHQLDS 387
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIELypearvsGEVYLDGQDIfkmdVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 LDPQASPLL----------HLQRIAPGERE--QTLKDFLGG---FDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLL 452
Cdd:PRK14247 89 QIPNPIPNLsifenvalglKLNRLVKSKKElqERVRWALEKaqlWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170
....*....|..
gi 15600445 453 LLDEPTNHLDLE 464
Cdd:PRK14247 169 LADEPTANLDPE 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
5.81e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.58 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNL-----TLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGD--CLLPADWriahmrqeV 73
Cdd:TIGR03269 279 IIKVRNVskryiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEW--------V 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 74 DTLDRlavdyvlDGDSRLREIQAALAVaeaaHDGSALARLHTELDN---ADGYT-----ADARARKLLAGLGFSSEQ--- 142
Cdd:TIGR03269 351 DMTKP-------GPDGRGRAKRYIGIL----HQEYDLYPHRTVLDNlteAIGLElpdelARMKAVITLKMVGFDEEKaee 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 143 -MERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKgypGTLVLISHDRDFLDAVVD 214
Cdd:TIGR03269 420 iLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAREEME---QTFIIVSHDMDFVLDVCD 496
|
250
....*....|
gi 15600445 215 HVVHLENRKL 224
Cdd:TIGR03269 497 RAALMRDGKI 506
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
324-510 |
5.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.67 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA------------IGYFAQ---HQL-- 385
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDITdkkvklsdirkkVGLVFQypeYQLfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 DSLDpqaspllhlQRIAPGEREQTLKD-----------FLGGFDFRGVRvDEPVLNFSGGEKARLALALIAWQKPNLLLL 454
Cdd:PRK13637 99 ETIE---------KDIAFGPINLGLSEeeienrvkramNIVGLDYEDYK-DKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 455 DEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVpFDG 510
Cdd:PRK13637 169 DEPTAGLDPKGRdeiLNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE-LQG 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
125-224 |
6.44e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.20 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD---LDAILWLEEWLKGYPGTLVL 201
Cdd:PRK10619 128 ARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVV 207
|
90 100
....*....|....*....|...
gi 15600445 202 ISHDRDFLDAVVDHVVHLENRKL 224
Cdd:PRK10619 208 VTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
321-506 |
6.59e-08 |
|
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: 53.77 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 321 GYGDK--AVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL-------AGDLpELGGRLLRGENLA-----IGYFAQHQL- 385
Cdd:cd03251 9 RYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRI-LIDGHDVRDYTLAslrrqIGLVSQDVFl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 386 --DSLdpqaspllhLQRIAPGEREQTLK------------DFL----GGFDfrgVRVDEPVLNFSGGEKARLALALIAWQ 447
Cdd:cd03251 88 fnDTV---------AENIAYGRPGATREeveeaaraanahEFImelpEGYD---TVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 448 KPNLLLLDEPTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLKStTDEFLLVADGRVV 506
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
143-223 |
6.94e-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: 53.38 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 143 MERRVGDFSGGWRM------RLNLAQALMCPSDLLLLDEPTNHLDLDAILW-----LEEWLKGYPGTLVLISHDRDFLDA 211
Cdd:cd03240 109 LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA 188
|
90
....*....|..
gi 15600445 212 vVDHVVHLENRK 223
Cdd:cd03240 189 -ADHIYRVEKDG 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-224 |
7.36e-08 |
|
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: 53.27 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWRIAHMRQEVDTLDRLAV----DYVLDGD 88
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaapPADRPVSMLFQENNLFAHLTVeqnvGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 89 SRLREIQAALAVaeaahdgSALARLhteldnadgytadararkllaGLGfssEQMERRVGDFSGGWRMRLNLAQALMCPS 168
Cdd:cd03298 99 LKLTAEDRQAIE-------VALARV---------------------GLA---GLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 169 DLLLLDEPTNHLD-------LDAILWLEEWLKgypGTLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:cd03298 148 PVLLLDEPFAALDpalraemLDLVLDLHAETK---MTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-181 |
7.89e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.56 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLlpadwriahmrqeVDTLDrla 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI-------------VDGLK--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 vdyVLDGDSRLREIQAALavaeaahdGSALARLH-----TELDN----------ADGYTADARARKLLAGLGFSsEQMER 145
Cdd:PRK09493 65 ---VNDPKVDERLIRQEA--------GMVFQQFYlfphlTALENvmfgplrvrgASKEEAEKQARELLAKVGLA-ERAHH 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600445 146 RVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK09493 133 YPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-218 |
8.28e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 13 PQRLLEA---AELTLHAGQKAGLIGANGAGKSSLFALL-------RGQLGQDAGDCLLPADWRIAHMRQEVD-------- 74
Cdd:PRK11308 24 PERLVKAldgVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYYQGQDLLKADPEAQKLLRQKIQivfqnpyg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 75 TLD-RLAVDYVLdgdsrlreiqaalavaeaahdGSALArLHTELDNADgytADARARKLLAGLGFSSEQMERRVGDFSGG 153
Cdd:PRK11308 104 SLNpRKKVGQIL---------------------EEPLL-INTSLSAAE---RREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 154 WRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLK-GYpgtlVLISHDRdfldAVVDHVVH 218
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDvsvqaqvLNLMMDLQQELGlSY----VFISHDL----SVVEHIAD 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-177 |
1.06e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRG----Q------LGQDAGD-----CLLPadwRI 66
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiQqgrvevLGGDMADarhrrAVCP---RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 67 AHMRQevdTLDR-----LAVDYVLDGDSRLReiqaalavaeaahdgsalarlhteldnadGYTADARARK---LLAGLGF 138
Cdd:NF033858 79 AYMPQ---GLGKnlyptLSVFENLDFFGRLF-----------------------------GQDAAERRRRideLLRATGL 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600445 139 SSEQmERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPT 177
Cdd:NF033858 127 APFA-DRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
328-531 |
1.09e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLR-GE--NLAIGYFAQHQLDSLDPqasplLHLQRIAPG 404
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRnGEvsVIAISAGLSGQLTGIEN-----IEFKMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 405 EREQTLKDFLGG---FDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEFSGA-- 479
Cdd:PRK13546 115 FKRKEIKAMTPKiieFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnk 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 480 -VLVVSHDRHLLKSTTDEFLLVADGRVVPFdGDLDD----YARWLVDYRAR-KAPQAE 531
Cdd:PRK13546 195 tIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDvlpkYEAFLNDFKKKsKAEQKE 251
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-224 |
1.13e-07 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 52.97 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLT----LQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwRIAHMRQEVDTL 76
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSG--------SVLVDGTDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 DRlavdyvldgdSRLREIQAA---------LAVAEAAHDGSALArlhTELDNADGYTADARARKLLAGLGFSsEQMERRV 147
Cdd:cd03258 73 SG----------KELRKARRRigmifqhfnLLSSRTVFENVALP---LEIAGVPKAEIEERVLELLELVGLE-DKADAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 148 GDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD---LDAILWLEEWLKGYPG-TLVLISHDRDFLDAVVDHVVHLENRK 223
Cdd:cd03258 139 AQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGE 218
|
.
gi 15600445 224 L 224
Cdd:cd03258 219 V 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
280-506 |
1.25e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.83 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 280 IKALERLEELAPAHVDSPFNFSfrESDKISRPLLDLGEGRLGYGDKA--VLEKVKLQLVPGARIGLLGPNGAGKSTLIKT 357
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTT--STAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 358 LAGD-LPELGGRLLRGENLAigYFAQHQLD---SLDPQASPLL------HLQRIAPGEREQTLKDFLGGFDFRGVRVDEP 427
Cdd:PRK11160 386 LTRAwDPQQGEILLNGQPIA--DYSEAALRqaiSVVSQRVHLFsatlrdNLLLAAPNASDEALIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 428 VLN---------FSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEM-RLALTMALQEFSG-AVLVVSHDRHLLKStTDE 496
Cdd:PRK11160 464 GLNawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQ-FDR 542
|
250
....*....|
gi 15600445 497 FLLVADGRVV 506
Cdd:PRK11160 543 ICVMDNGQII 552
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
323-506 |
1.29e-07 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 53.00 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENL-AIGYFAQHQLDSLDPQASPLLH--- 397
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGIDIrDISRKSLRSMIGVVLQDTFLFSgti 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 398 -----LQR-IAPGEREQTLKDFLGGFDF-----RGVR--VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE 464
Cdd:cd03254 94 menirLGRpNATDEEVIEAAKEAGAHDFimklpNGYDtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 465 MRLALTMALQEFSG--AVLVVSHdrHLlkSTT---DEFLLVADGRVV 506
Cdd:cd03254 174 TEKLIQEALEKLMKgrTSIIIAH--RL--STIknaDKILVLDDGKII 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-495 |
1.43e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLaGDLPELGGRLlRGENlAIGYFAQH------QLDSLDPQAS-- 393
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEV-RVEG-RVEFFNQNiyerrvNLNRLRRQVSmv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 -------PLLHLQRIAPGER--------------EQTLKDfLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLL 452
Cdd:PRK14258 94 hpkpnlfPMSVYDNVAYGVKivgwrpkleiddivESALKD-ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 453 LLDEPTNHLD-------------LEMRLALTMalqefsgavLVVSHDRHLLKSTTD 495
Cdd:PRK14258 173 LMDEPCFGLDpiasmkvesliqsLRLRSELTM---------VIVSHNLHQVSRLSD 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-205 |
1.52e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.83 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLleAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWRIAHMRQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalpPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 72 EVDTLDRLAV-DYV---LDGDSRLREIQAalavaeaahdgsalARLHteldnadgytaDARARKLLAGLGfsseqmERRV 147
Cdd:COG3840 79 ENNLFPHLTVaQNIglgLRPGLKLTAEQR--------------AQVE-----------QALERVGLAGLL------DRLP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 148 GDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD----LDAILWLEEWLKGYPGTLVLISHD 205
Cdd:COG3840 128 GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
1.52e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAG-----DCLLPADWRIAHMRQEV--- 73
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGkitvlGVPVPARARLARARIGVvpq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 74 -DTLDR-LAVDYVLDGDSRL-----REIQAALAVAEAahdgsaLARLHTELDNadgytadararkllaglgfsseqmerR 146
Cdd:PRK13536 122 fDNLDLeFTVRENLLVFGRYfgmstREIEAVIPSLLE------FARLESKADA--------------------------R 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600445 147 VGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDA--ILW 187
Cdd:PRK13536 170 VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIW 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
125-235 |
1.54e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLgfsseqmerRVGDF--------SGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLE 189
Cdd:PRK11124 118 ALARAEKLLERL---------RLKPYadrfplhlSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELA 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15600445 190 EwlkgyPG-TLVLISHDRDFLDAVVDHVVHLENRKLtLYRGGYSAFE 235
Cdd:PRK11124 189 E-----TGiTQVIVTHEVEVARKTASRVVYMENGHI-VEQGDASCFT 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
125-241 |
1.58e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEwlkgyPG 197
Cdd:COG4161 118 AREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvVEIIRELSQ-----TG 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15600445 198 -TLVLISHDRDFLDAVVDHVVHLENRKLTLYrGGYSAFERTRAER 241
Cdd:COG4161 192 iTQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
324-506 |
1.74e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA-IGYFAQHQLDSLDPQaSPLLH---- 397
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVPLVqYDHHYLHRQVALVGQ-EPVLFsgsv 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 398 LQRIAPG----EREQTLK--------DFLGGF-DFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE 464
Cdd:TIGR00958 572 RENIAYGltdtPDEEIMAaakaanahDFIMEFpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 465 MRLALTMALQEFSGAVLVVSHDRHLLKStTDEFLLVADGRVV 506
Cdd:TIGR00958 652 CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-205 |
1.80e-07 |
|
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: 52.30 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 27 GQKAGLIGANGAGKSSLFALLRGQLGQDAGD---------------CLLPADWRIAHMRQEVDTLDRLAV----DYVLDG 87
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvlfdsrkkiNLPPQQRKIGLVFQQYALFPHLNVrenlAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 88 DSRlREIQAalavaeaahdgsalarlhteldnadgytadaRARKLLAGLGFSSEQmERRVGDFSGGWRMRLNLAQALMCP 167
Cdd:cd03297 103 KRN-REDRI-------------------------------SVDELLDLLGLDHLL-NRYPAQLSGGEKQRVALARALAAQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 168 SDLLLLDEPTNHLD----LDAILWLEEWLKGYPGTLVLISHD 205
Cdd:cd03297 150 PELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHD 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
309-506 |
1.96e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDlPE---LGGR-LLRGEN---------- 374
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAykiLEGDiLFKGESildlepeera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 375 -----LAIGY----------------FAQHQLDSLDPQASPLLHLQRIAPgereqtlKDFLGGFD--FRGVRVDEpvlNF 431
Cdd:CHL00131 83 hlgifLAFQYpieipgvsnadflrlaYNSKRKFQGLPELDPLEFLEIINE-------KLKLVGMDpsFLSRNVNE---GF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 432 SGGEKAR---LALALIawqKPNLLLLDEPTNHLDLEMRLALTMALQEFSG---AVLVVSHDRHLLKSTTDEFLLV-ADGR 504
Cdd:CHL00131 153 SGGEKKRneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITHYQRLLDYIKPDYVHVmQNGK 229
|
..
gi 15600445 505 VV 506
Cdd:CHL00131 230 II 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-468 |
1.97e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLAIGYFAQHQ-------LDSLDPQASP 394
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARPDAGEVLWQGEPIRRQRDEYHQdllylghQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 LLHL---QRIAPGEREQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD------LEM 465
Cdd:PRK13538 92 LENLrfyQRLHGPGDDEALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvarLEA 170
|
...
gi 15600445 466 RLA 468
Cdd:PRK13538 171 LLA 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-219 |
2.18e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.42 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEV--DTLDR 78
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLylDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 79 LAVDYVLdgdsRLREiqaalaVAEAAHDGSALARLHTeldnadGYTADARARKLlaglgfsseqmerrvgdfSGGWRMRL 158
Cdd:PRK09544 84 LTVNRFL----RLRP------GTKKEDILPALKRVQA------GHLIDAPMQKL------------------SGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTL----VLISHDRDFLDAVVDHVVHL 219
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLCL 194
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-211 |
2.42e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQL--GQDAGDCLLPADwriaHMRQEVDTLDRL 79
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN----QFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 80 AvdyvldgdsrlreiqaalavaeaaHDGSALArlhteldnadgytadarARKLLAGLGFSSEQ-MERRVGDFSGGWRMRL 158
Cdd:COG2401 107 G------------------------RKGDFKD-----------------AVELLNAVGLSDAVlWLRRFKELSTGQKFRF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLD-----AILWLEEWLKGyPGTLVLISHDRDFLDA 211
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQtakrvARNLQKLARRA-GITLVVATHHYDVIDD 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
313-505 |
2.43e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 313 LDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGG--------RLLRGENLAIGYFAQH 383
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlEKPSEGSivvngqtiNLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 QLDSL---------------------DPQASPLLHLQRIAPGEREQTLKdFLG--GFDFRGvRVDEPVlNFSGGEKARLA 440
Cdd:PRK10619 86 QLRLLrtrltmvfqhfnlwshmtvleNVMEAPIQVLGLSKQEARERAVK-YLAkvGIDERA-QGKYPV-HLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 441 LALIAWQKPNLLLLDEPTNHLDLEM---RLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELvgeVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-219 |
2.68e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 52.26 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQlgqdagdcllpADWRIAHMRQEVDTLDRLAvdyvL 85
Cdd:TIGR01978 5 DLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-----------PSYEVTSGTILFKGQDLLE----L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 DGDSRLR-----------EIQAALAVAEAAhdgSAL-----ARLHTELDNADGYTadaRARKLLAGLGFSSEQMERRVGD 149
Cdd:TIGR01978 70 EPDERARaglflafqypeEIPGVSNLEFLR---SALnarrsARGEEPLDLLDFEK---LLKEKLALLDMDEEFLNRSVNE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 150 -FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY--PGT-LVLISHDRDFLDAVVDHVVHL 219
Cdd:TIGR01978 144 gFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLNYIKPDYVHV 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-222 |
3.26e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRgP--QRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRG--QLGQdaGDCLLPADWRIAHMRQEVdtl 76
Cdd:COG4178 362 ALALEDLTLRT-PdgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwPYGS--GRIARPAGARVLFLPQRP--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 drlavdYVLDGDsrLREiqaalavaeaahdgsALARLHTELDnadgyTADARARKLL--AGLGFSSEQMER-----RVgd 149
Cdd:COG4178 436 ------YLPLGT--LRE---------------ALLYPATAEA-----FSDAELREALeaVGLGHLAERLDEeadwdQV-- 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 150 FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKG-YPG-TLVLISHdRDFLDAVVDHVVHLENR 222
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
322-506 |
3.41e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.43 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEkVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQLDSLDPQASPLLHLQRI 401
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 402 APGErEQTLKDFLGGFDFRGVRVDE---------------------PVLNFSGGEKARLALALIAWQKPNLLLLDEPTNH 460
Cdd:PRK13643 96 QLFE-ETVLKDVAFGPQNFGIPKEKaekiaaeklemvgladefwekSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 461 LDLEMR---LALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13643 175 LDPKARiemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
150-221 |
3.54e-07 |
|
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: 50.68 E-value: 3.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 150 FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLD---AILWLEEWLKGYPGTLVLISHdRDFLDAVVDHVVHLEN 221
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEgerALNQAIAALKAAGATRIVIAH-RPETLASADRILVLED 170
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
325-506 |
3.74e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVlEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLL-RGENLA-------------IGYFAQHQLDSLDP 390
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLgmkddewravrsdIQMIFQDPLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 Q-------ASPLL----HLQRIAPGEREQTLKDFLGgfdfrgvrVDEPVLN-----FSGGEKARL--ALALIAwqKPNLL 452
Cdd:PRK15079 114 RmtigeiiAEPLRtyhpKLSRQEVKDRVKAMMLKVG--------LLPNLINrypheFSGGQCQRIgiARALIL--EPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 453 LLDEPTNHLDLEMR---LALTMALQEFSGAVLV-VSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK15079 184 ICDEPVSALDVSIQaqvVNLLQQLQREMGLSLIfIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
324-486 |
4.01e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.94 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLRGENL-----AIGYFAQH--------- 383
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpeagtiTVGGMVLSEETVwdvrrQVGMVFQNpdnqfvgat 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 -QLD---SLDPQASP-LLHLQRIAPGEREQTLKDFLGgfdfrgvrvDEPVlNFSGGEKARLALALIAWQKPNLLLLDEPT 458
Cdd:PRK13635 99 vQDDvafGLENIGVPrEEMVERVDQALRQVGMEDFLN---------REPH-RLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190
....*....|....*....|....*....|..
gi 15600445 459 NHLDLEMR---LALTMALQEFSGA-VLVVSHD 486
Cdd:PRK13635 169 SMLDPRGRrevLETVRQLKEQKGItVLSITHD 200
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
324-506 |
4.27e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--DLPElGGRLLRGENLAigyfaQHQLDSLDPQ---ASPLLHL 398
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfyDIDE-GEILLDGHDLR-----DYTLASLRNQvalVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 399 ------QRIAPG-----EREQTLK--------DFLG----GFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLD 455
Cdd:PRK11176 429 fndtiaNNIAYArteqySREQIEEaarmayamDFINkmdnGLD---TVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600445 456 EPTNHLDLEMRLALTMALQEFSG--AVLVVSHDRHLLKStTDEFLLVADGRVV 506
Cdd:PRK11176 506 EATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
323-509 |
4.81e-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: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAgdlpelggRLLRGEnlaigyfAQHQLDSLDpQASPLLHLQRIA 402
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL--------RLLSTE-------GEIQIDGVS-WNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 403 PGEREQTLKDFLGGF-----------DFRGVRVDEPV------------LNF---------SGGEKARLALALIAWQKPN 450
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFrknldpyeqwsDEEIWKVAEEVglksvieqfpdkLDFvlvdggyvlSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 451 LLLLDEPTNHLD-LEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFD 509
Cdd:TIGR01271 1374 ILLLDEPSAHLDpVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-505 |
4.94e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELG-----GRLLRGENL-----AIGYFAQHQLDS----- 387
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGqiiidGDLLTEENVwdirhKIGMVFQNPDNQfvgat 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 --------LDPQASPLLHLQriapgEREQTLKDFLGGFDFRgvrVDEPVlNFSGGEKARLALALIAWQKPNLLLLDEPTN 459
Cdd:PRK13650 99 veddvafgLENKGIPHEEMK-----ERVNEALELVGMQDFK---EREPA-RLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 460 HLDLEMRLALTMAL----QEFSGAVLVVSHDRHLLkSTTDEFLLVADGRV 505
Cdd:PRK13650 170 MLDPEGRLELIKTIkgirDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
322-506 |
5.17e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 51.29 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL------------AGDLPELGGRLLRGENLAIGYFAQH-----Q 384
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLIRQLRQHvgfvfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 385 LDSLDPQASPL-------LHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPvLNFSGGEKARLALALIAWQKPNLLLLDEP 457
Cdd:PRK11264 93 NFNLFPHRTVLeniiegpVIVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600445 458 TNHLDLEM---RLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11264 172 TSALDPELvgeVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
326-489 |
5.27e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.93 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 326 AVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-----------------DLPELGGRLLRGENlaIGYFAQHQLdsL 388
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGlddgssgevslvgqplhQMDEEARAKLRAKH--VGFVFQSFM--L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 DPQASPLLHLQRIA--PGERE-------QTLKDFLGgfdfRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTN 459
Cdd:PRK10584 100 IPTLNALENVELPAllRGESSrqsrngaKALLEQLG----LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|....
gi 15600445 460 HLDLEM--RLA-LTMAL-QEFSGAVLVVSHDRHL 489
Cdd:PRK10584 176 NLDRQTgdKIAdLLFSLnREHGTTLILVTHDLQL 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-508 |
5.40e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGdlpELGGRLLRGENLA------------IGYFAQHqlDSLDPQ 391
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGNNFTGTILAnnrkptkqilkrTGFVTQD--DILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 AS--------PLLHLQRIAPGEREQTLKD--------------FLGGFDFRGVrvdepvlnfSGGEKARLALALIAWQKP 449
Cdd:PLN03211 155 LTvretlvfcSLLRLPKSLTKQEKILVAEsviselgltkcentIIGNSFIRGI---------SGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 450 NLLLLDEPTNHLD--LEMRLALTMALQEFSGAVLVVShdRHLLKSTT----DEFLLVADGRVVPF 508
Cdd:PLN03211 226 SLLILDEPTSGLDatAAYRLVLTLGSLAQKGKTIVTS--MHQPSSRVyqmfDSVLVLSEGRCLFF 288
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
5.67e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAG------------DCLLPADWRIAH 68
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinninynklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 69 MRQEVDTLDRLAVDYVLdgdsrlreiqaalavaeaaHDGSALARLHTELDNADGYTADARARKLLAGLGFSSEqMERRVG 148
Cdd:PRK09700 85 IYQELSVIDELTVLENL-------------------YIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 149 DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHL---DLDAILWLEEWLKGYPGTLVLISH 204
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
6.34e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.16 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---PADWR---IAHMRQEVD 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgkPLDYSkrgLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 75 TLDRlavdyvlDGDSRLreiqaalavaeaahdgsalarLHTELDNADGYTadararklLAGLGFSSEQMERRVGD----- 149
Cdd:PRK13638 81 TVFQ-------DPEQQI---------------------FYTDIDSDIAFS--------LRNLGVPEAEITRRVDEaltlv 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 150 ------------FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD------LDAILwleEWLKGYPGTLVLISHDRDFLDA 211
Cdd:PRK13638 125 daqhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqMIAII---RRIVAQGNHVIISSHDIDLIYE 201
|
250 260
....*....|....*....|....*...
gi 15600445 212 VVDHVVHLENRKLTLYRGGYSAFERTRA 239
Cdd:PRK13638 202 ISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
327-458 |
7.54e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.94 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLP------ELGGRLLR---------------------------GE 373
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQpdsgeiLLDGEPVRfrsprdaqaagiaiihqelnlvpnlsvAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 374 NLAIGYFaqhqldsldPQASPLLHLQRIapgeREQTlKDFLGGFDFRgVRVDEPVLNFSGGEK-----ARlALAliawQK 448
Cdd:COG1129 99 NIFLGRE---------PRRGGLIDWRAM----RRRA-RELLARLGLD-IDPDTPVGDLSVAQQqlveiAR-ALS----RD 158
|
170
....*....|
gi 15600445 449 PNLLLLDEPT 458
Cdd:COG1129 159 ARVLILDEPT 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-181 |
8.51e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQRLLEAAELTLHAGQKAGLIGANGAGKSSL-FALLRgqlgqdagdcLLPADWRIAHMRQEVDTLDRLAVDYVLdgdsr 90
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLR----------LINSQGEIWFDGQPLHNLNRRQLLPVR----- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 91 lREIQAALAVaeaahDGSAL-ARLHTELDNADGYTA----------DARARKLLAGLGFSSEQMERRVGDFSGGWRMRLN 159
Cdd:PRK15134 362 -HRIQVVFQD-----PNSSLnPRLNVLQIIEEGLRVhqptlsaaqrEQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIA 435
|
170 180
....*....|....*....|..
gi 15600445 160 LAQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLD 457
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
8.94e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.88 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwriahMRQEVDTLDRLA 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW--------DGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VDYV-----LDGDSRLREiQAAlavaeaahdgsALARLHTeLDNADgytADARARKLLAGLGFsSEQMERRVGDFSGGWR 155
Cdd:COG4152 73 IGYLpeergLYPKMKVGE-QLV-----------YLARLKG-LSKAE---AKRRADEWLERLGL-GDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 156 MRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY--PGTLVLIS-HDRDFLDAVVDHVV 217
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFSsHQMELVEELCDRIV 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
308-458 |
9.04e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 308 ISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGD-------------------------- 361
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpratsgrivfdgkditdwqtakimre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 362 ----LPE---LGGRLLRGENLAI-GYFAQHQldsldpqasplLHLQRIapgerEQTLKDFLGGFDFRGVRVDepvlNFSG 433
Cdd:PRK11614 81 avaiVPEgrrVFSRMTVEENLAMgGFFAERD-----------QFQERI-----KWVYELFPRLHERRIQRAG----TMSG 140
|
170 180
....*....|....*....|....*
gi 15600445 434 GEKARLALALIAWQKPNLLLLDEPT 458
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-505 |
9.16e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 15 RLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDcLLPADWRIAHMR-------------QEVDTLDRLAV 81
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT-LEIGGNPCARLTpakahqlgiylvpQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 -DYVLDGDSRLREIQAALAVAeaahdgsaLARLHTELDnadgytADARArkllAGLGFSSEQMerrvgdfsggwrmrLNL 160
Cdd:PRK15439 104 kENILFGLPKRQASMQKMKQL--------LAALGCQLD------LDSSA----GSLEVADRQI--------------VEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 161 AQALMCPSDLLLLDEPTNHL---DLDAIL-WLEEWLKGYPGtLVLISHDRDFLDAVVDHVvhlenrklTLYRGGYSAFER 236
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLtpaETERLFsRIRELLAQGVG-IVFISHKLPEIRQLADRI--------SVMRDGTIALSG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 237 TRAErlaqqqqayekqqAQRAHMESFIARfKAKATKARQAQSRIKALerleelaPAHvdspfnfsfRESDKISRPLLDL- 315
Cdd:PRK15439 223 KTAD-------------LSTDDIIQAITP-AAREKSLSASQKLWLEL-------PGN---------RRQQAAGAPVLTVe 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 316 ---GEGrlgygdkavLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAIGYFAQHQLD------ 386
Cdd:PRK15439 273 dltGEG---------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvyl 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 387 SLDPQAS-------------PLLHLQR---IAPGEREQTLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPN 450
Cdd:PRK15439 344 PEDRQSSglyldaplawnvcALTHNRRgfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQ 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 451 LLLLDEPTNHLDLEMR-----LALTMALQEFsgAVLVVSHDRHLLKSTTDEFLLVADGRV 505
Cdd:PRK15439 424 LLIVDEPTRGVDVSARndiyqLIRSIAAQNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-509 |
9.61e-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: 50.62 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAgdlpelggRLLRGEnlaigyfAQHQLDSLDPQASPlLHLQRIA 402
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL--------RLLNTE-------GDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 403 PGEREQTLKDFLGGF----DFRGVRVDEPV-------------------LNF---------SGGEKARLALALIAWQKPN 450
Cdd:cd03289 79 FGVIPQKVFIFSGTFrknlDPYGKWSDEEIwkvaeevglksvieqfpgqLDFvlvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 451 LLLLDEPTNHLDLEMRLALTMAL-QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVPFD 509
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
430-511 |
9.98e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.86 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 430 NFSGGEKARLALALIAWQKPNLLLLDEPTNHLD----LEMrLALTMALQEFSGAVLVVSHD-RHLLKsTTDEFLLVADGR 504
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEI-LEIFDNLNKQGKTIILVTHDlDNVLE-WTKRTIFFKDGK 242
|
....*..
gi 15600445 505 VVpFDGD 511
Cdd:PRK13651 243 II-KDGD 248
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-504 |
1.03e-06 |
|
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: 49.78 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENlaIGYFAQhqldsldpqaSPLLhlqriapgeR 406
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQ----------EPWI---------Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 407 EQTLKD-FLGGFDFRGVRVDEPV------------------------LNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:cd03250 79 NGTIREnILFGKPFDEERYEKVIkacalepdleilpdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 462 DLE-----MRLALTMALQEfSGAVLVVSHDRHLLKStTDEFLLVADGR 504
Cdd:cd03250 159 DAHvgrhiFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-181 |
1.31e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGD--------CLLPADWR----IAHMRQEV 73
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddediSLLPLHARarrgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 74 DTLDRLAvdyVLDGDSRLREIQaalavaeaaHDGSALARlhteldnadgytaDARARKLLAglGFSSEQMERRVGD-FSG 152
Cdd:PRK10895 88 SIFRRLS---VYDNLMAVLQIR---------DDLSAEQR-------------EDRANELME--EFHIEHLRDSMGQsLSG 140
|
170 180
....*....|....*....|....*....
gi 15600445 153 GWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK10895 141 GERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
561-622 |
1.46e-06 |
|
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: 45.92 E-value: 1.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 561 KREADKLERELGGLHEKLAAIEARLGDSALYdvSRKDELRELLSEQSSLKVREGELEERWLE 622
Cdd:pfam16326 7 QRELEELEAEIEKLEEEIAELEAQLADPELY--SDYEKLQELSAELEELEAELEELYERWEE 66
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-462 |
1.62e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.04 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL------------AGDLpelggrLLRGENLaigyfaqhqldsLD 389
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarvEGEI------LLDGEDI------------YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 390 PQASPLLHLQRIA-----P------------------GER---------EQTL---------KDflggfdfrgvRVDEPV 428
Cdd:COG1117 83 PDVDVVELRRRVGmvfqkPnpfpksiydnvayglrlhGIKskseldeivEESLrkaalwdevKD----------RLKKSA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600445 429 LNFSGGEKARL----ALALiawqKPNLLLLDEPTNHLD 462
Cdd:COG1117 153 LGLSGGQQQRLciarALAV----EPEVLLMDEPTSALD 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
309-543 |
1.67e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRPLLDLGEGRLGY----GDKAVLEKVKLQLVPGARIGLLGPNGAGKST-------LIKT-----LAGDL---------- 362
Cdd:PRK15134 2 TQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSppvvyPSGDIrfhgesllha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 363 PELGGRLLRGENLAIGYfaQHQLDSLDP------QASPLLHLQRIApgEREQTLKDFLGGFDFRGVRVDEPVLN-----F 431
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIF--QEPMVSLNPlhtlekQLYEVLSLHRGM--RREAARGEILNCLDRVGIRQAAKRLTdyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 432 SGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMAL-QEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVVP 507
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqiLQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15600445 508 -------FDGDLDDYARWLVDYRARKAPQAETAPGAPTERTDK 543
Cdd:PRK15134 238 qnraatlFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQ 280
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
271-462 |
1.69e-06 |
|
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: 51.48 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 271 TKARQAQSRIKALERLEELAPahvdspfnfsfresDKISRPLLDLGEGR----------LGYGDKAVLEKVKLQLVPGAR 340
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELEP--------------DSIERRTIKPGEGNsitvhnatftWARDLPPTLNGITFSIPEGAL 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 341 IGLLGPNGAGKSTLIKTLAGDLPELGGRL-LRGenlAIGYFAQH---QLDSLDPQaspLLHLQRIAPGEREQTLK----- 411
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVhMKG---SVAYVPQQawiQNDSLREN---ILFGKALNEKYYQQVLEacall 740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600445 412 ---DFLGGFDfrGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLD 462
Cdd:TIGR00957 741 pdlEILPSGD--RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-242 |
1.79e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.01 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpADWRIAHMRQEVDTLDRLA 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS-----AGSHIELLGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 vdyvldgdsrlREIQAALAVAEAAHDGSALARLHTELDNAdgytadararkLLAGLG-----------FSSEQMER---- 145
Cdd:PRK09984 79 -----------RDIRKSRANTGYIFQQFNLVNRLSVLENV-----------LIGALGstpfwrtcfswFTREQKQRalqa 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 146 ------------RVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG----TLVLISHDRDFL 209
Cdd:PRK09984 137 ltrvgmvhfahqRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYA 216
|
250 260 270
....*....|....*....|....*....|...
gi 15600445 210 DAVVDHVVHLENRKLtLYRGGYSAFERTRAERL 242
Cdd:PRK09984 217 LRYCERIVALRQGHV-FYDGSSQQFDNERFDHL 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-181 |
1.85e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDclLPADWRIAHMRQEVDTLDRLAVDYVLdgdsrlreiqa 96
Cdd:PRK13409 355 LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKISYKPQYIKPDYDGTVEDLL----------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 97 alavaeaahdGSALARLHTELDNADgytadararkLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEP 176
Cdd:PRK13409 422 ----------RSITDDLGSSYYKSE----------IIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
....*
gi 15600445 177 TNHLD 181
Cdd:PRK13409 481 SAHLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-181 |
2.21e-06 |
|
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: 50.55 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDclLPADWRIAHMRQEVDTLDRLAVDYVLDGDSrlreiqa 96
Cdd:COG1245 356 LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQYISPDYDGTVEEFLRSAN------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 97 alavaEAAHDGSalaRLHTELdnadgytadarARKLlaGLgfsSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEP 176
Cdd:COG1245 427 -----TDDFGSS---YYKTEI-----------IKPL--GL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
....*
gi 15600445 177 TNHLD 181
Cdd:COG1245 483 SAHLD 487
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
325-517 |
2.34e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLAigYFAQH----------QLDSLDPQASP 394
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIA--YVPQQawimnatvrgNILFFDEEDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 LLHlQRIAPGEREQTLKDFLGGFDfrgVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEM--RLALTMA 472
Cdd:PTZ00243 751 RLA-DAVRVSQLEADLAQLGGGLE---TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRVVEECF 826
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 473 LQEFSGAVLVV-SHDRHLLkSTTDEFLLVADGRVVpFDGDLDDYAR 517
Cdd:PTZ00243 827 LGALAGKTRVLaTHQVHVV-PRADYVVALGDGRVE-FSGSSADFMR 870
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-229 |
2.35e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 23 TLHAGQKAGLIGANGAGKS-SLFALL-----RGQLGQDA---GDCLLPADWR-IAHMRQE------VDTLDRLAvDYVLD 86
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqTAFALMgllaaNGRIGGSAtfnGREILNLPEKeLNKLRAEqismifQDPMTSLN-PYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 87 GDsRLREIqaalavaeaahdgsalARLHTELDNADGYTADAR---------ARKllaglgfsseQMERRVGDFSGGWRMR 157
Cdd:PRK09473 117 GE-QLMEV----------------LMLHKGMSKAEAFEESVRmldavkmpeARK----------RMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 158 LNLAQALMCPSDLLLLDEPTNHLDLDA---ILWLEEWLKGYPGT-LVLISHDRDFLDAVVDHVvhlenrkLTLYRG 229
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTaIIMITHDLGVVAGICDKV-------LVMYAG 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-181 |
2.55e-06 |
|
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: 48.81 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 15 RLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDA---GDCLL------PADW--RIAHMRQEVDTLDRLAVDY 83
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFngqprkPDQFqkCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 84 VL--DGDSRLREIQAALAVAEAAHDgSALARLhteldnadgytADARARkllaglgfsseqmERRVGDFSGGWRMRLNLA 161
Cdd:cd03234 101 TLtyTAILRLPRKSSDAIRKKRVED-VLLRDL-----------ALTRIG-------------GNLVKGISGGERRRVSIA 155
|
170 180
....*....|....*....|
gi 15600445 162 QALMCPSDLLLLDEPTNHLD 181
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-227 |
2.88e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 48.68 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwriahmrqEVDTLDR----LAVDYVLDGDSRLRE-IQA 96
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG---------------TVTVRGRvsslLGLGGGFNPELTGREnIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 97 alavaeaahdgsaLARLHteldnadGYTADARARKL-----LAGLGfssEQMERRVGDFSGGWRMRLNLAQALMCPSDLL 171
Cdd:cd03220 108 -------------NGRLL-------GLSRKEIDEKIdeiieFSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 172 LLDEPT----NHLDLDAILWLEEWLKGyPGTLVLISHDRDFLDAVVDHVVHLENRKLTLY 227
Cdd:cd03220 165 LIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
324-464 |
3.03e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 324 DKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLAIGYFAQH-----QLDSLDPQASPL-- 395
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATRGDRSRFmaylgHLPGLKADLSTLen 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 396 LHLQRIAPGER-EQTLKDFLGGFDFRGvRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE 464
Cdd:PRK13543 103 LHFLCGLHGRRaKQMPGSALAIVGLAG-YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-204 |
3.05e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 50.16 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALL-------RGQL---GQDAGDcLLPADWR--IAHMRQEVdtldrlavdYVLDGDs 89
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLlrfydptSGRIlidGVDIRD-LTLESLRrqIGVVPQDT---------FLFSGT- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 90 rLRE-IqaalavaeaahdgsALARLH---TELDNAdgyTADARARKLLAGLgfsSEQMERRVGD----FSGGWRMRLNLA 161
Cdd:COG1132 430 -IREnI--------------RYGRPDatdEEVEEA---AKAAQAHEFIEAL---PDGYDTVVGErgvnLSGGQRQRIAIA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 162 QALMCPSDLLLLDEPTNHLD-------LDAilwLEEWLKGYpgTLVLISH 204
Cdd:COG1132 489 RALLKDPPILILDEATSALDtetealiQEA---LERLMKGR--TTIVIAH 533
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
431-506 |
3.35e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 431 FSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQaqvLNLMMDLQqELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-181 |
3.37e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.93 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGP-----QRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwRIAHMRQEVdt 75
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSG--------SILIDGKDV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 76 ldrlavdyvldgdSRLREIQAALAVAEAAHD---GSAlARLhTELDN---AD----------GYTADARA--RKLLAGLG 137
Cdd:COG1101 71 -------------TKLPEYKRAKYIGRVFQDpmmGTA-PSM-TIEENlalAYrrgkrrglrrGLTKKRRElfRELLATLG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 138 FSSE-QMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:COG1101 136 LGLEnRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-185 |
3.49e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 7 LTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwriahmRQEVDTLDRLAVDyvld 86
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESG-------------QIQIDGKTATRGD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 87 gdsRLREIQAALAVAEAAHDGSALARLHTeLDNADGYTADARARKLLAGLGFSSEQmERRVGDFSGGWRMRLNLAQALMC 166
Cdd:PRK13543 80 ---RSRFMAYLGHLPGLKADLSTLENLHF-LCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLS 154
|
170
....*....|....*....
gi 15600445 167 PSDLLLLDEPTNHLDLDAI 185
Cdd:PRK13543 155 PAPLWLLDEPYANLDLEGI 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-224 |
3.82e-06 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 48.17 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRL-LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEVDTLDRLA 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV-NGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VDYVLDgDSRLreiqaalAVAEAAHDGSALArlhTELDNADGYTADARARKLLAGLGFSSEQMERRVGdFSGGWRMRLNL 160
Cdd:cd03292 80 IGVVFQ-DFRL-------LPDRNVYENVAFA---LEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 161 AQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY--PGTLVLIS-HDRDFLDAVVDHVVHLENRKL 224
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-506 |
3.91e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENL-AIG----YFAQHQLDSL-------- 388
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIaPDHGEILFDGENIpAMSrsrlYTVRKRMSMLfqsgalft 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 389 -----DPQASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVlNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:PRK11831 98 dmnvfDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPS-ELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 464 EMRLALTMALQEFSGAV----LVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK11831 177 ITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-204 |
3.94e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.82 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP----ADWRIAHMRQEV-----------DTL 76
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNgqpiADYSEAALRQAIsvvsqrvhlfsATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 -DRLAVDYVLDGDSRLREIqaalavaeaahdgsaLAR--LHTELDNADGytadararkLLAGLGFSSEQMerrvgdfSGG 153
Cdd:PRK11160 431 rDNLLLAAPNASDEALIEV---------------LQQvgLEKLLEDDKG---------LNAWLGEGGRQL-------SGG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 154 WRMRLNLAQALMCPSDLLLLDEPTNHLDLDA---IL-WLEEWLKGypGTLVLISH 204
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILeLLAEHAQN--KTVLMITH 532
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
112-506 |
3.95e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 112 RLHTELDNADgytADARARKLLAGLGFSSEQM--ERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLD---AIL 186
Cdd:PRK10261 132 RLHQGASREE---AMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQIL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 187 WLEEWL-KGYPGTLVLISHDRDFLDAVVDHVvhlenrkLTLYRGgySAFERTRAERLaqqqqayeKQQAQRAHMESFIAR 265
Cdd:PRK10261 209 QLIKVLqKEMSMGVIFITHDMGVVAEIADRV-------LVMYQG--EAVETGSVEQI--------FHAPQHPYTRALLAA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 266 FKAKATKARQAQSRIKALERLEELAPAHVDSpfnfsfrESDKI--SRPLLD---------LGEGRLGYGDKAV--LEKVK 332
Cdd:PRK10261 272 VPQLGAMKGLDYPRRFPLISLEHPAKQEPPI-------EQDTVvdGEPILQvrnlvtrfpLRSGLLNRVTREVhaVEKVS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 333 LQLVPGARIGLLGPNGAGKST-------LIKTLAGDLPELGGRL-------LRGENLAIGYFAQHQLDSLDPQAS----- 393
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTtgrallrLVESQGGEIIFNGQRIdtlspgkLQALRRDIQFIFQDPYASLDPRQTvgdsi 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 --PL-LH--LQRIAPGEREQTLKDFLGGFDFRGVRVDEpvlNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR-- 466
Cdd:PRK10261 425 mePLrVHglLPGKAAAARVAWLLERVGLLPEHAWRYPH---EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRgq 501
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15600445 467 -LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK10261 502 iINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
330-509 |
4.16e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 330 KVKLQLvPGARI-GLLGPNGAGKSTLIKTLAG-DLPE-----LGGRLL----RGENLA-----IGYFAQhqlDS-LDPQA 392
Cdd:PRK11144 16 TVNLTL-PAQGItAIFGRSGAGKTSLINAISGlTRPQkgrivLNGRVLfdaeKGICLPpekrrIGYVFQ---DArLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPLLHLQR-IAPGEREQTLK--DFLGgfdfrgvrvDEPVLN-----FSGGEKARLAL--ALIAwqKPNLLLLDEPTNHLD 462
Cdd:PRK11144 92 KVRGNLRYgMAKSMVAQFDKivALLG---------IEPLLDrypgsLSGGEKQRVAIgrALLT--APELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 463 LEMRLALTMALQEFSGAV----LVVSHdrhllksTTDEFLLVAD-------GRVVPFD 509
Cdd:PRK11144 161 LPRKRELLPYLERLAREInipiLYVSH-------SLDEILRLADrvvvleqGKVKAFG 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
112-216 |
5.08e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 48.90 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 112 RLHTELDNADgytADARARKLLAGLGFSSEqmERRVGD----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD------ 181
Cdd:COG0444 114 RIHGGLSKAE---ARERAIELLERVGLPDP--ERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaq 188
|
90 100 110
....*....|....*....|....*....|....*.
gi 15600445 182 -LDAILWLEEWLKgypGTLVLISHDrdfLdAVVDHV 216
Cdd:COG0444 189 iLNLLKDLQRELG---LAILFITHD---L-GVVAEI 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
322-458 |
5.59e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLA-------GDLPELGG----RLLR--------------GENL- 375
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarkiqqGRVEVLGGdmadARHRravcpriaympqglGKNLy 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 376 -------AIGYFAqhQLDSLDPQaspllhlqriapgEREQTLKDFL---GGFDFRgvrvDEPVLNFSGGEKARLAL--AL 443
Cdd:NF033858 91 ptlsvfeNLDFFG--RLFGQDAA-------------ERRRRIDELLratGLAPFA----DRPAGKLSGGMKQKLGLccAL 151
|
170
....*....|....*
gi 15600445 444 IawQKPNLLLLDEPT 458
Cdd:NF033858 152 I--HDPDLLILDEPT 164
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-204 |
6.84e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.49 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLlpadWR---IAHMRQEV--DT 75
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL----WQgepIRRQRDEYhqDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 76 L---DRLAVDYVLDGDSRLReiqaalavaeaahdgsALARLHTELDNADgyTADARARKLLAGlgfsseQMERRVGDFSG 152
Cdd:PRK13538 77 LylgHQPGIKTELTALENLR----------------FYQRLHGPGDDEA--LWEALAQVGLAG------FEDVPVRQLSA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 153 GWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWL-----KGypGTLVLISH 204
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhaeQG--GMVILTTH 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
325-513 |
7.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 48.26 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 325 KAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-----DLPE----LGGRLLRGENL-----AIGYFAQHQLDS--- 387
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPNskitVDGITLTAKTVwdireKVGIVFQNPDNQfvg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 ----------LDPQASPLLHLQRIApgerEQTLKDfLGGFDFRGvrvDEPVlNFSGGEKARLALALIAWQKPNLLLLDEP 457
Cdd:PRK13640 100 atvgddvafgLENRAVPRPEMIKIV----RDVLAD-VGMLDYID---SEPA-NLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 458 TNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHlLKSTTDEFLLVADGRVVPFDGDLD 513
Cdd:PRK13640 171 TSMLDPAGKeqiLKLIRKLKKKNNlTVISITHDID-EANMADQVLVLDDGKLLAQGSPVE 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
328-506 |
7.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPE------LGGRLLRGENL-----AIGYFAQHQLD-----SLDPQ 391
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfegkvkIDGELLTAENVwnlrrKIGMVFQNPDNqfvgaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 392 ASPLLHLQRIAPGEREQTLKDFLGGFDFRGVRVDEPVlNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALTM 471
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPA-RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600445 472 ALQE----FSGAVLVVSHDRHlLKSTTDEFLLVADGRVV 506
Cdd:PRK13642 182 VIHEikekYQLTVLSITHDLD-EAASSDRILVMKAGEII 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-226 |
7.88e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.75 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqLGQDAGDCLLPADWRIAHMRQEVdtldRLAVDyvl 85
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTAPLAEAREDT----RLMFQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 dgDSRLREIQaalavaeaahdgsalarlhTELDNAD-GYTAD--ARARKLLAGLGFSSeqmerRVGDF----SGGWRMRL 158
Cdd:PRK11247 89 --DARLLPWK-------------------KVIDNVGlGLKGQwrDAALQALAAVGLAD-----RANEWpaalSGGQKQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLD---------LDAILWLEEwlkGYpgTLVLISHDRDFLDAVVDHVVHLENRKLTL 226
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDaltriemqdLIESLWQQH---GF--TVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
304-504 |
8.88e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 304 ESDKISRPLLDLGEGRLGY----GDKAVLEKVKLQLVPGARIGLLGPNGAGKS----TLIKTLAGD-------------- 361
Cdd:PRK09473 4 LAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANgriggsatfngrei 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 362 --LPELGGRLLRGENLAIGYfaQHQLDSLDP------QASPLLHLQRiapGEREQTlkdflgGFDfRGVRVDEPVL---- 429
Cdd:PRK09473 84 lnLPEKELNKLRAEQISMIF--QDPMTSLNPymrvgeQLMEVLMLHK---GMSKAE------AFE-ESVRMLDAVKmpea 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 430 ---------NFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRlALTMAL-----QEFSGAVLVVSHDRHLLKSTTD 495
Cdd:PRK09473 152 rkrmkmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ-AQIMTLlnelkREFNTAIIMITHDLGVVAGICD 230
|
....*....
gi 15600445 496 EFLLVADGR 504
Cdd:PRK09473 231 KVLVMYAGR 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
337-506 |
9.29e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 337 PGARIGLLGPNGAGKSTLIKTL--AGDlPELGGRLLRGENL----------AIGYFAQHQL-------DSL---DPQASp 394
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLqrVFD-PQSGRILIDGTDIrtvtraslrrNIAVVFQDAGlfnrsieDNIrvgRPDAT- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 395 llHLQRIAPGEREQTLkDFL----GGFDFRgvrVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMRLALT 470
Cdd:PRK13657 438 --DEEMRAAAERAQAH-DFIerkpDGYDTV---VGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVK 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600445 471 MALQEfsgavlvVSHDR------HLLkST---TDEFLLVADGRVV 506
Cdd:PRK13657 512 AALDE-------LMKGRttfiiaHRL-STvrnADRILVFDNGRVV 548
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
111-218 |
1.03e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.37 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 111 ARLHTELDNADgytADARARKLLAGLGFSSEQMERRV-GDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLE 189
Cdd:COG0396 104 ARRGEELSARE---FLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVA 180
|
90 100 110
....*....|....*....|....*....|..
gi 15600445 190 E---WLKGYPGTLVLISHDRDFLDAVVDHVVH 218
Cdd:COG0396 181 EgvnKLRSPDRGILIITHYQRILDYIKPDFVH 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
327-506 |
1.06e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 47.15 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTL-------AG-------DLPELGGRLLRGEnlaIGYFAQhqldslDPQA 392
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGeilldgvDIRDLNLRWLRSQ---IGLVSQ------EPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 393 SPLLHLQRIAPGEREQTLK------------DFL----GGFD----FRGVRVdepvlnfSGGEKARLALALIAWQKPNLL 452
Cdd:cd03249 89 FDGTIAENIRYGKPDATDEeveeaakkanihDFImslpDGYDtlvgERGSQL-------SGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 453 LLDEPTNHLDLEMRLALTMALQEFSGA--VLVVSHdrHLlkSTT---DEFLLVADGRVV 506
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH--RL--STIrnaDLIAVLQNGQVV 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-219 |
1.16e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 3 RLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAdwriahmrQEVDTLDRLAVd 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA--------QPLESWSSKAF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 83 yvldgdsrLREIqaalavaeaahdgsalARLHTELDNADGYTadarARKLLA--------GLG-FSSEQME--------- 144
Cdd:PRK10575 84 --------ARKV----------------AYLPQQLPAAEGMT----VRELVAigrypwhgALGrFGAADREkveeaislv 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 145 -------RRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLD---AILWLEEWLKGYPG-TLVLISHDRDFLDAVV 213
Cdd:PRK10575 136 glkplahRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYC 215
|
....*.
gi 15600445 214 DHVVHL 219
Cdd:PRK10575 216 DYLVAL 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-217 |
1.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 21 ELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL--------PADWRIAHMRQEVDTLDRLAVDYVLDgDSRLR 92
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditithkTKDKYIRPVRKRIGMVFQFPESQLFE-DTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 93 EIQAALAvaeaahdgsalaRLHTELDNADgytadARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLL 172
Cdd:PRK13646 106 EIIFGPK------------NFKMNLDEVK-----NYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 173 LDEPTNHLDLDAILWLEEWLKGYP----GTLVLISHDRDFLDAVVDHVV 217
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVI 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
345-501 |
1.29e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 345 GPNGAGKSTLIK----TLAGDLP----------------------ELGGRLLRGENL-AIGYFAQ-------HQLDSldp 390
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPpnskggahdpkliregevraqvKLAFENANGKKYtITRSLAIlenvifcHQGES--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 qASPLLhlqriapgereqtlkdflggfdfrgvrvdEPVLNFSGGEKA------RLALALIAWQKPNLLLLDEPTNHLD-- 462
Cdd:cd03240 106 -NWPLL-----------------------------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDee 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 463 -LEMRLA--LTMALQEFSGAVLVVSHDRHLLKStTDEFLLVA 501
Cdd:cd03240 156 nIEESLAeiIEERKSQKNFQLIVITHDEELVDA-ADHIYRVE 196
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
293-522 |
1.43e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 293 HVDSPFNFSFRESDKISRPLLDLGEGRLGYGdkavLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLR 371
Cdd:PRK13545 9 HVTKKYKMYNKPFDKLKDLFFRSKDGEYHYA----LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGvTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 372 GEN--LAIGYFAQHQLDSLDPqasplLHLQRIAPGEREQTLKDFLGG-FDFR--GVRVDEPVLNFSGGEKARLALALIAW 446
Cdd:PRK13545 85 GSAalIAISSGLNGQLTGIEN-----IELKGLMMGLTKEKIKEIIPEiIEFAdiGKFIYQPVKTYSSGMKSRLGFAISVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 447 QKPNLLLLDEPTNHLDLEMRLALTMALQEFS---GAVLVVSHDRHLLKSTTDEFLLVADGRVVPFdGDL----DDYARWL 519
Cdd:PRK13545 160 INPDILVIDEALSVGDQTFTKKCLDKMNEFKeqgKTIFFISHSLSQVKSFCTKALWLHYGQVKEY-GDIkevvDHYDEFL 238
|
...
gi 15600445 520 VDY 522
Cdd:PRK13545 239 KKY 241
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
309-504 |
1.54e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 309 SRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG-----------DLPELGG---------- 367
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptggtillRGQHIEGlpghqiarmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 368 --------RLLRG----ENLAIgyfAQHQldsldPQASPLLHLQRIAPG---------EREQTLKDFLGGFDFrgvrVDE 426
Cdd:PRK11300 82 vvrtfqhvRLFREmtviENLLV---AQHQ-----QLKTGLFSGLLKTPAfrraesealDRAATWLERVGLLEH----ANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 427 PVLNFSGGEKARLALALIAWQKPNLLLLDEPT-----------NHLDLEMRlaltmalQEFSGAVLVVSHDRHLLKSTTD 495
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglnpketkelDELIAELR-------NEHNVTVLLIEHDMKLVMGISD 222
|
....*....
gi 15600445 496 EFLLVADGR 504
Cdd:PRK11300 223 RIYVVNQGT 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-205 |
1.78e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 16 LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAdwriahmrQEVDTLDRLAvdyvlDGDSRLREIQ 95
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG--------QPMSKLSSAA-----KAELRNQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 96 AALAVAEAAHDGSALARLHTEL--DNADGYTADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLL 173
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLliGKKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600445 174 DEPTNHLDL---DAILWLEEWLKGYPGTLVL-ISHD 205
Cdd:PRK11629 170 DEPTGNLDArnaDSIFQLLGELNRLQGTAFLvVTHD 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-181 |
2.04e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.39 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 11 RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAG----------------------DCLLPadWRiah 68
Cdd:COG4525 17 GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGeitldgvpvtgpgadrgvvfqkDALLP--WL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 69 mrqevDTLDRLAVDYvldgdsRLReiqaalavaeaahdGSALARLHteldnadgytadARARKLLAGLGFSsEQMERRVG 148
Cdd:COG4525 92 -----NVLDNVAFGL------RLR--------------GVPKAERR------------ARAEELLALVGLA-DFARRRIW 133
|
170 180 190
....*....|....*....|....*....|...
gi 15600445 149 DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:COG4525 134 QLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-462 |
2.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.37 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLaGDLPEL-------GGRLLRGENL------------AIGY 379
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF-NRLLELneearveGEVRLFGRNIyspdvdpievrrEVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 380 FAQHqldsldpqASPLLHL---QRIAPGEREQTLKDFLGGFDFR--------------GVRVDEPVLNFSGGEKARLALA 442
Cdd:PRK14267 90 VFQY--------PNPFPHLtiyDNVAIGVKLNGLVKSKKELDERvewalkkaalwdevKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180
....*....|....*....|
gi 15600445 443 LIAWQKPNLLLLDEPTNHLD 462
Cdd:PRK14267 162 RALAMKPKILLMDEPTANID 181
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-230 |
2.06e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.41 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPA----DWRIAHMRQEvdtl 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditDWQTAKIMRE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 drlAVDYVLDGdsrlREIqaalavaeaahdgsaLARLHTELDNA-DGYTAD--------ARARKLLAGLgfsSEQMERRV 147
Cdd:PRK11614 81 ---AVAIVPEG----RRV---------------FSRMTVEENLAmGGFFAErdqfqeriKWVYELFPRL---HERRIQRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 148 GDFSGGWRMRLNLAQALMCPSDLLLLDEPTnhLDLDAILWLE-----EWLKGYPGTLVLISHDRDFLDAVVDHVVHLENR 222
Cdd:PRK11614 136 GTMSGGEQQMLAIGRALMSQPRLLLLDEPS--LGLAPIIIQQifdtiEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
....*...
gi 15600445 223 KLTLYRGG 230
Cdd:PRK11614 214 HVVLEDTG 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-176 |
2.09e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 46.38 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMrqEVDTLDRLAV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-DGQDITKL--PMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVldgdsrlreiqaalavaeaAHDGSALARLhTELDNAD------GYTADARARKLLAGLG-FSSEQMERRVGDF-SGG 153
Cdd:cd03218 78 GYL-------------------PQEASIFRKL-TVEENILavleirGLSKKEREEKLEELLEeFHITHLRKSKASSlSGG 137
|
170 180
....*....|....*....|...
gi 15600445 154 WRMRLNLAQALMCPSDLLLLDEP 176
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-204 |
2.32e-05 |
|
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: 45.92 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 16 LLEAAELTLHAGQKAGLIGANGAGKSSLFALLR-------GQLGQDaGDCLLPADWRIAHMRQEVdtldrLAVDYVLDGD 88
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLD-GKPISQYEHKYLHSKVSL-----VGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 89 SRLREIQAalavaeaahdGSALARLHTELDNADGYTADARARKLlaGLGFSSEQMERRvGDFSGGWRMRLNLAQALMCPS 168
Cdd:cd03248 103 SLQDNIAY----------GLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNP 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600445 169 DLLLLDEPTNHLDLDAILWLEEWLKGYPG--TLVLISH 204
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-182 |
2.36e-05 |
|
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: 47.43 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 16 LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP----ADWRIAHMRQEVDTL-------DRLAVDYV 84
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTLRQFINYLpqepyifSGSILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 85 LDGDSRLREIQAALAVAEaahdgsaLARLHTELDNADgytadararkllagLGFSSEQMERRvGDFSGGWRMRLNLAQAL 164
Cdd:TIGR01193 569 LLGAKENVSQDEIWAACE-------IAEIKDDIENMP--------------LGYQTELSEEG-SSISGGQKQRIALARAL 626
|
170
....*....|....*...
gi 15600445 165 MCPSDLLLLDEPTNHLDL 182
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDT 644
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-227 |
2.47e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 46.23 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwRIaHMRQEVDTLdrLAVdyvldgdsrlreiqaalava 101
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG--------RV-EVNGRVSAL--LEL-------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 102 eaahdGSAlarLHTEL---DNAdgytadararkLLAG--LGFSSEQMERRV---------GDF--------SGGWRMRLN 159
Cdd:COG1134 96 -----GAG---FHPELtgrENI-----------YLNGrlLGLSRKEIDEKFdeivefaelGDFidqpvktySSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 160 LAQALMCPSDLLLLDEptnhldldaIL-------------WLEEwLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTL 226
Cdd:COG1134 157 FAVATAVDPDILLVDE---------VLavgdaafqkkclaRIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
.
gi 15600445 227 Y 227
Cdd:COG1134 227 D 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
2.52e-05 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 44.73 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwRIAHMRQEVDTLDRlav 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG--------EILVDGKEVSFASP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 dyvldgdsrlreiqaalavaeaahdgsalarlhteldnadgytADARArkllAGLGFSSeQMerrvgdfSGGWRMRLNLA 161
Cdd:cd03216 70 -------------------------------------------RDARR----AGIAMVY-QL-------SVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLDAILWLEEWLK-----GypGTLVLISHDRDFLDAVVDHVV 217
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRrlraqG--VAVIFISHRLDEVFEIADRVT 153
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
125-229 |
2.68e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.62 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD---LDAILWLEEWLKGYPGTLVL 201
Cdd:PRK13651 141 AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIIL 220
|
90 100
....*....|....*....|....*...
gi 15600445 202 ISHDrdfldavVDHVVHLENRKLTLYRG 229
Cdd:PRK13651 221 VTHD-------LDNVLEWTKRTIFFKDG 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-222 |
2.79e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 45.55 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDA---GDCLL---------PADWRIAH 68
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLngrrltalpAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 69 MRQEV------DTLDRLAVDyvLDGDSRLREIQaalavaeaahdgsalARLHTELDNADgytadararklLAGLGfsseq 142
Cdd:COG4136 81 LFQDDllfphlSVGENLAFA--LPPTIGRAQRR---------------ARVEQALEEAG-----------LAGFA----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 143 mERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWL------KGYPgtLVLISHDRDflDA-VVDH 215
Cdd:COG4136 128 -DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVfeqirqRGIP--ALLVTHDEE--DApAAGR 202
|
....*..
gi 15600445 216 VVHLENR 222
Cdd:COG4136 203 VLDLGNW 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-224 |
3.04e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.13 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEV-DTLDRLAVDYV 84
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVaRRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 85 LDGDSRLREIqaaLAVAEAAHDgSALARLHTEldNADGYTADARARKLlaglgfsSEQMERRVGDFSGGWRMRLNLAQAL 164
Cdd:PRK10253 92 TPGDITVQEL---VARGRYPHQ-PLFTRWRKE--DEEAVTKAMQATGI-------THLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600445 165 MCPSDLLLLDEPTNHLDLDAILWLEEWL------KGYpgTLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLselnreKGY--TLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-181 |
3.32e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.85 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwRIahmrqevdTLDRLA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHG--------SI--------TLDGKP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 81 VDyvldGDSRLREIQAALAVAEAAHDGSALARLHTELDNADGYTADARARKLLAGLGFSSEQmERRVGDFSGGWRMRLNL 160
Cdd:PRK11248 65 VE----GPGAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGI 139
|
170 180
....*....|....*....|.
gi 15600445 161 AQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALD 160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-503 |
3.33e-05 |
|
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: 47.21 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLaigyfaqhqldSLDPQASpllhlqRIAPGer 406
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-----------SFSPQTS------WIMPG-- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 407 eqTLKD---FLGGFD-FRGVRV----------------DEPVL-----NFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:TIGR01271 502 --TIKDniiFGLSYDeYRYTSVikacqleedialfpekDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 462 DL----EMRLALTMALQEFSGAVLVVSHDRHLLKSttDEFLLVADG 503
Cdd:TIGR01271 580 DVvtekEIFESCLCKLMSNKTRILVTSKLEHLKKA--DKILLLHEG 623
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-185 |
3.83e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqlgqdagdCLLPADWRIAHMRQEVDTLD-RLAVDYV 84
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG--------LLPPAAGTIKLDGGDIDDPDvAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 85 LDGDsrlreiqaalavaeaahdgsALARLHTELDN----------ADGYTADARARKLLAGLGfsseqmERRVGDFSGGW 154
Cdd:PRK13539 79 GHRN--------------------AMKPALTVAENlefwaaflggEELDIAAALEAVGLAPLA------HLPFGYLSAGQ 132
|
170 180 190
....*....|....*....|....*....|.
gi 15600445 155 RMRLNLAQALMCPSDLLLLDEPTNHLDLDAI 185
Cdd:PRK13539 133 KRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
343-509 |
4.08e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 343 LLGPNGAGKSTLIK------------TLAGDLPELGG-------RLLRGENLAIGYFAQHQL--DSLDPQ-ASPLLHLqr 400
Cdd:PRK13645 42 VIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANlkkikevKRLRKEIGLVFQFPEYQLfqETIEKDiAFGPVNL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 iapGEREQ----TLKDFLGGFDFRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE-----MRLALTM 471
Cdd:PRK13645 120 ---GENKQeaykKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKgeedfINLFERL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600445 472 AlQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV----PFD 509
Cdd:PRK13645 197 N-KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsigsPFE 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-504 |
4.83e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAvLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPE--------LGGRLLRGENL----AIGYFAQHQLDSLDP 390
Cdd:PRK13549 17 GVKA-LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtyegeiiFEGEELQASNIrdteRAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 391 QASPLLHL---QRIAPG---------EREQTLKDFLGgfdfRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPT 458
Cdd:PRK13549 96 ELSVLENIflgNEITPGgimdydamyLRAQKLLAQLK----LDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600445 459 NHL---DLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGR 504
Cdd:PRK13549 172 ASLtesETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-205 |
4.96e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 45.22 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 26 AGQKAGLIGANGAGKSSLFA----LLRGQ-----LGQDAGDCLLPAdwrIAHMR----QEVDTLDRLAVDYVLDgdsrlr 92
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLArmagLLPGQgeillNGRPLSDWSAAE---LARHRaylsQQQSPPFAMPVFQYLA------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 93 eiqaalavaeaahdgsalarLHTElDNADGYTADARARKLLAGLGFsSEQMERRVGDFSGGWRMRLNLAQALM--CPSD- 169
Cdd:COG4138 92 --------------------LHQP-AGASSEAVEQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLqvWPTIn 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 170 ----LLLLDEPTNHLD------LDAilWLEEwLKGYPGTLVLISHD 205
Cdd:COG4138 150 pegqLLLLDEPMNSLDvaqqaaLDR--LLRE-LCQQGITVVMSSHD 192
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
322-505 |
5.40e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVlEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAIGYFAQHQLDSLDPQASPLLHLQR 400
Cdd:TIGR01257 941 SGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTvLVGGKDIETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 401 IAPG-----------------EREQTLKDflGGFDFRGvrvDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDL 463
Cdd:TIGR01257 1020 VAEHilfyaqlkgrsweeaqlEMEAMLED--TGLHHKR---NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600445 464 EMRLAL-TMALQEFSGAVLVVS-HDRHLLKSTTDEFLLVADGRV 505
Cdd:TIGR01257 1095 YSRRSIwDLLLKYRSGRTIIMStHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
143-224 |
5.72e-05 |
|
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: 45.02 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 143 MERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDL----DAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVH 218
Cdd:cd03299 123 LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
....*.
gi 15600445 219 LENRKL 224
Cdd:cd03299 203 MLNGKL 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-181 |
5.83e-05 |
|
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: 46.25 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLP----ADWRIAHMRQEVDTLDRlavDYVLDGDSRLR 92
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASLRRQVALVSQ---DVVLFNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 93 EIQAALAvaeaahDGSALARLHTELdnadgytADARARKLLAGL--GFSSEqmerrVGD----FSGGWRMRLNLAQALMC 166
Cdd:TIGR02203 425 NIAYGRT------EQADRAEIERAL-------AAAYAQDFVDKLplGLDTP-----IGEngvlLSGGQRQRLAIARALLK 486
|
170
....*....|....*
gi 15600445 167 PSDLLLLDEPTNHLD 181
Cdd:TIGR02203 487 DAPILILDEATSALD 501
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
126-224 |
5.86e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 44.98 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 126 DARARKLLAGLGFSSEQ-MERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKgypG 197
Cdd:cd03295 111 RERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpitrdqlQEEFKRLQQELG---K 187
|
90 100
....*....|....*....|....*..
gi 15600445 198 TLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:cd03295 188 TIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
125-224 |
5.97e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.21 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG---TLVL 201
Cdd:PRK13641 121 AKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVIL 200
|
90 100
....*....|....*....|...
gi 15600445 202 ISHDRDFLDAVVDHVVHLENRKL 224
Cdd:PRK13641 201 VTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
432-506 |
7.29e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 432 SGGEKARLALALIAWQKPNLLLLDEPTNHLDLE-----MRLALTMALQefSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgehemMQLILDAKAN--NKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
125-226 |
7.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.12 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDA---ILWLEEWLKGYPGTLVL 201
Cdd:PRK13649 121 AEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGrkeLMTLFKKLHQSGMTIVL 200
|
90 100
....*....|....*....|....*
gi 15600445 202 ISHDRDFLDAVVDHVVHLENRKLTL 226
Cdd:PRK13649 201 VTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-220 |
1.03e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.72 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 15 RLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCllpadwRIAhmrqevdtldrlavDYVLDGDSRLREI 94
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVG--------------DIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 95 QAALAVAEAAHD--GSALARLHTELDNADG--------YTADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQAL 164
Cdd:PRK13643 80 KPVRKKVGVVFQfpESQLFEETVLKDVAFGpqnfgipkEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 165 MCPSDLLLLDEPTNHLDLDA---ILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLE 220
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-224 |
1.11e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQrGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqlgqdagdcLLPADWRiahmrqevdtldRLAV 81
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALG---------ILPAGVR------------QTAG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDGD----SRLREIQAALAVAEAAhdgSALARLHTELDNA-------DGYTADARARKLLAGLGFSSEQMERRVGDF 150
Cdd:PRK10418 63 RVLLDGKpvapCALRGRKIATIMQNPR---SAFNPLHTMHTHAretclalGKPADDATLTAALEAVGLENAARVLKLYPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 151 --SGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDA---ILWLEEWL--KGYPGTLvLISHDRDFLDAVVDHVVHLENRK 223
Cdd:PRK10418 140 emSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqarILDLLESIvqKRALGML-LVTHDMGVVARLADDVAVMSHGR 218
|
.
gi 15600445 224 L 224
Cdd:PRK10418 219 I 219
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
561-638 |
1.11e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 561 KREADKLERELGGLHEKLAAIEARLGDS--ALYDVSRKDELRELLSEQSSLKVREGELEERWLEALETLEALQKELEASE 638
Cdd:COG1579 51 KTELEDLEKEIKRLELEIEEVEARIKKYeeQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-458 |
1.17e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 322 YGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGE-----------NLAIGYFAQH-QL-DS 387
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPDSGEILIDGKpvrirsprdaiALGIGMVHQHfMLvPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 388 L----------DPQASPLLHLQRIApgereQTLKDFLGGFDFRgVRVDEPVLNFSGGEKARL----ALaliaWQKPNLLL 453
Cdd:COG3845 95 LtvaenivlglEPTKGGRLDRKAAR-----ARIRELSERYGLD-VDPDAKVEDLSVGEQQRVeilkAL----YRGARILI 164
|
....*
gi 15600445 454 LDEPT 458
Cdd:COG3845 165 LDEPT 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
328-509 |
1.26e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.43 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLAIGYfAQHQLDSLDPQASPLLHLQRIAPGEr 406
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGTITIAGYHITPET-GNKNLKKLRKKVSLVFQFPEAQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 407 EQTLKDFLGG---FDF-------------RGVRVDEPVLN-----FSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEM 465
Cdd:PRK13641 101 NTVLKDVEFGpknFGFsedeakekalkwlKKVGLSEDLISkspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600445 466 RLALTMALQEFSGA---VLVVSHDRHLLKSTTDEFLLVADGRVVPFD 509
Cdd:PRK13641 181 RKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHA 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-177 |
1.35e-04 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 43.58 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRQEvdTLDRLAVDYVLDGdsrlREIqaalava 101
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDITGLPPH--ERARAGIGYVPEG----RRI------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 102 eaahdgsaLARLhTELDN---ADGYTADARARKLLAGLgFS-----SEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLL 173
Cdd:cd03224 87 --------FPEL-TVEENlllGAYARRRAKRKARLERV-YElfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
....
gi 15600445 174 DEPT 177
Cdd:cd03224 157 DEPS 160
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-229 |
1.37e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.31 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLF-ALLR------GQ---LGQDAGDcLLPADWRiaHMRQEVDTL--DRLAVdyvLDGDS 89
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFArAIIGlvkatdGEvawLGKDLLG-MKDDEWR--AVRSDIQMIfqDPLAS---LNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 90 RLREIQaalavaeaahdGSALARLHTELDNADgytADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSD 169
Cdd:PRK15079 116 TIGEII-----------AEPLRTYHPKLSRQE---VKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600445 170 LLLLDEPTNHLDLD----AILWLEEWLKGYPGTLVLISHDRdfldAVVDHVvhlENRKLTLYRG 229
Cdd:PRK15079 182 LIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHDL----AVVKHI---SDRVLVMYLG 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
311-369 |
1.48e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 311 PLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRL 369
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL 68
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
123-234 |
1.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.46 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 123 YTADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-----------LDAilwleew 191
Cdd:PRK13631 150 SEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehemmqliLDA------- 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15600445 192 lKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLYRGGYSAF 234
Cdd:PRK13631 223 -KANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
327-503 |
1.51e-04 |
|
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: 44.08 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 327 VLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGENLaigyfaqhqldSLDPQASpllhlqRIAPGer 406
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-----------SFSSQFS------WIMPG-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 407 eqTLKD-FLGGFDFRGVR------------------------VDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:cd03291 113 --TIKEnIIFGVSYDEYRyksvvkacqleeditkfpekdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 462 DL----EMRLALTMALQEFSGAVLVVSHDRHLLKSttDEFLLVADG 503
Cdd:cd03291 191 DVftekEIFESCVCKLMANKTRILVTSKMEHLKKA--DKILILHEG 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.93e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 43.64 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQ-RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwriahmRQEVDTldrl 79
Cdd:PRK13652 3 LIETRDLCYSySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI---------RGEPIT---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 80 avdyvldgDSRLREIQAALAVAEAAHDGSALARLhTELDNA--------DGYTADARARKLLAGLGFSsEQMERRVGDFS 151
Cdd:PRK13652 70 --------KENIREVRKFVGLVFQNPDDQIFSPT-VEQDIAfgpinlglDEETVAHRVSSALHMLGLE-ELRDRVPHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 152 GGWRMRLNLAQALMCPSDLLLLDEPTNHLD----LDAILWLEEWLKGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTLY 227
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
276-355 |
2.24e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 44.32 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 276 AQSRIKALerLEElAPAHVDSpfnfsfRESDKISRPLLDLGEGRLGY--GDKAVLEKVKLQLVPGARIGLLGPNGAGKST 353
Cdd:PRK10789 286 AYSRIRAM--LAE-APVVKDG------SEPVPEGRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKST 356
|
..
gi 15600445 354 LI 355
Cdd:PRK10789 357 LL 358
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
328-506 |
2.27e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG--------------DLPELGGRLLRGENLAIGYFAQHQLDSLDPQAS 393
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiheptkgtitinniNYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 PLL--HLQRIAPG----------EREQTLKDFLGgfdfRGVRVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHL 461
Cdd:PRK09700 101 LYIgrHLTKKVCGvniidwremrVRAAMMLLRVG----LKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 462 ---DLEMRLALTMALQEFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK09700 177 tnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-182 |
2.40e-04 |
|
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: 44.52 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPqrLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLgqdagdclLPADWRIAHMrqevdtlDRLA----V 81
Cdd:TIGR01271 433 NFSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL--------EPSEGKIKHS-------GRISfspqT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDGDSRlreiqaalavaeaahDGSALARLHTELDnadgYTADARARKLLAGLGFSSEQMERRVGD----FSGGWRMR 157
Cdd:TIGR01271 496 SWIMPGTIK---------------DNIIFGLSYDEYR----YTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRAR 556
|
170 180
....*....|....*....|....*
gi 15600445 158 LNLAQALMCPSDLLLLDEPTNHLDL 182
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
427-491 |
2.42e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 427 PVLNFSGGEKARLALA---LIAWQKPNLLLLDEPTNHL---DLEMRLALTMALQEFSGAVLVVSHDRHLLK 491
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVVK 876
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
148-224 |
2.55e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 148 GDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWL----KGYpgTLVLISHDRDFLDAVVDHVVHLENRK 223
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfelkKEY--TIVLVTHSPAQAARVSDYVAFLYLGK 225
|
.
gi 15600445 224 L 224
Cdd:PRK14267 226 L 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-458 |
2.93e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.85 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 12 GPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWR---IAHMRQEVDTLDRL 79
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrsPRDAQaagIAIIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 80 AVdyvldgdsrlRE-IqaalavaeaahdgsALARLHTELDNADGYTADARARKLLAGLGFsSEQMERRVGDFSGGWRMRL 158
Cdd:COG1129 95 SV----------AEnI--------------FLGREPRRGGLIDWRAMRRRARELLARLGL-DIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAIlwleEWL---------KGypGTLVLISHdrdFLD---AVVDHVvhlenrklTL 226
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREV----ERLfriirrlkaQG--VAIIYISH---RLDevfEIADRV--------TV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 227 YRGGysafertraerlaqqqqayekqqaqrahmeSFIARFKAKATKARQAqsrIKAL--ERLEELAPahvdspfnfsfRE 304
Cdd:COG1129 213 LRDG------------------------------RLVGTGPVAELTEDEL---VRLMvgRELEDLFP-----------KR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 305 SDKISRPLLDLGegrlGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGR-LLRGENLAIGyfaqh 383
Cdd:COG1129 249 AAAPGEVVLEVE----GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEiRLDGKPVRIR----- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 qldslDPQAS--------P-------------------LLHLQRIAPG-------EREQTlKDFLGGFDFRGVRVDEPVL 429
Cdd:COG1129 320 -----SPRDAiragiayvPedrkgeglvldlsirenitLASLDRLSRGglldrrrERALA-EEYIKRLRIKTPSPEQPVG 393
|
490 500 510
....*....|....*....|....*....|.
gi 15600445 430 NFSGG--EKARLALALIAwqKPNLLLLDEPT 458
Cdd:COG1129 394 NLSGGnqQKVVLAKWLAT--DPKVLILDEPT 422
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
323-509 |
3.00e-04 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 42.67 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 323 GDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDL-PELGGRLLRGENLA----------IGYFAQ------H-- 383
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGEIFIDGEDIReqdpvelrrkIGYVIQqiglfpHmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 384 --QLDSLDPQ------------ASPLLHLQRIAPGEreqtlkdflggfdFRGVRVDEpvlnFSGGEKAR--LALALIAwq 447
Cdd:cd03295 92 veENIALVPKllkwpkekirerADELLALVGLDPAE-------------FADRYPHE----LSGGQQQRvgVARALAA-- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 448 KPNLLLLDEPTNHLDLEMRLALT---MALQEFSGAVLV-VSHDrhllkstTDEFLLVAD-------GRVVPFD 509
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQeefKRLQQELGKTIVfVTHD-------IDEAFRLADriaimknGEIVQVG 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-224 |
3.27e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.73 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 141 EQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG--TLVLISHDRDFLDAVVDHVVH 218
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAF 224
|
....*.
gi 15600445 219 LENRKL 224
Cdd:PRK14246 225 LYNGEL 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-221 |
3.91e-04 |
|
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: 42.45 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 17 LEAAELTLHAGQKAGLIGANGAGKSSLFAL-------------LRGQLGQDAGD---------CLLPadWRIAhmRQEVd 74
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLisglaqptsggviLEGKQITEPGPdrmvvfqnySLLP--WLTV--RENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 75 tldRLAVDYVLDGDSRlreiqaalavaeaaHDGSALARLHTELdnadgytadararkllAGLGfssEQMERRVGDFSGGW 154
Cdd:TIGR01184 76 ---ALAVDRVLPDLSK--------------SERRAIVEEHIAL----------------VGLT---EAADKRPGQLSGGM 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600445 155 RMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWL----KGYPGTLVLISHDRDFLDAVVDHVVHLEN 221
Cdd:TIGR01184 120 KQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-237 |
4.15e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 13 PQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLlpADWRIAHMRQEVDTLDRLAVDYVLdgdsrlr 92
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQQAWIMNATVRGNIL------- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 93 eiqaalavaeaahdgsalarLHTELDNADgyTADA-RARKLLAGLGFSSEQMERRVGD----FSGGWRMRLNLAQALMCP 167
Cdd:PTZ00243 743 --------------------FFDEEDAAR--LADAvRVSQLEADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYAN 800
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 168 SDLLLLDEPTNHLDLD-AILWLEEWLKGYPG--TLVLISHDRDFLdAVVDHVVHLENRKLTlYRGGYSAFERT 237
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHvGERVVEECFLGALAgkTRVLATHQVHVV-PRADYVVALGDGRVE-FSGSSADFMRT 871
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-205 |
6.97e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.00 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDC----LLPADWRIAHMRQ----------------EVDTLDRLAV 81
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgYVPFKRRKEFARRigvvfgqrsqlwwdlpAIDSFRLLKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDgDSRLREiqaalavaeaahdgsALARLHTELDnadgytadararkllagLGfssEQMERRVGDFSGGWRMRLNLA 161
Cdd:COG4586 123 IYRIP-DAEYKK---------------RLDELVELLD-----------------LG---ELLDTPVRQLSLGQRMRCELA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 162 QALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY----PGTLVLISHD 205
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrerGTTILLTSHD 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-221 |
7.47e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.33 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 20 AELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAdwriahmrqevdtldrlaVDYVLDGDSRLREIQAALA 99
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------------------VDIAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 100 VAEaaHDGSALARLHTELDNAD------GYTADARARKLLAGLgfsseqmeRRVG----------DFSGGWRMRLNLAQA 163
Cdd:PRK10070 109 AMV--FQSFALMPHMTVLDNTAfgmelaGINAEERREKALDAL--------RQVGlenyahsypdELSGGMRQRVGLARA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 164 LMCPSDLLLLDEPTNHLD-LDAILWLEEWLK---GYPGTLVLISHDRDFLDAVVDHVVHLEN 221
Cdd:PRK10070 179 LAINPDILLMDEAFSALDpLIRTEMQDELVKlqaKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
319-534 |
7.60e-04 |
|
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: 42.36 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 319 RLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKS----TLIKTLAGDLPELGGR-LLRGENLA--------------IGY 379
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSiLFDGQDLLglserelrrirgnrIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 380 FAQHQLDSLDP------Q-ASPLLHLQRIAPGEREQTLKDFLggfdfRGVRVDEPV--LN-----FSGGEKAR--LALAL 443
Cdd:COG4172 97 IFQEPMTSLNPlhtigkQiAEVLRLHRGLSGAAARARALELL-----ERVGIPDPErrLDayphqLSGGQRQRvmIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 444 IAwqKPNLLLLDEPTNHLDLEMR---LALTMALQEFSG-AVLVVSHDRHLLKSTTDEFLLVADGRVVP-------FDGDL 512
Cdd:COG4172 172 AN--EPDLLIADEPTTALDVTVQaqiLDLLKDLQRELGmALLLITHDLGVVRRFADRVAVMRQGEIVEqgptaelFAAPQ 249
|
250 260
....*....|....*....|....
gi 15600445 513 DDYARWLVDY--RARKAPQAETAP 534
Cdd:COG4172 250 HPYTRKLLAAepRGDPRPVPPDAP 273
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-205 |
7.87e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 41.30 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 16 LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpadwrIAHMRQEVDTLDRLAVdyvldgdsRLREIQ 95
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL-----VGQPLHQMDEEARAKL--------RAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 96 AALAVAEAAHDGSAL------ARLHTELDNadgyTADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSD 169
Cdd:PRK10584 92 FVFQSFMLIPTLNALenvelpALLRGESSR----QSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600445 170 LLLLDEPTNHLDL---DAILWLEEWL-KGYPGTLVLISHD 205
Cdd:PRK10584 167 VLFADEPTGNLDRqtgDKIADLLFSLnREHGTTLILVTHD 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-224 |
8.48e-04 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 41.56 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMrqevdTLDRLAV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF-GGEDATDV-----PVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 DYVLDgdsrlreiqaalavaeaaHdgSALARLHTELDN-------------ADGYTADARARKLLAGLGFSSEQmERRVG 148
Cdd:cd03296 77 GFVFQ------------------H--YALFRHMTVFDNvafglrvkprserPPEAEIRAKVHELLKLVQLDWLA-DRYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 149 DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPG----TLVLISHDRDFLDAVVDHVVHLENRKL 224
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-204 |
9.79e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.40 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 11 RGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPAD-----------WRIAHMRQEVDTLDRL 79
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhRQVALVGQEPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 80 AVDYVLDGDSRLREIQAALAvaeaahdgSALARLHTELDN-ADGYTADararkllagLGFSSEQMerrvgdfSGGWRMRL 158
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAA--------AKAANAHDFIMEfPNGYDTE---------VGEKGSQL-------SGGQKQRI 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISH 204
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-181 |
9.97e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.11 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLT--LQRGPQRLleaaELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLL---------PADWRIAHM 69
Cdd:PRK10771 1 MLKLTDITwlYHHLPMRF----DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLngqdhtttpPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 70 RQEVDTLDRLAV--DYVLDGDSRLReiqaalavaeaahdgsalarlhteLDNADGYTADARARKLlaGLgfsSEQMERRV 147
Cdd:PRK10771 77 FQENNLFSHLTVaqNIGLGLNPGLK------------------------LNAAQREKLHAIARQM--GI---EDLLARLP 127
|
170 180 190
....*....|....*....|....*....|....
gi 15600445 148 GDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK10771 128 GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
125-181 |
1.02e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.54 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 125 ADARARKLLAGLGFSSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK13634 121 AKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
127-207 |
1.05e-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: 41.48 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 127 ARARKLLAGLGFssEQME-RRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKgypGT 198
Cdd:cd03294 139 ERAAEALELVGL--EGWEhKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQ---KT 213
|
....*....
gi 15600445 199 LVLISHDRD 207
Cdd:cd03294 214 IVFITHDLD 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
144-217 |
1.10e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 41.61 E-value: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600445 144 ERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKG----YPGTLVLISHDRDFLDAVVDHVV 217
Cdd:PRK10851 131 DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVV 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
417-492 |
1.33e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 417 FDFRGVRVD-------------EPVLNFSGGEKA------RLALALIAWQKPNLLLLDEPTNHLDLEMRLALT----MAL 473
Cdd:PRK01156 775 LDFDDIDVDqdfnitvsrggmvEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKdiieYSL 854
|
90 100
....*....|....*....|.
gi 15600445 474 QEFSG--AVLVVSHDRHLLKS 492
Cdd:PRK01156 855 KDSSDipQVIMISHHRELLSV 875
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-360 |
1.39e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15600445 323 GDKAvLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG 360
Cdd:PRK10762 16 GVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTG 52
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
323-373 |
1.52e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 1.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15600445 323 GDKAvLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGD-LPELGGRLLRGE 373
Cdd:PRK11288 16 GVKA-LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQ 66
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
432-506 |
1.55e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.92 E-value: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 432 SGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---LALTMALQ-EFSGAVLVVSHDRHLLKSTTDEFLLVADGRVV 506
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKrqvMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-181 |
1.68e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600445 125 ADARARKLLAGLGFSsEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:NF000106 121 ARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-182 |
1.70e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.58 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLPADWRIAHMRQEVDTLD--R 78
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDapR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 79 LA-VDYVLDGDSR------LREIqaaLAVAEAAHDGSALARLHTELDNADGYTADARARKLLAglgfsseqmeRRVGDFS 151
Cdd:PRK13547 81 LArLRAVLPQAAQpafafsAREI---VLLGRYPHARRAGALTHRDGEIAWQALALAGATALVG----------RDVTTLS 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600445 152 GGWRMRLNLAQAL---------MCPSDLLLLDEPTNHLDL 182
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
345-489 |
1.79e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.33 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 345 GPNGAGKSTLIK--TLAgdlpeLGGRLLR-GENLAIGYFAQHQLD----SLDPQASPLLHLQRIAPGEREQTLKD--FL- 414
Cdd:cd03279 35 GPTGAGKSTILDaiTYA-----LYGKTPRyGRQENLRSVFAPGEDtaevSFTFQLGGKKYRVERSRGLDYDQFTRivLLp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 415 -GGFDFRGVRvdePVLNFSGGE--KARLALAL----IAWQKPN----LLLLDEPTNHLDLEMRLALTMALQEFSG---AV 480
Cdd:cd03279 110 qGEFDRFLAR---PVSTLSGGEtfLASLSLALalseVLQNRGGarleALFIDEGFGTLDPEALEAVATALELIRTenrMV 186
|
....*....
gi 15600445 481 LVVSHDRHL 489
Cdd:cd03279 187 GVISHVEEL 195
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
295-490 |
2.04e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 295 DSPFNFSFRESDKISRPLLDLGEGRLGYGDKAVLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAGDLPELGGRLLRGEN 374
Cdd:pfam13304 95 EKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAAD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 375 LAIGYFAQHQLDSLDPQ-ASPLLHLQRIAPGEREQTLKDFL-----GGFDFRGVRVDEPVLNFSGGEKARLALALIAW-- 446
Cdd:pfam13304 175 LALFPDLKELLQRLVRGlKLADLNLSDLGEGIEKSLLVDDRlrergLILLENGGGGELPAFELSDGTKRLLALLAALLsa 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600445 447 -QKPNLLLLDEPTNHLDLEM--RLALTMALQEFSGA-VLVVSHDRHLL 490
Cdd:pfam13304 255 lPKGGLLLIDEPESGLHPKLlrRLLELLKELSRNGAqLILTTHSPLLL 302
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
125-207 |
2.11e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 40.85 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLA--GLGfssEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGY----PGT 198
Cdd:COG3842 112 IRARVAELLElvGLE---GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGIT 188
|
....*....
gi 15600445 199 LVLISHDRD 207
Cdd:COG3842 189 FIYVTHDQE 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
151-181 |
2.18e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 39.84 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|..
gi 15600445 151 SGGWRMRLNLAQAL-MCPSdLLLLDEPTNHLD 181
Cdd:cd03213 113 SGGERKRVSIALELvSNPS-LLFLDEPTSGLD 143
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-181 |
2.38e-03 |
|
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: 40.16 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 16 LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGqlgqdagdCLLPADWRIAHMRQEVDTLD----RLAVDYVLdgdsrl 91
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR--------FYVPENGRVLVDGHDLALADpawlRRQVGVVL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 92 reiQAALAVAEAAHDGSALARLHTELDNADGYTADARARKLLAGLGFSSEQM--ERRVGdFSGGWRMRLNLAQALMCPSD 169
Cdd:cd03252 83 ---QENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIvgEQGAG-LSGGQRQRIAIARALIHNPR 158
|
170
....*....|..
gi 15600445 170 LLLLDEPTNHLD 181
Cdd:cd03252 159 ILIFDEATSALD 170
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-224 |
2.44e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 1 MIRLLNLTLQ-RGPQRLLEA---AELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLlpadwriahmrqeVDTL 76
Cdd:PRK11153 1 MIELKNISKVfPQGGRTIHAlnnVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-------------VDGQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 77 DRLAVDyvlDGDSRL--REI----QaalavaeaaH----------DGSALArlhTELDNADGYTADARARKLLA--GLgf 138
Cdd:PRK11153 68 DLTALS---EKELRKarRQIgmifQ---------HfnllssrtvfDNVALP---LELAGTPKAEIKARVTELLElvGL-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 139 sSEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD---LDAILWLeewLKG----YPGTLVLISHDRDFLDA 211
Cdd:PRK11153 131 -SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSILEL---LKDinreLGLTIVLITHEMDVVKR 206
|
250
....*....|...
gi 15600445 212 VVDHVVHLENRKL 224
Cdd:PRK11153 207 ICDRVAVIDAGRL 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
423-503 |
3.32e-03 |
|
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: 39.62 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 423 RVDEPVLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLE-----MRLALTMALQEFSGAVLVVSHDRHLLkSTTDEF 497
Cdd:cd03290 133 EIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL-PHADWI 211
|
....*.
gi 15600445 498 LLVADG 503
Cdd:cd03290 212 IAMKDG 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
125-221 |
3.48e-03 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 39.59 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 125 ADARARKLLA--GLgfsSEQMERRVGDFSGGWRMRLNLAQAL-MCPsDLLLLDEPTNHLD-------LDAILWL-EEwlk 193
Cdd:COG1126 113 AEERAMELLErvGL---ADKADAYPAQLSGGQQQRVAIARALaMEP-KVMLFDEPTSALDpelvgevLDVMRDLaKE--- 185
|
90 100
....*....|....*....|....*....
gi 15600445 194 gypG-TLVLISHDRDFLDAVVDHVVHLEN 221
Cdd:COG1126 186 ---GmTMVVVTHEMGFAREVADRVVFMDG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-181 |
3.51e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.52 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 6 NLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGdcllpadwriahmrqevdtldrlAVDYvl 85
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAG-----------------------EVHY-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 86 dgdsRLREIQAALAVAEAAHDGSALARlhTEL-----DNADGY----TADARARKLLAGLGF---------SSEQMER-- 145
Cdd:PRK11701 66 ----RMRDGQLRDLYALSEAERRRLLR--TEWgfvhqHPRDGLrmqvSAGGNIGERLMAVGArhygdiratAGDWLERve 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600445 146 ----RVGD----FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:PRK11701 140 idaaRIDDlpttFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
561-635 |
3.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 561 KREADKLERELGGLHEKLAAIEARLGDSAlydvSRKDELRELLSEQSSLKVREGELEErWLEALETLEALQKELE 635
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELE 375
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
151-221 |
3.68e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 38.99 E-value: 3.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600445 151 SGGWRMRLNLAQALMCPSDLLLLDEP--------TNHLDLDAIlwLEEWLKGypGTLVLISHDRDFLDAvVDHVVHLEN 221
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRHIFENCI--LGLLLNN--KTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-177 |
3.81e-03 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 39.20 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 22 LTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpADWRIAHMRqeVDTLDRLAVDYVLDGdsrlREIqaalava 101
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF-DGEDITGLP--PHRIARLGIGYVPEG----RRI------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 102 eaahdgsaLARLhTELDN---AdgytadARARKLLAGLGFSSEQM--------ERR---VGDFSGGWRMRLNLAQALMCP 167
Cdd:COG0410 90 --------FPSL-TVEENlllG------AYARRDRAEVRADLERVyelfprlkERRrqrAGTLSGGEQQMLAIGRALMSR 154
|
170
....*....|
gi 15600445 168 SDLLLLDEPT 177
Cdd:COG0410 155 PKLLLLDEPS 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-239 |
4.46e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 40.31 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQRLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDcllpadwriAHMRQEVDTLDRLAV 81
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH---------VHMKGSVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 82 dyvLDGDSrLREIQAAlavaeaahdGSALarlhteldNADGYTADARARKLLAGL-----GFSSEQMERRVgDFSGGWRM 156
Cdd:TIGR00957 710 ---IQNDS-LRENILF---------GKAL--------NEKYYQQVLEACALLPDLeilpsGDRTEIGEKGV-NLSGGQKQ 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 157 RLNLAQALMCPSDLLLLDEPTNHLD-------LDAILWLEEWLKGypGTLVLISHDRDFLDAvVDHVVHLENRKLT---- 225
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYLPQ-VDVIIVMSGGKISemgs 844
|
250
....*....|....*....
gi 15600445 226 ----LYR-GGYSAFERTRA 239
Cdd:TIGR00957 845 yqelLQRdGAFAEFLRTYA 863
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
343-509 |
5.04e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.18 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 343 LLGPNGAGKSTLIKTLAG-------------------------DLPELGgrlLRGENlAIGYFAQHQLDSLDPQASPLLH 397
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLllqsnfiylpaersgparlypslvrELSDLG---SRGEY-TADFLAELENLEILDDKSKELL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 398 ------LQRIAPGEREQTLKDFLGGFDFRgvrvdepvlNFSGGEKARLALA--------------LIAWQKPNLLLLDEP 457
Cdd:COG4938 101 eqveewLEKIFPGKVEVDASSDLVRLVFR---------PSGNGKRIPLSNVgsgvsellpillalLSAAKPGSLLIIEEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600445 458 TNHLDLEMRLALTMALQEFSGA---VLVVSHDRHLLKSTTdefLLVADGRVVPFD 509
Cdd:COG4938 172 EAHLHPKAQSALAELLAELANSgvqVIIETHSDYILNGLR---NLIKEGKLLDPD 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
136-226 |
5.21e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 39.26 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 136 LGFSSEQMERRVG-------------------DFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD---LDAILWLEEWL- 192
Cdd:PRK13637 112 LGLSEEEIENRVKramnivgldyedykdkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKIKELh 191
|
90 100 110
....*....|....*....|....*....|....
gi 15600445 193 KGYPGTLVLISHDRDFLDAVVDHVVHLENRKLTL 226
Cdd:PRK13637 192 KEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
331-516 |
5.32e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 331 VKLQLVPGARIGLLGPNGAGKSTLIKTLAG-DLPELGGRLLRGENLAIG----------------YFAQHQLDSLDPQAS 393
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQSGEILLDGKPVTAEqpedyrklfsavftdfHLFDQLLGPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 394 PLLH---LQRIAPGEReqtlkdflggFDFRGVRVDEpvLNFSGGEKARLALALIAWQKPNLLLLDEPTNHLDLEMR---- 466
Cdd:PRK10522 422 PALVekwLERLKMAHK----------LELEDGRISN--LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRrefy 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600445 467 LALTMALQEFSGAVLVVSHDRHLLKStTDEFLLVADGRVVPFDGDLDDYA 516
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELTGEERDAA 538
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
323-360 |
6.10e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 6.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15600445 323 GDKAvLEKVKLQLVPGARIGLLGPNGAGKSTLIKTLAG 360
Cdd:PRK10982 10 GVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG 46
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-221 |
6.12e-03 |
|
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: 37.90 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 2 IRLLNLTLQRGPQR-LLEAAELTLHAGQKAGLIGANGAGKSSLFALLRG--QLGQdaGDCLLPADWRIAHMRQEvdtldr 78
Cdd:cd03223 1 IELENLSLATPDGRvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwPWGS--GRIGMPEGEDLLFLPQR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 79 lavDYVLDGdsRLREiqaalavaeaahdgsALArlhteldnadgYTADARarkllaglgfsseqmerrvgdFSGGWRMRL 158
Cdd:cd03223 73 ---PYLPLG--TLRE---------------QLI-----------YPWDDV---------------------LSGGEQQRL 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600445 159 NLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLKGYPGTLVLISHdRDFLDAVVDHVVHLEN 221
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
328-492 |
6.58e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.07 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 328 LEKVKLQLVPGARIGLLGPNGAGKSTLIKTL---AGDLPELGGRLLRGENLAIgyfaqhQLDSLdpqaspllhlqriapg 404
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGlyaSGKARLISFLPKFSRNKLI------FIDQL---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 405 ereQTLKDFLGGFdfrgVRVDEPVLNFSGGEKARLALA--LIAWQKPNLLLLDEPTNHLDLEMRLALTMALQEF---SGA 479
Cdd:cd03238 69 ---QFLIDVGLGY----LTLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLidlGNT 141
|
170
....*....|...
gi 15600445 480 VLVVSHDRHLLKS 492
Cdd:cd03238 142 VILIEHNLDVLSS 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-180 |
6.78e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.51 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 15 RLLEAAELTLHAGQKAGLIGANGAGKSSLFALLRGQLGQDAGDCLLpaDWRIAHMRQEVDTLDR-LAVDYvldgdsrlRE 93
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI--DGQEMRFASTTAALAAgVAIIY--------QE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 94 IQAALAVAEAahDGSALARLHTELDNADGYTADARARKLLAGLGFSSEQmERRVGDFSGGWRMRLNLAQALMCPSDLLLL 173
Cdd:PRK11288 88 LHLVPEMTVA--ENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDP-DTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
....*..
gi 15600445 174 DEPTNHL 180
Cdd:PRK11288 165 DEPTSSL 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
429-489 |
7.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 429 LNF-SGGEKA------RLALALIAWQKPNLLLLDEPTNHLDLEMRLAL----TMALQEFSgAVLVVSHDRHL 489
Cdd:PRK03918 786 LTFlSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRKIP-QVIIVSHDEEL 856
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
150-181 |
8.21e-03 |
|
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: 38.01 E-value: 8.21e-03
10 20 30
....*....|....*....|....*....|..
gi 15600445 150 FSGGWRMRLNLAQALMCPSDLLLLDEPTNHLD 181
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
140-205 |
9.13e-03 |
|
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: 38.37 E-value: 9.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600445 140 SEQMERRVGDFSGGWRMRLNLAQALMCPSDLLLLDEPTNHLDLDAILWLEEWLK------GYpgTLVLISHD 205
Cdd:cd03300 121 EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKrlqkelGI--TFVFVTHD 190
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-210 |
9.55e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 37.69 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600445 135 GLGFSSeqMERRVGDFSGGWRMRLNLAQALMCPSD--LLLLDEPTNHLDLDAILWLEEWLKGY---PGTLVLISHDRDFL 209
Cdd:cd03238 75 GLGYLT--LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
.
gi 15600445 210 D 210
Cdd:cd03238 153 S 153
|
|
| |
